The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates

Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present...
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Autor*in:	Yavuz-Düzgün, Merve [verfasserIn] Zeeb, Benjamin [verfasserIn] Dreher, Johannes [verfasserIn] Özçelik, Beraat [verfasserIn] Weiss, Jochen [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	Potato protein isolate Apple pectin Citrus pectin Complex coacervation Bitterness

Übergeordnetes Werk:	Enthalten in: Food biophysics - New York, NY : Springer, 2006, 15(2020), 3 vom: 15. Apr., Seite 376-385
Übergeordnetes Werk:	volume:15 ; year:2020 ; number:3 ; day:15 ; month:04 ; pages:376-385

Links:	Volltext

DOI / URN:	10.1007/s11483-020-09631-1

Katalog-ID:	SPR040552381

Internformat


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245	1	4	\|a The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates
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520			\|a Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications.
650		4	\|a Potato protein isolate \|7 (dpeaa)DE-He213
650		4	\|a Apple pectin \|7 (dpeaa)DE-He213
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650		4	\|a Bitterness \|7 (dpeaa)DE-He213
700	1		\|a Zeeb, Benjamin \|e verfasserin \|4 aut
700	1		\|a Dreher, Johannes \|e verfasserin \|4 aut
700	1		\|a Özçelik, Beraat \|e verfasserin \|4 aut
700	1		\|a Weiss, Jochen \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Food biophysics \|d New York, NY : Springer, 2006 \|g 15(2020), 3 vom: 15. Apr., Seite 376-385 \|w (DE-627)51061714X \|w (DE-600)2231378-3 \|x 1557-1866 \|7 nnns
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912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
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_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_138
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_152
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_250
912			\|a GBV_ILN_281
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
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_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
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_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2107
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2446
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2472
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_2548
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4246
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_4328
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4336
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
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author_variant	m y d myd b z bz j d jd b ö bö j w jw
matchkey_str	article:15571866:2020----::hipcoetrfctodgeadorefetnocmlxocrainstotmste
hierarchy_sort_str	2020
bklnumber	58.34
publishDate	2020
allfields	10.1007/s11483-020-09631-1 doi (DE-627)SPR040552381 (SPR)s11483-020-09631-1-e DE-627 ger DE-627 rakwb eng 630 640 ASE 58.34 bkl Yavuz-Düzgün, Merve verfasserin aut The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications. Potato protein isolate (dpeaa)DE-He213 Apple pectin (dpeaa)DE-He213 Citrus pectin (dpeaa)DE-He213 Complex coacervation (dpeaa)DE-He213 Bitterness (dpeaa)DE-He213 Zeeb, Benjamin verfasserin aut Dreher, Johannes verfasserin aut Özçelik, Beraat verfasserin aut Weiss, Jochen verfasserin aut Enthalten in Food biophysics New York, NY : Springer, 2006 15(2020), 3 vom: 15. Apr., Seite 376-385 (DE-627)51061714X (DE-600)2231378-3 1557-1866 nnns volume:15 year:2020 number:3 day:15 month:04 pages:376-385 https://dx.doi.org/10.1007/s11483-020-09631-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 ASE AR 15 2020 3 15 04 376-385
spelling	10.1007/s11483-020-09631-1 doi (DE-627)SPR040552381 (SPR)s11483-020-09631-1-e DE-627 ger DE-627 rakwb eng 630 640 ASE 58.34 bkl Yavuz-Düzgün, Merve verfasserin aut The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications. Potato protein isolate (dpeaa)DE-He213 Apple pectin (dpeaa)DE-He213 Citrus pectin (dpeaa)DE-He213 Complex coacervation (dpeaa)DE-He213 Bitterness (dpeaa)DE-He213 Zeeb, Benjamin verfasserin aut Dreher, Johannes verfasserin aut Özçelik, Beraat verfasserin aut Weiss, Jochen verfasserin aut Enthalten in Food biophysics New York, NY : Springer, 2006 15(2020), 3 vom: 15. Apr., Seite 376-385 (DE-627)51061714X (DE-600)2231378-3 1557-1866 nnns volume:15 year:2020 number:3 day:15 month:04 pages:376-385 https://dx.doi.org/10.1007/s11483-020-09631-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 ASE AR 15 2020 3 15 04 376-385
