Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction

Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase...
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Autor*in:	Dandan Gao [verfasserIn] Penghui Guo [verfasserIn] Xin Cao [verfasserIn] Lili Ge [verfasserIn] Hongxin Ma [verfasserIn] Hao Cheng [verfasserIn] Yiqiang Ke [verfasserIn] Shien Chen [verfasserIn] Gongtao Ding [verfasserIn] Ruofei Feng [verfasserIn] Zilin Qiao [verfasserIn] Jialin Bai [verfasserIn] Nurul I. Nordin [verfasserIn] Zhongren Ma [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology

Übergeordnetes Werk:	In: Food Science & Nutrition - Wiley, 2014, 8(2020), 6, Seite 2798-2808
Übergeordnetes Werk:	volume:8 ; year:2020 ; number:6 ; pages:2798-2808

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1002/fsn3.1572

Katalog-ID:	DOAJ055977219

Internformat


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520			\|a Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%.
650		4	\|a ACE inhibitory activity
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700	0		\|a Zilin Qiao \|e verfasserin \|4 aut
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700	0		\|a Nurul I. Nordin \|e verfasserin \|4 aut
700	0		\|a Zhongren Ma \|e verfasserin \|4 aut
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allfields	10.1002/fsn3.1572 doi (DE-627)DOAJ055977219 (DE-599)DOAJ04d7de312a4d41d8b687485b14125a46 DE-627 ger DE-627 rakwb eng TX341-641 Dandan Gao verfasserin aut Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%. ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology Nutrition. Foods and food supply Penghui Guo verfasserin aut Xin Cao verfasserin aut Lili Ge verfasserin aut Hongxin Ma verfasserin aut Hao Cheng verfasserin aut Yiqiang Ke verfasserin aut Shien Chen verfasserin aut Gongtao Ding verfasserin aut Ruofei Feng verfasserin aut Zilin Qiao verfasserin aut Jialin Bai verfasserin aut Nurul I. Nordin verfasserin aut Zhongren Ma verfasserin aut In Food Science & Nutrition Wiley, 2014 8(2020), 6, Seite 2798-2808 (DE-627)73655713X (DE-600)2703010-6 20487177 nnns volume:8 year:2020 number:6 pages:2798-2808 https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/article/04d7de312a4d41d8b687485b14125a46 kostenfrei https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/toc/2048-7177 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 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_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 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_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_4367 GBV_ILN_4700 AR 8 2020 6 2798-2808
spelling	10.1002/fsn3.1572 doi (DE-627)DOAJ055977219 (DE-599)DOAJ04d7de312a4d41d8b687485b14125a46 DE-627 ger DE-627 rakwb eng TX341-641 Dandan Gao verfasserin aut Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%. ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology Nutrition. Foods and food supply Penghui Guo verfasserin aut Xin Cao verfasserin aut Lili Ge verfasserin aut Hongxin Ma verfasserin aut Hao Cheng verfasserin aut Yiqiang Ke verfasserin aut Shien Chen verfasserin aut Gongtao Ding verfasserin aut Ruofei Feng verfasserin aut Zilin Qiao verfasserin aut Jialin Bai verfasserin aut Nurul I. Nordin verfasserin aut Zhongren Ma verfasserin aut In Food Science & Nutrition Wiley, 2014 8(2020), 6, Seite 2798-2808 (DE-627)73655713X (DE-600)2703010-6 20487177 nnns volume:8 year:2020 number:6 pages:2798-2808 https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/article/04d7de312a4d41d8b687485b14125a46 kostenfrei https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/toc/2048-7177 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 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_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 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_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_4367 GBV_ILN_4700 AR 8 2020 6 2798-2808
