Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities

Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Wu, Yamei [verfasserIn] Xiang, Huan [verfasserIn] Chen, Shengjun [verfasserIn] Zhao, Yongqiang [verfasserIn] Cai, Qiuxing [verfasserIn] Lin, Wanling [verfasserIn] Wu, Yanyan [verfasserIn] Wang, Yueqi [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Emulsifying properties Gelation Structural properties Functional properties

Übergeordnetes Werk:	Enthalten in: LWT - food science and technology - Amsterdam [u.a.] : Elsevier, 1993, 189
Übergeordnetes Werk:	volume:189

DOI / URN:	10.1016/j.lwt.2023.115483

Katalog-ID:	ELV065888960

Internformat


LEADER	01000caa a22002652 4500
001	ELV065888960
003	DE-627
005	20240105093219.0
007	cr uuu---uuuuu
008	231130s2023 xx \|\|\|\|\|o 00\| \|\|eng c
024	7		\|a 10.1016/j.lwt.2023.115483 \|2 doi
035			\|a (DE-627)ELV065888960
035			\|a (ELSEVIER)S0023-6438(23)01062-9
040			\|a DE-627 \|b ger \|c DE-627 \|e rda
041			\|a eng
082	0	4	\|a 660 \|q VZ
084			\|a 48.00 \|2 bkl
084			\|a 58.34 \|2 bkl
100	1		\|a Wu, Yamei \|e verfasserin \|4 aut
245	1	0	\|a Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities
264		1	\|c 2023
336			\|a nicht spezifiziert \|b zzz \|2 rdacontent
337			\|a Computermedien \|b c \|2 rdamedia
338			\|a Online-Ressource \|b cr \|2 rdacarrier
520			\|a Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products.
650		4	\|a Emulsifying properties
650		4	\|a Gelation
650		4	\|a Structural properties
650		4	\|a Functional properties
700	1		\|a Xiang, Huan \|e verfasserin \|4 aut
700	1		\|a Chen, Shengjun \|e verfasserin \|4 aut
700	1		\|a Zhao, Yongqiang \|e verfasserin \|4 aut
700	1		\|a Cai, Qiuxing \|e verfasserin \|4 aut
700	1		\|a Lin, Wanling \|e verfasserin \|4 aut
700	1		\|a Wu, Yanyan \|e verfasserin \|4 aut
700	1		\|a Wang, Yueqi \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t LWT - food science and technology \|d Amsterdam [u.a.] : Elsevier, 1993 \|g 189 \|h Online-Ressource \|w (DE-627)266892248 \|w (DE-600)1469139-5 \|w (DE-576)103373179 \|7 nnns
773	1	8	\|g volume:189
912			\|a GBV_USEFLAG_U
912			\|a GBV_ELV
912			\|a SYSFLAG_U
912			\|a SSG-OPC-FOR
912			\|a GBV_ILN_20
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_95
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
936	b	k	\|a 48.00 \|j Land- und Forstwirtschaft: Allgemeines \|q VZ
936	b	k	\|a 58.34 \|j Lebensmitteltechnologie \|q VZ
951			\|a AR
952			\|d 189

