Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates
Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of pl...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Qian, Fang [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2018 |
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| Schlagwörter: |
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| Anmerkung: |
© Association of Food Scientists & Technologists (India) 2018 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of food science and technology - Mysore, India : Springer, 2010, 55(2018), 3 vom: 05. Feb., Seite 1021-1027 |
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| Übergeordnetes Werk: |
volume:55 ; year:2018 ; number:3 ; day:05 ; month:02 ; pages:1021-1027 |
| Links: |
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| DOI / URN: |
10.1007/s13197-017-3015-8 |
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| Katalog-ID: |
SPR031113249 |
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| 520 | |a Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. | ||
| 650 | 4 | |a Soybean protein hydrolysate |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Whey protein hydrolysate |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Pepsin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Plastein reaction |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Bile acid binding capacity |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Wang, Ying |4 aut | |
| 700 | 1 | |a Wen, Zi-jian |4 aut | |
| 700 | 1 | |a Jiang, Shu-juan |4 aut | |
| 700 | 1 | |a Tuo, Yan-feng |4 aut | |
| 700 | 1 | |a Mu, Guang-qing |4 aut | |
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10.1007/s13197-017-3015-8 doi (DE-627)SPR031113249 (SPR)s13197-017-3015-8-e DE-627 ger DE-627 rakwb eng Qian, Fang verfasserin aut Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Association of Food Scientists & Technologists (India) 2018 Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. Soybean protein hydrolysate (dpeaa)DE-He213 Whey protein hydrolysate (dpeaa)DE-He213 Pepsin (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Bile acid binding capacity (dpeaa)DE-He213 Wang, Ying aut Wen, Zi-jian aut Jiang, Shu-juan aut Tuo, Yan-feng aut Mu, Guang-qing aut Enthalten in Journal of food science and technology Mysore, India : Springer, 2010 55(2018), 3 vom: 05. Feb., Seite 1021-1027 (DE-627)618327800 (DE-600)2537738-3 0975-8402 nnns volume:55 year:2018 number:3 day:05 month:02 pages:1021-1027 https://dx.doi.org/10.1007/s13197-017-3015-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA 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_101 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_2472 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_4367 GBV_ILN_4393 GBV_ILN_4700 AR 55 2018 3 05 02 1021-1027 |
| spelling |
10.1007/s13197-017-3015-8 doi (DE-627)SPR031113249 (SPR)s13197-017-3015-8-e DE-627 ger DE-627 rakwb eng Qian, Fang verfasserin aut Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Association of Food Scientists & Technologists (India) 2018 Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. Soybean protein hydrolysate (dpeaa)DE-He213 Whey protein hydrolysate (dpeaa)DE-He213 Pepsin (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Bile acid binding capacity (dpeaa)DE-He213 Wang, Ying aut Wen, Zi-jian aut Jiang, Shu-juan aut Tuo, Yan-feng aut Mu, Guang-qing aut Enthalten in Journal of food science and technology Mysore, India : Springer, 2010 55(2018), 3 vom: 05. Feb., Seite 1021-1027 (DE-627)618327800 (DE-600)2537738-3 0975-8402 nnns volume:55 year:2018 number:3 day:05 month:02 pages:1021-1027 https://dx.doi.org/10.1007/s13197-017-3015-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA 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_101 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_2472 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_4367 GBV_ILN_4393 GBV_ILN_4700 AR 55 2018 3 05 02 1021-1027 |
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10.1007/s13197-017-3015-8 doi (DE-627)SPR031113249 (SPR)s13197-017-3015-8-e DE-627 ger DE-627 rakwb eng Qian, Fang verfasserin aut Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Association of Food Scientists & Technologists (India) 2018 Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. Soybean protein hydrolysate (dpeaa)DE-He213 Whey protein hydrolysate (dpeaa)DE-He213 Pepsin (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Bile acid binding capacity (dpeaa)DE-He213 Wang, Ying aut Wen, Zi-jian aut Jiang, Shu-juan aut Tuo, Yan-feng aut Mu, Guang-qing aut Enthalten in Journal of food science and technology Mysore, India : Springer, 2010 55(2018), 3 vom: 05. Feb., Seite 1021-1027 (DE-627)618327800 (DE-600)2537738-3 0975-8402 nnns volume:55 year:2018 number:3 day:05 month:02 pages:1021-1027 https://dx.doi.org/10.1007/s13197-017-3015-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA 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_101 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_2472 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_4367 GBV_ILN_4393 GBV_ILN_4700 AR 55 2018 3 05 02 1021-1027 |
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10.1007/s13197-017-3015-8 doi (DE-627)SPR031113249 (SPR)s13197-017-3015-8-e DE-627 ger DE-627 rakwb eng Qian, Fang verfasserin aut Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Association of Food Scientists & Technologists (India) 2018 Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. Soybean protein hydrolysate (dpeaa)DE-He213 Whey protein hydrolysate (dpeaa)DE-He213 Pepsin (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Bile acid binding capacity (dpeaa)DE-He213 Wang, Ying aut Wen, Zi-jian aut Jiang, Shu-juan aut Tuo, Yan-feng aut Mu, Guang-qing aut Enthalten in Journal of food science and technology Mysore, India : Springer, 2010 55(2018), 3 vom: 05. Feb., Seite 1021-1027 (DE-627)618327800 (DE-600)2537738-3 0975-8402 nnns volume:55 year:2018 number:3 day:05 month:02 pages:1021-1027 https://dx.doi.org/10.1007/s13197-017-3015-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA 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_101 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_2472 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_4367 GBV_ILN_4393 GBV_ILN_4700 AR 55 2018 3 05 02 1021-1027 |
