氧自由基吸收能力
化学
水解物
二肽基肽酶
酶
IC50型
抗氧化剂
生物化学
血管紧张素转换酶
二肽基肽酶-4
氨基酸
肽
色谱法
抗氧化能力
水解
体外
生物
内分泌学
糖尿病
2型糖尿病
血压
作者
Adriana Cunha Neves,Pádraigín A. Harnedy,Martina B. O’Keeffe,Richard J. Fitzgerald
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2016-09-12
卷期号:218: 396-405
被引量:154
标识
DOI:10.1016/j.foodchem.2016.09.053
摘要
The pH shift method was utilised for the recovery of proteins from salmon trimmings (ST), yielding 93% (w/w) protein. ST protein (STP) hydrolysates were generated with different enzyme preparations. STP incubated with Corolase PP for 1h (STP-C1) had the most potent angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory and oxygen radical absorbance capacity (ORAC) activities. Analysis of fractions of STP-C1 using UPLC-MS/MS identified sixteen peptides/amino acids. Tyr-Pro had the highest ACE inhibitory activity (ACE IC50=5.21±0.94μM). The highest DPP-IV inhibitory activity was found with the amino acid Tyr (DPP-IV IC50=75.15±0.84μM). Val-Pro had the highest ORAC activity (19.45±2.15μmol of TEg-1). To our knowledge, the peptides Gly-Pro-Ala-Val, Val-Cys, and Phe-Phe have not been previously identified to have the activities tested in this study. These results indicate that STP hydrolysates are potential sources of bioactive peptides.
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