研究报告

中国毛虾二肽基肽酶-IV抑制肽的分离纯化与结构鉴定

  • 孙洁 ,
  • 李燕 ,
  • 郑昌亮 ,
  • 汪之和
展开
  • (上海海洋大学 食品学院,上海,201306)
第一作者:硕士研究生(汪之和教授为通信作者,E-mail:zhwang@shou.edu.cn)

收稿日期: 2022-03-20

  修回日期: 2022-05-06

  网络出版日期: 2023-02-14

基金资助

国家重点研发计划项目(2019YFD0902000)

Purification and identification of dipeptidyl peptidase-IV inhibitory peptide from Acetes chinensis hydrolysates

  • SUN Jie ,
  • LI Yan ,
  • ZHENG Changliang ,
  • WANG Zhihe
Expand
  • (College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China)

Received date: 2022-03-20

  Revised date: 2022-05-06

  Online published: 2023-02-14

摘要

食源性二肽基肽酶-IV(dipeptidyl peptidase-IV,DPP-IV)抑制肽有助于调节机体血糖。为实现中国毛虾的高值化利用,从中国毛虾酶解产物中制备DPP-IV抑制肽,使用动物蛋白酶水解中国毛虾,以DPP-IV抑制率为评价指标分离多肽,并通过分子对接确定抑制作用位点。结果表明,酶解液经超滤、Sephadex G15和反相高效液相色谱分离纯化和液相-质谱联用技术鉴定后,得到了5条DPP-IV抑制肽,氨基酸序列分别为YGGQFPTRPD、PALPSIPH、IFTAPQVP、PAFPHPLP和LGDAPGEVP;其中PALPSIPH和PAFPHPLP对DPP-IV的抑制活性较高,二者的IC50值分别为(2.68±0.06)和(1.61±0.06) mmol/mL。分子对接结果表明PALPSIPH和PAFPHPLP主要通过氢键与DPP-IV活性中心及其以外的位点相结合,以此达到抑制作用。该研究基于中国毛虾制备食源性DPP-IV抑制肽,为水产蛋白来源降血糖功能性食品开发利用和新型DPP-IV抑制肽的研究提供参考。

本文引用格式

孙洁 , 李燕 , 郑昌亮 , 汪之和 . 中国毛虾二肽基肽酶-IV抑制肽的分离纯化与结构鉴定[J]. 食品与发酵工业, 2023 , 49(1) : 160 -167 . DOI: 10.13995/j.cnki.11-1802/ts.031672

Abstract

Food-derived dipeptidyl peptidase-IV (DPP-IV) inhibitory peptides can help regulate blood sugar in the body. To realize the high-value utilization of Acetes chinensis, DPP-IV inhibitory peptide was extracted from A. chinensis by animal protease. The peptides were separated according to the DPP-IV inhibition rate, and the inhibition sites were determined by molecular docking. The results showed that after the enzymatic hydrolysate was separated and purified by ultrafiltration, Sephadex G15, and reversed-phase high performance liquid chromatography, and identified by liquid chromatography-mass spectrometry, five DPP-IV inhibitory peptides were obtained, and their amino acid sequences were identified as YGGQFPTRPD, PALPSIPH, IFTAPQVP, PAFPHPLP, and LGDAPGEVP, respectively. Among those amino acid sequences, PALPSIPH and PAFPHPLP had higher inhibitory activities on DPP-IV, and their IC50 values were (2.68±0.06) and (1.61±0.06) mmol/mL, respectively. Molecular docking results showed that PALPSIPH and PAFPHPLP were mainly combined with the active center of DPP-IV and its other sites through hydrogen bonds, so as to achieve the inhibitory effect. The results provide a reference for the development and utilization of hypoglycemic functional foods from aquatic-protein source and the research of novel DPP-IV inhibitory peptides.

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