allfields_unstemmed	10.1002/fsn3.1572 doi (DE-627)DOAJ055977219 (DE-599)DOAJ04d7de312a4d41d8b687485b14125a46 DE-627 ger DE-627 rakwb eng TX341-641 Dandan Gao verfasserin aut Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%. ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology Nutrition. Foods and food supply Penghui Guo verfasserin aut Xin Cao verfasserin aut Lili Ge verfasserin aut Hongxin Ma verfasserin aut Hao Cheng verfasserin aut Yiqiang Ke verfasserin aut Shien Chen verfasserin aut Gongtao Ding verfasserin aut Ruofei Feng verfasserin aut Zilin Qiao verfasserin aut Jialin Bai verfasserin aut Nurul I. Nordin verfasserin aut Zhongren Ma verfasserin aut In Food Science & Nutrition Wiley, 2014 8(2020), 6, Seite 2798-2808 (DE-627)73655713X (DE-600)2703010-6 20487177 nnns volume:8 year:2020 number:6 pages:2798-2808 https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/article/04d7de312a4d41d8b687485b14125a46 kostenfrei https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/toc/2048-7177 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 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_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 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_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_4367 GBV_ILN_4700 AR 8 2020 6 2798-2808
allfieldsGer	10.1002/fsn3.1572 doi (DE-627)DOAJ055977219 (DE-599)DOAJ04d7de312a4d41d8b687485b14125a46 DE-627 ger DE-627 rakwb eng TX341-641 Dandan Gao verfasserin aut Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%. ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology Nutrition. Foods and food supply Penghui Guo verfasserin aut Xin Cao verfasserin aut Lili Ge verfasserin aut Hongxin Ma verfasserin aut Hao Cheng verfasserin aut Yiqiang Ke verfasserin aut Shien Chen verfasserin aut Gongtao Ding verfasserin aut Ruofei Feng verfasserin aut Zilin Qiao verfasserin aut Jialin Bai verfasserin aut Nurul I. Nordin verfasserin aut Zhongren Ma verfasserin aut In Food Science & Nutrition Wiley, 2014 8(2020), 6, Seite 2798-2808 (DE-627)73655713X (DE-600)2703010-6 20487177 nnns volume:8 year:2020 number:6 pages:2798-2808 https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/article/04d7de312a4d41d8b687485b14125a46 kostenfrei https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/toc/2048-7177 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 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_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 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_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_4367 GBV_ILN_4700 AR 8 2020 6 2798-2808
allfieldsSound	10.1002/fsn3.1572 doi (DE-627)DOAJ055977219 (DE-599)DOAJ04d7de312a4d41d8b687485b14125a46 DE-627 ger DE-627 rakwb eng TX341-641 Dandan Gao verfasserin aut Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%. ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology Nutrition. Foods and food supply Penghui Guo verfasserin aut Xin Cao verfasserin aut Lili Ge verfasserin aut Hongxin Ma verfasserin aut Hao Cheng verfasserin aut Yiqiang Ke verfasserin aut Shien Chen verfasserin aut Gongtao Ding verfasserin aut Ruofei Feng verfasserin aut Zilin Qiao verfasserin aut Jialin Bai verfasserin aut Nurul I. Nordin verfasserin aut Zhongren Ma verfasserin aut In Food Science & Nutrition Wiley, 2014 8(2020), 6, Seite 2798-2808 (DE-627)73655713X (DE-600)2703010-6 20487177 nnns volume:8 year:2020 number:6 pages:2798-2808 https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/article/04d7de312a4d41d8b687485b14125a46 kostenfrei https://doi.org/10.1002/fsn3.1572 kostenfrei https://doaj.org/toc/2048-7177 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_171 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 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_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 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_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_4367 GBV_ILN_4700 AR 8 2020 6 2798-2808
language	English
source	In Food Science & Nutrition 8(2020), 6, Seite 2798-2808 volume:8 year:2020 number:6 pages:2798-2808
sourceStr	In Food Science & Nutrition 8(2020), 6, Seite 2798-2808 volume:8 year:2020 number:6 pages:2798-2808
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology Nutrition. Foods and food supply
isfreeaccess_bool	true
container_title	Food Science & Nutrition
authorswithroles_txt_mv	Dandan Gao @@aut@@ Penghui Guo @@aut@@ Xin Cao @@aut@@ Lili Ge @@aut@@ Hongxin Ma @@aut@@ Hao Cheng @@aut@@ Yiqiang Ke @@aut@@ Shien Chen @@aut@@ Gongtao Ding @@aut@@ Ruofei Feng @@aut@@ Zilin Qiao @@aut@@ Jialin Bai @@aut@@ Nurul I. Nordin @@aut@@ Zhongren Ma @@aut@@