Indexfelder

author_variant	y w yw h x hx s c sc y z yz q c qc w l wl y w yw y w yw
matchkey_str	wuyameixianghuanchenshengjunzhaoyongqian:2023----:hrceiainfhageaineairfebsltoarxaoiumoirlapoenmdaebdfeetoisrntsrti
hierarchy_sort_str	2023
bklnumber	48.00 58.34
publishDate	2023
allfields	10.1016/j.lwt.2023.115483 doi (DE-627)ELV065888960 (ELSEVIER)S0023-6438(23)01062-9 DE-627 ger DE-627 rda eng 660 VZ 48.00 bkl 58.34 bkl Wu, Yamei verfasserin aut Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products. Emulsifying properties Gelation Structural properties Functional properties Xiang, Huan verfasserin aut Chen, Shengjun verfasserin aut Zhao, Yongqiang verfasserin aut Cai, Qiuxing verfasserin aut Lin, Wanling verfasserin aut Wu, Yanyan verfasserin aut Wang, Yueqi verfasserin aut Enthalten in LWT - food science and technology Amsterdam [u.a.] : Elsevier, 1993 189 Online-Ressource (DE-627)266892248 (DE-600)1469139-5 (DE-576)103373179 nnns volume:189 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-FOR GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 48.00 Land- und Forstwirtschaft: Allgemeines VZ 58.34 Lebensmitteltechnologie VZ AR 189
spelling	10.1016/j.lwt.2023.115483 doi (DE-627)ELV065888960 (ELSEVIER)S0023-6438(23)01062-9 DE-627 ger DE-627 rda eng 660 VZ 48.00 bkl 58.34 bkl Wu, Yamei verfasserin aut Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products. Emulsifying properties Gelation Structural properties Functional properties Xiang, Huan verfasserin aut Chen, Shengjun verfasserin aut Zhao, Yongqiang verfasserin aut Cai, Qiuxing verfasserin aut Lin, Wanling verfasserin aut Wu, Yanyan verfasserin aut Wang, Yueqi verfasserin aut Enthalten in LWT - food science and technology Amsterdam [u.a.] : Elsevier, 1993 189 Online-Ressource (DE-627)266892248 (DE-600)1469139-5 (DE-576)103373179 nnns volume:189 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-FOR GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 48.00 Land- und Forstwirtschaft: Allgemeines VZ 58.34 Lebensmitteltechnologie VZ AR 189
allfields_unstemmed	10.1016/j.lwt.2023.115483 doi (DE-627)ELV065888960 (ELSEVIER)S0023-6438(23)01062-9 DE-627 ger DE-627 rda eng 660 VZ 48.00 bkl 58.34 bkl Wu, Yamei verfasserin aut Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products. Emulsifying properties Gelation Structural properties Functional properties Xiang, Huan verfasserin aut Chen, Shengjun verfasserin aut Zhao, Yongqiang verfasserin aut Cai, Qiuxing verfasserin aut Lin, Wanling verfasserin aut Wu, Yanyan verfasserin aut Wang, Yueqi verfasserin aut Enthalten in LWT - food science and technology Amsterdam [u.a.] : Elsevier, 1993 189 Online-Ressource (DE-627)266892248 (DE-600)1469139-5 (DE-576)103373179 nnns volume:189 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-FOR GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 48.00 Land- und Forstwirtschaft: Allgemeines VZ 58.34 Lebensmitteltechnologie VZ AR 189
allfieldsGer	10.1016/j.lwt.2023.115483 doi (DE-627)ELV065888960 (ELSEVIER)S0023-6438(23)01062-9 DE-627 ger DE-627 rda eng 660 VZ 48.00 bkl 58.34 bkl Wu, Yamei verfasserin aut Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products. Emulsifying properties Gelation Structural properties Functional properties Xiang, Huan verfasserin aut Chen, Shengjun verfasserin aut Zhao, Yongqiang verfasserin aut Cai, Qiuxing verfasserin aut Lin, Wanling verfasserin aut Wu, Yanyan verfasserin aut Wang, Yueqi verfasserin aut Enthalten in LWT - food science and technology Amsterdam [u.a.] : Elsevier, 1993 189 Online-Ressource (DE-627)266892248 (DE-600)1469139-5 (DE-576)103373179 nnns volume:189 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-FOR GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 48.00 Land- und Forstwirtschaft: Allgemeines VZ 58.34 Lebensmitteltechnologie VZ AR 189
allfieldsSound	10.1016/j.lwt.2023.115483 doi (DE-627)ELV065888960 (ELSEVIER)S0023-6438(23)01062-9 DE-627 ger DE-627 rda eng 660 VZ 48.00 bkl 58.34 bkl Wu, Yamei verfasserin aut Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products. Emulsifying properties Gelation Structural properties Functional properties Xiang, Huan verfasserin aut Chen, Shengjun verfasserin aut Zhao, Yongqiang verfasserin aut Cai, Qiuxing verfasserin aut Lin, Wanling verfasserin aut Wu, Yanyan verfasserin aut Wang, Yueqi verfasserin aut Enthalten in LWT - food science and technology Amsterdam [u.a.] : Elsevier, 1993 189 Online-Ressource (DE-627)266892248 (DE-600)1469139-5 (DE-576)103373179 nnns volume:189 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-FOR GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 48.00 Land- und Forstwirtschaft: Allgemeines VZ 58.34 Lebensmitteltechnologie VZ AR 189
language	English
source	Enthalten in LWT - food science and technology 189 volume:189
sourceStr	Enthalten in LWT - food science and technology 189 volume:189
format_phy_str_mv	Article
bklname	Land- und Forstwirtschaft: Allgemeines Lebensmitteltechnologie
institution	findex.gbv.de
topic_facet	Emulsifying properties Gelation Structural properties Functional properties
dewey-raw	660
isfreeaccess_bool	false
container_title	LWT - food science and technology
authorswithroles_txt_mv	Wu, Yamei @@aut@@ Xiang, Huan @@aut@@ Chen, Shengjun @@aut@@ Zhao, Yongqiang @@aut@@ Cai, Qiuxing @@aut@@ Lin, Wanling @@aut@@ Wu, Yanyan @@aut@@ Wang, Yueqi @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	266892248
dewey-sort	3660
id	ELV065888960
language_de	englisch
fullrecord	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV065888960</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20240105093219.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">231130s2023 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.lwt.2023.115483</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV065888960</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0023-6438(23)01062-9</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">660</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">48.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">58.34</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Wu, Yamei</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2023</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Emulsifying properties</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Gelation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Structural properties</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Functional properties</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Xiang, Huan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chen, Shengjun</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhao, Yongqiang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cai, Qiuxing</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lin, Wanling</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wu, Yanyan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Yueqi</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">LWT - food science and technology</subfield><subfield code="d">Amsterdam [u.a.] : Elsevier, 1993</subfield><subfield code="g">189</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)266892248</subfield><subfield code="w">(DE-600)1469139-5</subfield><subfield