金枪鱼暗色肉酶解优势肽鉴定及其体外抗氧化和血管紧张素转换酶抑制活性分析

doi:10.7506/spkx1002-6630-20191102-015

食品科学 ›› 2020, Vol. 41 ›› Issue (23): 91-99.doi: 10.7506/spkx1002-6630-20191102-015

金枪鱼暗色肉酶解优势肽鉴定及其体外抗氧化和血管紧张素转换酶抑制活性分析

王锐，张迪雅，李晔，苏秀榕

（1.宁波大学海洋学院，浙江宁波 315211；2.宁波大学食品与药学学院，浙江宁波 315211）

出版日期:2020-12-15 发布日期:2020-12-28
基金资助:
国家海洋局2016年海洋经济创新发展区域示范项目；宁波大学科研创新基金项目（IF2020001）

Identification of Dominant Peptides from Hydrolyzed Tuna Dark Muscle and Their Antioxidant and Angiotensin-Converting Enzyme Inhibitory Activities

WANG Rui, ZHANG Diya, LI Ye, SU Xiurong

(1. School of Marine Sciences, Ningbo University, Ningbo 315211, China;2. College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo 315211, China)

Online:2020-12-15 Published:2020-12-28

摘要/Abstract

摘要： 为获得高活性功能多肽，实现水产蛋白资源的高值化利用，本研究在单因素试验的基础上，结合响应面试验，优化金枪鱼暗色肉胰蛋白酶与碱性蛋白酶双酶酶解条件。将所得的酶解液通过基质辅助激光解离飞行时间串联质谱仪进行多肽分子质量测定，利用Discovery Studio中CDocker模块对其中的优势肽进行功能预测，并进一步采用体外活性实验比较酶解液和合成多肽对1,1-二苯基-2-苦基肼（1,1-diphenyl-2-picrylhydrazyl，DPPH）自由基清除活性和对血管紧张素转换酶（angiotensin-converting enzyme，ACE）抑制活性的差异。结果表明，金枪鱼暗色肉在双酶质量比1∶1、固液比1∶4、加酶量2%、酶解温度51 ℃和酶解时间5 h条件下，获得61.01%的最佳水解度。经分子对接发现，优势肽为VSSK和EPR，可与具有抗氧化功能相关的Kelch样环氧氯丙烷相关蛋白-1（Kelch-like ECH-associated protein 1，Keap1）和降血压相关的ACE对接。体外实验进一步证明酶解液的DPPH半抑制浓度（half maximal inhibitory concentration，IC50）为0.204 mg/mL，ACE IC50为2.321 mg/mL；合成多肽VSSK的DPPH IC50为3.050 mg/mL，ACE IC50为2.914 mg/mL；合成多肽EPR的DPPH IC50为3.368 mg/mL，ACE IC50为4.857 mg/mL；酶解液比合成多肽具有更好的抗氧化活性和ACE抑制活性。本研究结果可为金枪鱼暗色肉高值化利用提供理论参考。

关键词: 金枪鱼暗色肉；酶解液；多肽；分子对接；体外活性

Abstract: In order to obtain highly bioactive peptides and to achieve high-valued utilization of aquatic product proteins, this study determined the optimal conditions for the hydrolysis of tuna dark muscle by a mixture of trypsin and alcalase using combination of one-factor-at-a-time method and response surface methodology. The molecular mass of peptides in the prepared hydrolysate was measured by matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry (MALDI-TOF MS/MS), and the functions of the dominant peptides were predicted using the CDocker module in Discovery Studio. The 1,1-diphenyl-2-picrylhydrazyl (DPPH) free radical scavenging capacity and angiotensin-converting enzyme (ACE) inhibitory activity of the peptides synthetized in vitro were compared with those of the hydrolysate. The optimal processing conditions that provided maximal degree of hydrolysis of 61.01% were determined as 1:1, 1:4, 51 ℃, 2% and 5 h for mass ratio between the two enzymes, solid-to-liquid ratio, hydrolysis temperature, enzyme concentration and time, respectively. Molecular docking showed that the dominant peptides VSSK and EPR could separately bind to Kelch-like ECH-associated protein 1 (Keap1) and ACE to exert antioxidant and hypotensive effects, respectively. Further, in vitro tests showed that the half maximal inhibitory concentration (IC50) values of the hydrolysate, VSSK and EPR were 0.204, 3.050 and 3.368 mg/mL for DPPH radical scavenging activity; and 2.321, 2.914 and 4.857 mg/mL for ACE inhibitory activity, respectively. These data illustrated that the hydrolysate had stronger antioxidant and hypotensive effects. The results of this study provide a theoretical basis for the high-value utilization of tuna dark muscle.

Key words: tuna dark muscle; hydrolysis; polypeptide; molecular docking; in vitro activity

中图分类号:

TS254.9

王锐，张迪雅，李晔，苏秀榕. 金枪鱼暗色肉酶解优势肽鉴定及其体外抗氧化和血管紧张素转换酶抑制活性分析[J]. 食品科学, 2020, 41(23): 91-99.

WANG Rui, ZHANG Diya, LI Ye, SU Xiurong. Identification of Dominant Peptides from Hydrolyzed Tuna Dark Muscle and Their Antioxidant and Angiotensin-Converting Enzyme Inhibitory Activities[J]. FOOD SCIENCE, 2020, 41(23): 91-99.

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金枪鱼暗色肉酶解优势肽鉴定及其体外抗氧化和血管紧张素转换酶抑制活性分析

Identification of Dominant Peptides from Hydrolyzed Tuna Dark Muscle and Their Antioxidant and Angiotensin-Converting Enzyme Inhibitory Activities

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