Characterization of the purified actinidin as a plant coagulant of bovine milk

Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and S...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Lo Piero, Angela Roberta [verfasserIn] Puglisi, Ivana Petrone, Goffredo

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2011

Schlagwörter:	Actinidin Plant coagulant Milk-clotting SDS–PAGE Casein

Anmerkung:	© Springer-Verlag 2011

Übergeordnetes Werk:	Enthalten in: European food research and technology - Berlin : Springer, 1999, 233(2011), 3 vom: 30. Juli
Übergeordnetes Werk:	volume:233 ; year:2011 ; number:3 ; day:30 ; month:07

Links:	Volltext

DOI / URN:	10.1007/s00217-011-1543-4

Katalog-ID:	SPR002303094

Internformat


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100	1		\|a Lo Piero, Angela Roberta \|e verfasserin \|4 aut
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520			\|a Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments.
650		4	\|a Actinidin \|7 (dpeaa)DE-He213
650		4	\|a Plant coagulant \|7 (dpeaa)DE-He213
650		4	\|a Milk-clotting \|7 (dpeaa)DE-He213
650		4	\|a SDS–PAGE \|7 (dpeaa)DE-He213
650		4	\|a Casein \|7 (dpeaa)DE-He213
700	1		\|a Puglisi, Ivana \|4 aut
700	1		\|a Petrone, Goffredo \|4 aut
773	0	8	\|i Enthalten in \|t European food research and technology \|d Berlin : Springer, 1999 \|g 233(2011), 3 vom: 30. Juli \|w (DE-627)27012859X \|w (DE-600)1476605-X \|x 1438-2385 \|7 nnns
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856	4	0	\|u https://dx.doi.org/10.1007/s00217-011-1543-4 \|z lizenzpflichtig \|3 Volltext
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912			\|a GBV_ILN_23
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_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_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_2070
912			\|a GBV_ILN_2086
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_2116
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
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_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_2548
912			\|a GBV_ILN_4012
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
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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_4335
912			\|a GBV_ILN_4336
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
951			\|a AR
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Indexfelder