code="w">(DE-576)103373179</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:189</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_39</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_63</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_161</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_170</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_224</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_285</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_293</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2001</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2003</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2004</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2005</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2007</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2008</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2009</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2010</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2011</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2015</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2020</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2021</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2025</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2026</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2027</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2034</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2044</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2048</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2049</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2050</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2055</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2056</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2059</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2061</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2064</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2088</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2106</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2122</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2129</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2143</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2152</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2153</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2190</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2232</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2336</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2470</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2507</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4035</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4126</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4242</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4251</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4325</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4326</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4333</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4334</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4367</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4393</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">48.00</subfield><subfield code="j">Land- und Forstwirtschaft: Allgemeines</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">58.34</subfield><subfield code="j">Lebensmitteltechnologie</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">189</subfield></datafield></record></collection>
author	Wu, Yamei
spellingShingle	Wu, Yamei ddc 660 bkl 48.00 bkl 58.34 misc Emulsifying properties misc Gelation misc Structural properties misc Functional properties Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities
authorStr	Wu, Yamei
ppnlink_with_tag_str_mv	@@773@@(DE-627)266892248
format	electronic Article
dewey-ones	660 - Chemical engineering
delete_txt_mv	keep
author_role	aut aut aut aut aut aut aut aut
collection	elsevier
remote_str	true
illustrated	Not Illustrated
topic_title	660 VZ 48.00 bkl 58.34 bkl Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities Emulsifying properties Gelation Structural properties Functional properties
topic	ddc 660 bkl 48.00 bkl 58.34 misc Emulsifying properties misc Gelation misc Structural properties misc Functional properties
topic_unstemmed	ddc 660 bkl 48.00 bkl 58.34 misc Emulsifying properties misc Gelation misc Structural properties misc Functional properties
topic_browse	ddc 660 bkl 48.00 bkl 58.34 misc Emulsifying properties misc Gelation misc Structural properties misc Functional properties
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
format_main_str_mv	Text Zeitschrift/Artikel
carriertype_str_mv	cr
hierarchy_parent_title	LWT - food science and technology
hierarchy_parent_id	266892248
dewey-tens	660 - Chemical engineering
hierarchy_top_title	LWT - food science and technology
isfreeaccess_txt	false
familylinks_str_mv	(DE-627)266892248 (DE-600)1469139-5 (DE-576)103373179
title	Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities
ctrlnum	(DE-627)ELV065888960 (ELSEVIER)S0023-6438(23)01062-9
title_full	Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities
author_sort	Wu, Yamei
journal	LWT - food science and technology
journalStr	LWT - food science and technology
lang_code	eng
isOA_bool	false
dewey-hundreds	600 - Technology
recordtype	marc
publishDateSort	2023
contenttype_str_mv	zzz
author_browse	Wu, Yamei Xiang, Huan Chen, Shengjun Zhao, Yongqiang Cai, Qiuxing Lin, Wanling Wu, Yanyan Wang, Yueqi
container_volume	189
class	660 VZ 48.00 bkl 58.34 bkl
format_se	Elektronische Aufsätze
author-letter	Wu, Yamei
doi_str_mv	10.1016/j.lwt.2023.115483
dewey-full	660
author2-role	verfasserin
title_sort	characterization of the aggregation behavior of sea bass ( lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: protein structures, gel properties, and emulsion stabilities
title_auth	Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities
abstract	Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products.
abstractGer	Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products.
abstract_unstemmed	Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products.
collection_details	GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-FOR GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700
title_short	Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities
remote_bool	true
author2	Xiang, Huan Chen, Shengjun Zhao, Yongqiang Cai, Qiuxing Lin, Wanling Wu, Yanyan Wang, Yueqi
author2Str	Xiang, Huan Chen, Shengjun Zhao, Yongqiang Cai, Qiuxing Lin, Wanling Wu, Yanyan Wang, Yueqi
ppnlink	266892248
mediatype_str_mv	c
isOA_txt	false
hochschulschrift_bool	false
doi_str	10.1016/j.lwt.2023.115483
up_date	2024-07-07T00:36:01.920Z
_version_	1803878464929923072
fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV065888960</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20240105093219.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">231130s2023 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.lwt.2023.115483</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV065888960</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0023-6438(23)01062-9</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">660</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">48.00</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">58.34</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Wu, Yamei</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2023</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from α-helices to β-sheets and increased the reactive sulfhydryl groups from 3.12 μmol/g to 3.93 μmol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%–69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Emulsifying properties</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Gelation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Structural properties</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Functional properties</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Xiang, Huan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chen, Shengjun</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhao, Yongqiang</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cai, Qiuxing</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lin, Wanling</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wu, Yanyan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wang, Yueqi</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">LWT - food science and technology</subfield><subfield code="d">Amsterdam [u.a.] : Elsevier, 1993</subfield><subfield code="g">189</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)266892248</subfield><subfield code="w">(DE-600)1469139-5</subfield><subfield code="w">(DE-576)103373179</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:189</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_23</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_39</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_60</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_62</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_63</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_65</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_69</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_70</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_73</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_95</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_105</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_151</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_161</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_170</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_213</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_224</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_230</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_285</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_293</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_602</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2001</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2003</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2004</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2005</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2007</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2008</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2009</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2010</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2011</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2014</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2015</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2020</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2021</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2025</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2026</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2027</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2034</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2044</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2048</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2049</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2050</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2055</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2056</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2059</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2061</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2064</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2088</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2106</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2110</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2122</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2129</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2143</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2152</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2153</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2190</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2232</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2336</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2470</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_2507</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4012</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4035</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4037</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4112</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4125</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4126</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4242</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4249</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4251</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4305</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4306</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4307</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4313</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4322</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4323</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4324</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4325</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4326</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4333</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4334</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4338</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4367</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4393</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_4700</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">48.00</subfield><subfield code="j">Land- und Forstwirtschaft: Allgemeines</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">58.34</subfield><subfield code="j">Lebensmitteltechnologie</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">189</subfield></datafield></record></collection>
score	7.399186

Nicht das Richtige dabei?

Schreiben Sie uns!

Characterization of the aggregation behavior of sea bass ( Lateolabrax japonicus ) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities

Nicht das Richtige dabei?

Zugang & Verfügbarkeit

Vorhandene Bände

Nicht das Richtige dabei?