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10.1007/s13197-017-3015-8 doi (DE-627)SPR031113249 (SPR)s13197-017-3015-8-e DE-627 ger DE-627 rakwb eng Qian, Fang verfasserin aut Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Association of Food Scientists & Technologists (India) 2018 Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. Soybean protein hydrolysate (dpeaa)DE-He213 Whey protein hydrolysate (dpeaa)DE-He213 Pepsin (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Bile acid binding capacity (dpeaa)DE-He213 Wang, Ying aut Wen, Zi-jian aut Jiang, Shu-juan aut Tuo, Yan-feng aut Mu, Guang-qing aut Enthalten in Journal of food science and technology Mysore, India : Springer, 2010 55(2018), 3 vom: 05. Feb., Seite 1021-1027 (DE-627)618327800 (DE-600)2537738-3 0975-8402 nnns volume:55 year:2018 number:3 day:05 month:02 pages:1021-1027 https://dx.doi.org/10.1007/s13197-017-3015-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA 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_101 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_2472 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_4367 GBV_ILN_4393 GBV_ILN_4700 AR 55 2018 3 05 02 1021-1027 |
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Enthalten in Journal of food science and technology 55(2018), 3 vom: 05. Feb., Seite 1021-1027 volume:55 year:2018 number:3 day:05 month:02 pages:1021-1027 |
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Qian, Fang @@aut@@ Wang, Ying @@aut@@ Wen, Zi-jian @@aut@@ Jiang, Shu-juan @@aut@@ Tuo, Yan-feng @@aut@@ Mu, Guang-qing @@aut@@ |
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The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. 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|
| author |
Qian, Fang |
| spellingShingle |
Qian, Fang misc Soybean protein hydrolysate misc Whey protein hydrolysate misc Pepsin misc Plastein reaction misc Bile acid binding capacity Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates |
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0975-8402 |
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Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates Soybean protein hydrolysate (dpeaa)DE-He213 Whey protein hydrolysate (dpeaa)DE-He213 Pepsin (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Bile acid binding capacity (dpeaa)DE-He213 |
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misc Soybean protein hydrolysate misc Whey protein hydrolysate misc Pepsin misc Plastein reaction misc Bile acid binding capacity |
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misc Soybean protein hydrolysate misc Whey protein hydrolysate misc Pepsin misc Plastein reaction misc Bile acid binding capacity |
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misc Soybean protein hydrolysate misc Whey protein hydrolysate misc Pepsin misc Plastein reaction misc Bile acid binding capacity |
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Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates |
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Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates |
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Qian, Fang |
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Journal of food science and technology |
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Qian, Fang Wang, Ying Wen, Zi-jian Jiang, Shu-juan Tuo, Yan-feng Mu, Guang-qing |
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Qian, Fang |
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10.1007/s13197-017-3015-8 |
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plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates |
| title_auth |
Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates |
| abstract |
Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. © Association of Food Scientists & Technologists (India) 2018 |
| abstractGer |
Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. © Association of Food Scientists & Technologists (India) 2018 |
| abstract_unstemmed |
Abstract Plastein reaction is a modification reaction that can improve the functional properties of protein hydrolysate. The product of the reaction is a thixotropic aggregation of peptides. This study investigated the formation condition of soybean-whey plastein and bile acid binding capacity of plastein. Soy protein and whey protein were hydrolyzed by pepsin. The mixture (1:1, w/w) of two hydrolysates was modified by pepsin again. After the reaction, the decrease in free amino groups and the turbidity of the modified hydrolysate were measured to obtain appropriate reaction condition. Results showed that the concentration of hydrolysates 40% (w/v), enzyme ratio of 2.0 KU/g protein, pH 5.0, 37 °C, reaction time of 3.0 h respectively, were showed maximum changes in protein hydrolysates. Tricine SDS-PAGE analysis under denaturing conditions revealed that whey protein was more sensitive to pepsin and yielded different polypeptides (PPs) of molecular weight ranged from 3.5–17 kDa. However, a high molecular weight PP was completely hydrolyzed while PPs of 14.2–26 kDa were partially digested after pepsin treatment. Native page analysis further revealed the presence of a high-molecular weight PP in crude and purified plastein product. The bile acid binding capacity was improved by the plastein reaction. The amount of binding sodium deoxycholate, sodium taurocholate, and sodium cholate were 0.75, 2.0 and 1.87 μmol/100 mg respectively. © Association of Food Scientists & Technologists (India) 2018 |
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| title_short |
Plastein reaction enhanced bile-acid binding capacity of soybean protein hydrolysates and whey protein hydrolysates |
| url |
https://dx.doi.org/10.1007/s13197-017-3015-8 |
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| author2 |
Wang, Ying Wen, Zi-jian Jiang, Shu-juan Tuo, Yan-feng Mu, Guang-qing |
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Wang, Ying Wen, Zi-jian Jiang, Shu-juan Tuo, Yan-feng Mu, Guang-qing |
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10.1007/s13197-017-3015-8 |
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2024-07-03T22:02:48.806Z |
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| score |
7.4020147 |