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matchkey_str	article:14382385:2011----::hrceiainfhprfeatndnspato
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publishDate	2011
allfields	10.1007/s00217-011-1543-4 doi (DE-627)SPR002303094 (SPR)s00217-011-1543-4-e DE-627 ger DE-627 rakwb eng Lo Piero, Angela Roberta verfasserin aut Characterization of the purified actinidin as a plant coagulant of bovine milk 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2011 Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. Actinidin (dpeaa)DE-He213 Plant coagulant (dpeaa)DE-He213 Milk-clotting (dpeaa)DE-He213 SDS–PAGE (dpeaa)DE-He213 Casein (dpeaa)DE-He213 Puglisi, Ivana aut Petrone, Goffredo aut Enthalten in European food research and technology Berlin : Springer, 1999 233(2011), 3 vom: 30. Juli (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:233 year:2011 number:3 day:30 month:07 https://dx.doi.org/10.1007/s00217-011-1543-4 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 233 2011 3 30 07
spelling	10.1007/s00217-011-1543-4 doi (DE-627)SPR002303094 (SPR)s00217-011-1543-4-e DE-627 ger DE-627 rakwb eng Lo Piero, Angela Roberta verfasserin aut Characterization of the purified actinidin as a plant coagulant of bovine milk 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2011 Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. Actinidin (dpeaa)DE-He213 Plant coagulant (dpeaa)DE-He213 Milk-clotting (dpeaa)DE-He213 SDS–PAGE (dpeaa)DE-He213 Casein (dpeaa)DE-He213 Puglisi, Ivana aut Petrone, Goffredo aut Enthalten in European food research and technology Berlin : Springer, 1999 233(2011), 3 vom: 30. Juli (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:233 year:2011 number:3 day:30 month:07 https://dx.doi.org/10.1007/s00217-011-1543-4 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 233 2011 3 30 07
allfields_unstemmed	10.1007/s00217-011-1543-4 doi (DE-627)SPR002303094 (SPR)s00217-011-1543-4-e DE-627 ger DE-627 rakwb eng Lo Piero, Angela Roberta verfasserin aut Characterization of the purified actinidin as a plant coagulant of bovine milk 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2011 Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. Actinidin (dpeaa)DE-He213 Plant coagulant (dpeaa)DE-He213 Milk-clotting (dpeaa)DE-He213 SDS–PAGE (dpeaa)DE-He213 Casein (dpeaa)DE-He213 Puglisi, Ivana aut Petrone, Goffredo aut Enthalten in European food research and technology Berlin : Springer, 1999 233(2011), 3 vom: 30. Juli (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:233 year:2011 number:3 day:30 month:07 https://dx.doi.org/10.1007/s00217-011-1543-4 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 233 2011 3 30 07
allfieldsGer	10.1007/s00217-011-1543-4 doi (DE-627)SPR002303094 (SPR)s00217-011-1543-4-e DE-627 ger DE-627 rakwb eng Lo Piero, Angela Roberta verfasserin aut Characterization of the purified actinidin as a plant coagulant of bovine milk 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2011 Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. Actinidin (dpeaa)DE-He213 Plant coagulant (dpeaa)DE-He213 Milk-clotting (dpeaa)DE-He213 SDS–PAGE (dpeaa)DE-He213 Casein (dpeaa)DE-He213 Puglisi, Ivana aut Petrone, Goffredo aut Enthalten in European food research and technology Berlin : Springer, 1999 233(2011), 3 vom: 30. Juli (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:233 year:2011 number:3 day:30 month:07 https://dx.doi.org/10.1007/s00217-011-1543-4 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 233 2011 3 30 07
allfieldsSound	10.1007/s00217-011-1543-4 doi (DE-627)SPR002303094 (SPR)s00217-011-1543-4-e DE-627 ger DE-627 rakwb eng Lo Piero, Angela Roberta verfasserin aut Characterization of the purified actinidin as a plant coagulant of bovine milk 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2011 Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. Actinidin (dpeaa)DE-He213 Plant coagulant (dpeaa)DE-He213 Milk-clotting (dpeaa)DE-He213 SDS–PAGE (dpeaa)DE-He213 Casein (dpeaa)DE-He213 Puglisi, Ivana aut Petrone, Goffredo aut Enthalten in European food research and technology Berlin : Springer, 1999 233(2011), 3 vom: 30. Juli (DE-627)27012859X (DE-600)1476605-X 1438-2385 nnns volume:233 year:2011 number:3 day:30 month:07 https://dx.doi.org/10.1007/s00217-011-1543-4 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 233 2011 3 30 07
language	English
source	Enthalten in European food research and technology 233(2011), 3 vom: 30. Juli volume:233 year:2011 number:3 day:30 month:07
sourceStr	Enthalten in European food research and technology 233(2011), 3 vom: 30. Juli volume:233 year:2011 number:3 day:30 month:07
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Actinidin Plant coagulant Milk-clotting SDS–PAGE Casein
isfreeaccess_bool	false
container_title	European food research and technology
authorswithroles_txt_mv	Lo Piero, Angela Roberta @@aut@@ Puglisi, Ivana @@aut@@ Petrone, Goffredo @@aut@@
publishDateDaySort_date	2011-07-30T00:00:00Z
hierarchy_top_id	27012859X
id	SPR002303094
language_de	englisch
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author	Lo Piero, Angela Roberta
spellingShingle	Lo Piero, Angela Roberta misc Actinidin misc Plant coagulant misc Milk-clotting misc SDS–PAGE misc Casein Characterization of the purified actinidin as a plant coagulant of bovine milk
authorStr	Lo Piero, Angela Roberta
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topic_title	Characterization of the purified actinidin as a plant coagulant of bovine milk Actinidin (dpeaa)DE-He213 Plant coagulant (dpeaa)DE-He213 Milk-clotting (dpeaa)DE-He213 SDS–PAGE (dpeaa)DE-He213 Casein (dpeaa)DE-He213
topic	misc Actinidin misc Plant coagulant misc Milk-clotting misc SDS–PAGE misc Casein
topic_unstemmed	misc Actinidin misc Plant coagulant misc Milk-clotting misc SDS–PAGE misc Casein
topic_browse	misc Actinidin misc Plant coagulant misc Milk-clotting misc SDS–PAGE misc Casein
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title	Characterization of the purified actinidin as a plant coagulant of bovine milk
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title_full	Characterization of the purified actinidin as a plant coagulant of bovine milk
author_sort	Lo Piero, Angela Roberta
journal	European food research and technology
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author_browse	Lo Piero, Angela Roberta Puglisi, Ivana Petrone, Goffredo
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doi_str_mv	10.1007/s00217-011-1543-4
title_sort	characterization of the purified actinidin as a plant coagulant of bovine milk
title_auth	Characterization of the purified actinidin as a plant coagulant of bovine milk
abstract	Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. © Springer-Verlag 2011
abstractGer	Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. © Springer-Verlag 2011
abstract_unstemmed	Abstract In this work, actinidin was characterized in view of its possible suitability as a coagulant enzyme in the manufacturing process of cheese. The results show that actinidin does exhibit milk-clotting activity, which is correlated with the enzyme concentrations. The combined use of urea and SDS–PAGE led to the conclusion that the milk clot is clearly separated from the whey proteins and corresponds to casein coagulum. Moreover, both the enzyme dependence on pH and temperature and the stability profiles are fully suitable with the chemical–physical conditions adopted during the cheese-making procedure. The analysis of the kinetic constants as well as the electrophoretic pattern of the hydrolysis products suggests that β-casein is the preferred substrate of actinidin, whereas κ-casein seems to be hydrolyzed only in a few large fragments. © Springer-Verlag 2011
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title_short	Characterization of the purified actinidin as a plant coagulant of bovine milk
url	https://dx.doi.org/10.1007/s00217-011-1543-4
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up_date	2024-07-04T02:33:27.606Z
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Characterization of the purified actinidin as a plant coagulant of bovine milk

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