allfields_unstemmed	10.1007/s11483-020-09631-1 doi (DE-627)SPR040552381 (SPR)s11483-020-09631-1-e DE-627 ger DE-627 rakwb eng 630 640 ASE 58.34 bkl Yavuz-Düzgün, Merve verfasserin aut The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications. Potato protein isolate (dpeaa)DE-He213 Apple pectin (dpeaa)DE-He213 Citrus pectin (dpeaa)DE-He213 Complex coacervation (dpeaa)DE-He213 Bitterness (dpeaa)DE-He213 Zeeb, Benjamin verfasserin aut Dreher, Johannes verfasserin aut Özçelik, Beraat verfasserin aut Weiss, Jochen verfasserin aut Enthalten in Food biophysics New York, NY : Springer, 2006 15(2020), 3 vom: 15. Apr., Seite 376-385 (DE-627)51061714X (DE-600)2231378-3 1557-1866 nnns volume:15 year:2020 number:3 day:15 month:04 pages:376-385 https://dx.doi.org/10.1007/s11483-020-09631-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 ASE AR 15 2020 3 15 04 376-385
allfieldsGer	10.1007/s11483-020-09631-1 doi (DE-627)SPR040552381 (SPR)s11483-020-09631-1-e DE-627 ger DE-627 rakwb eng 630 640 ASE 58.34 bkl Yavuz-Düzgün, Merve verfasserin aut The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications. Potato protein isolate (dpeaa)DE-He213 Apple pectin (dpeaa)DE-He213 Citrus pectin (dpeaa)DE-He213 Complex coacervation (dpeaa)DE-He213 Bitterness (dpeaa)DE-He213 Zeeb, Benjamin verfasserin aut Dreher, Johannes verfasserin aut Özçelik, Beraat verfasserin aut Weiss, Jochen verfasserin aut Enthalten in Food biophysics New York, NY : Springer, 2006 15(2020), 3 vom: 15. Apr., Seite 376-385 (DE-627)51061714X (DE-600)2231378-3 1557-1866 nnns volume:15 year:2020 number:3 day:15 month:04 pages:376-385 https://dx.doi.org/10.1007/s11483-020-09631-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 ASE AR 15 2020 3 15 04 376-385
allfieldsSound	10.1007/s11483-020-09631-1 doi (DE-627)SPR040552381 (SPR)s11483-020-09631-1-e DE-627 ger DE-627 rakwb eng 630 640 ASE 58.34 bkl Yavuz-Düzgün, Merve verfasserin aut The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications. Potato protein isolate (dpeaa)DE-He213 Apple pectin (dpeaa)DE-He213 Citrus pectin (dpeaa)DE-He213 Complex coacervation (dpeaa)DE-He213 Bitterness (dpeaa)DE-He213 Zeeb, Benjamin verfasserin aut Dreher, Johannes verfasserin aut Özçelik, Beraat verfasserin aut Weiss, Jochen verfasserin aut Enthalten in Food biophysics New York, NY : Springer, 2006 15(2020), 3 vom: 15. Apr., Seite 376-385 (DE-627)51061714X (DE-600)2231378-3 1557-1866 nnns volume:15 year:2020 number:3 day:15 month:04 pages:376-385 https://dx.doi.org/10.1007/s11483-020-09631-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 58.34 ASE AR 15 2020 3 15 04 376-385
language	English
source	Enthalten in Food biophysics 15(2020), 3 vom: 15. Apr., Seite 376-385 volume:15 year:2020 number:3 day:15 month:04 pages:376-385
sourceStr	Enthalten in Food biophysics 15(2020), 3 vom: 15. Apr., Seite 376-385 volume:15 year:2020 number:3 day:15 month:04 pages:376-385
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Potato protein isolate Apple pectin Citrus pectin Complex coacervation Bitterness
dewey-raw	630
isfreeaccess_bool	false
container_title	Food biophysics
authorswithroles_txt_mv	Yavuz-Düzgün, Merve @@aut@@ Zeeb, Benjamin @@aut@@ Dreher, Johannes @@aut@@ Özçelik, Beraat @@aut@@ Weiss, Jochen @@aut@@
publishDateDaySort_date	2020-04-15T00:00:00Z
hierarchy_top_id	51061714X
dewey-sort	3630
id	SPR040552381
language_de	englisch
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author	Yavuz-Düzgün, Merve
spellingShingle	Yavuz-Düzgün, Merve ddc 630 bkl 58.34 misc Potato protein isolate misc Apple pectin misc Citrus pectin misc Complex coacervation misc Bitterness The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates
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topic_title	630 640 ASE 58.34 bkl The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates Potato protein isolate (dpeaa)DE-He213 Apple pectin (dpeaa)DE-He213 Citrus pectin (dpeaa)DE-He213 Complex coacervation (dpeaa)DE-He213 Bitterness (dpeaa)DE-He213