publishDateDaySort_date	2020-01-01T00:00:00Z
hierarchy_top_id	73655713X
id	DOAJ055977219
language_de	englisch
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callnumber-first	T - Technology
author	Dandan Gao
spellingShingle	Dandan Gao misc TX341-641 misc ACE inhibitory activity misc chicken plasma protein misc hydrolysate misc plastein reaction misc response surface methodology misc Nutrition. Foods and food supply Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction
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topic_title	TX341-641 Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction ACE inhibitory activity chicken plasma protein hydrolysate plastein reaction response surface methodology
topic	misc TX341-641 misc ACE inhibitory activity misc chicken plasma protein misc hydrolysate misc plastein reaction misc response surface methodology misc Nutrition. Foods and food supply
topic_unstemmed	misc TX341-641 misc ACE inhibitory activity misc chicken plasma protein misc hydrolysate misc plastein reaction misc response surface methodology misc Nutrition. Foods and food supply
topic_browse	misc TX341-641 misc ACE inhibitory activity misc chicken plasma protein misc hydrolysate misc plastein reaction misc response surface methodology misc Nutrition. Foods and food supply
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title	Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction
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title_full	Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction
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author_browse	Dandan Gao Penghui Guo Xin Cao Lili Ge Hongxin Ma Hao Cheng Yiqiang Ke Shien Chen Gongtao Ding Ruofei Feng Zilin Qiao Jialin Bai Nurul I. Nordin Zhongren Ma
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title_sort	improvement of chicken plasma protein hydrolysate angiotensin i‐converting enzyme inhibitory activity by optimizing plastein reaction
callnumber	TX341-641
title_auth	Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction
abstract	Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%.
abstractGer	Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%.
abstract_unstemmed	Abstract Chicken plasma protein hydrolysate (CPPH) was prepared by trypsin with angiotensin I‐converting enzyme (ACE) inhibitory activity of 53.5% ± 0.14% and the degree of hydrolysis (DH) of 16.22% ± 0.21% at 1 mg·ml−1; then, five proteases, including pepsin, trypsin, papain, alcalase, and neutrase, were employed to improve ACE inhibitory ability by catalyzing plastein reaction. The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. The results indicated that trypsin‐catalyzed plastein reaction increased ACE inhibitory activity of chicken plasma protein hydrolysates by 28.57%.
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title_short	Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction
url	https://doi.org/10.1002/fsn3.1572 https://doaj.org/article/04d7de312a4d41d8b687485b14125a46 https://doaj.org/toc/2048-7177
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up_date	2024-07-03T18:08:34.275Z
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The results indicated that trypsin‐catalyzed plastein reaction showed the highest ACE inhibitory activity. The exogenous amino acids of leucine, histidine, tyrosine, valine, and cysteine were selected to modify the CPPH. The leucine‐modified plastein reaction released the highest ACE inhibitory activity. The effects of four reaction parameters on plastein reaction were studied, and the optimal conditions with the purpose of obtaining the most powerful ACE inhibitory peptides from modified products were obtained by response surface methodology (RSM). The maximum ACE inhibition rate of the modified hydrolysate reached 82.07% ± 0.03% prepared at concentration of hydrolysates of 30%, reaction time of 4.9 hr, pH value of 8.0, temperature of 40°C, and E/S ratio of 5,681.62 U·g−1. 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Improvement of chicken plasma protein hydrolysate angiotensin I‐converting enzyme inhibitory activity by optimizing plastein reaction

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