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基于表面等离子体共振技术筛选马氏珠母贝肉酶解产物中血管紧张素转换酶抑制肽

夏小雨 高加龙 温财兴 曹文红 秦小明 李钰金 林海生 陈忠琴 郑惠娜 朱国萍

食品科学2025,Vol.46Issue(7):143-150,8.
食品科学2025,Vol.46Issue(7):143-150,8.DOI:10.7506/spkx1002-6630-20241008-016

基于表面等离子体共振技术筛选马氏珠母贝肉酶解产物中血管紧张素转换酶抑制肽

Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance

夏小雨 1高加龙 1温财兴 2曹文红 1秦小明 1李钰金 3林海生 1陈忠琴 1郑惠娜 1朱国萍1

作者信息

  • 1. 广东海洋大学食品科技学院,广东 湛江 524088||国家贝类加工技术研发分中心(湛江),广东省水产品加工与安全重点实验室,广东省海洋生物制品工程实验室,水产品深加工广东普通高校重点实验室,广东 湛江 524088
  • 2. 广东海洋大学食品科技学院,广东 湛江 524088
  • 3. 中国海洋大学食品科学与工程学院,山东 青岛 266003
  • 折叠

摘要

Abstract

Surface plasmon resonance(SPR)technology was used to analyze the binding of the three ultrafiltration fractions of the protein hydrolysate of Pinctada martensii(PHPM)with angiotensin I converting enzyme(ACE)as a protein ligand.The amino acid sequences of the bound peptides were identified by mass spectrometry(MS)and those with strong inhibitory potential against ACE were selected and synthesized.The in vitro ACE inhibitory activity and inhibition type of the peptides were studied as well as their interaction with ACE.It was found that the ultrafiltration fraction with a molecular mass of 3 000-5 000 Da had a strong binding signal to ACE.Among the four synthesized ACE inhibitory peptides,SLPWPMKPMNLIE had the lowest 50%inhibitory concentration(IC50)value and bound to the hydrophobic pocket of the C domain in ACE through hydrogen bonding.

关键词

马氏珠母贝/血管紧张素转换酶抑制肽/表面等离子体共振/酶抑制动力学/分子对接

Key words

Pinctada martensii/angiotensin I converting enzyme inhibitory peptide/surface plasmon resonance/enzymatic inhibition kinetics/molecular docking

分类

轻工纺织

引用本文复制引用

夏小雨,高加龙,温财兴,曹文红,秦小明,李钰金,林海生,陈忠琴,郑惠娜,朱国萍..基于表面等离子体共振技术筛选马氏珠母贝肉酶解产物中血管紧张素转换酶抑制肽[J].食品科学,2025,46(7):143-150,8.

基金项目

贝类产业技术体系项目(CARS-49) (CARS-49)

湛江市科技计划项目(230906164548720) (230906164548720)

山东省重点扶持区域紧缺人才项目(鲁发改动能办[2024]658号) (鲁发改动能办[2024]658号)

食品科学

OA北大核心

1002-6630

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