topic	ddc 630 bkl 58.34 misc Potato protein isolate misc Apple pectin misc Citrus pectin misc Complex coacervation misc Bitterness
topic_unstemmed	ddc 630 bkl 58.34 misc Potato protein isolate misc Apple pectin misc Citrus pectin misc Complex coacervation misc Bitterness
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title	The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates
ctrlnum	(DE-627)SPR040552381 (SPR)s11483-020-09631-1-e
title_full	The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates
author_sort	Yavuz-Düzgün, Merve
journal	Food biophysics
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author_browse	Yavuz-Düzgün, Merve Zeeb, Benjamin Dreher, Johannes Özçelik, Beraat Weiss, Jochen
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title_sort	impact of esterification degree and source of pectins on complex coacervation as a tool to mask the bitterness of potato protein isolates
title_auth	The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates
abstract	Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications.
abstractGer	Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications.
abstract_unstemmed	Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. Our results might have significant implications for the utilization of potato proteins in beverage applications.
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title_short	The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates
url	https://dx.doi.org/10.1007/s11483-020-09631-1
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author2	Zeeb, Benjamin Dreher, Johannes Özçelik, Beraat Weiss, Jochen
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up_date	2024-07-03T16:44:41.519Z
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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">SPR040552381</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20220111072738.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2020 xx \|\|\|\|\|o 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s11483-020-09631-1</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR040552381</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s11483-020-09631-1-e</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">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">630</subfield><subfield code="a">640</subfield><subfield code="q">ASE</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">Yavuz-Düzgün, Merve</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="4"><subfield code="a">The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</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">Abstract There is an increasing interest in the food industry to use potato protein as an alternative plant protein. However, its bitter taste often limits the utilization in novel foods and beverages. Coacervation is a promising technique to mask bitterness of certain food compounds. In the present study, we aimed to reduce the degree of bitterness of potato protein by generating protein-pectin complexes based on coacervation. Potato protein isolate and pectins derived from various origins having different degree of esterification (DE) were initially mixed under acidic conditions to promote the formation of complexes. Single and complex biopolymers were then characterized in terms of surface charge, solubility, rheological and sensorial properties as a function of protein pectin ratio, pectin source, and the degree of esterification, respectively. The protein-pectin ratio and degree of esterification of pectins substantially influenced the interaction behaviour and phase separation of the protein-pectin mixtures. The bitterness score decreased with increasing surface charge and pectin concentration. Bitterness was strongly reduced for complexes formed with high DE citrus pectin at a protein pectin ratio 0.33. The complexes generated at this ratio were relatively stable based on visual observation and microscopic images. 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The Impact of Esterification Degree and Source of Pectins on Complex Coacervation as a Tool to Mask the Bitterness of Potato Protein Isolates

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