食品科学 ›› 2013, Vol. 34 ›› Issue (9): 336-339.doi: 10.7506/spkx1002-6630-201309067

• 专题论述 • 上一篇    下一篇

鱼类肌原纤维结合型丝氨酸蛋白酶研究进展

杜翠红,曹敏杰*   

  1. 集美大学生物工程学院,福建 厦门 361021
  • 收稿日期:2013-03-14 修回日期:2013-04-16 出版日期:2013-05-15 发布日期:2013-05-07
  • 通讯作者: 曹敏杰 E-mail:cuihongdu@jmu.edu.cn
  • 基金资助:

    国家自然科学基金面上项目(30571450;20872049)

Progress in Research on Myofibril-bound Serine Proteinase from Fish

DU Cui-hong,CAO Min-jie*   

  1. College of Biological Engineering, Jimei University, Xiamen 361021, China
  • Received:2013-03-14 Revised:2013-04-16 Online:2013-05-15 Published:2013-05-07
  • Contact: CAO Min-jie E-mail:cuihongdu@jmu.edu.cn

摘要:

本文综述鱼类肌原纤维结合型丝氨酸蛋白酶(myofibril-bound serine proteinase,MBSP)的分离纯化、酶学特性、分子生物学及基因重组表达等方面的研究进展。鱼类MBSP是一种弱碱性蛋白酶,它普遍存在于鱼类肌肉中。MBSP降解肌原纤维蛋白是造成鱼糜凝胶劣化的主要原因。同时,由于鱼类MBSP具有良好的热稳定性及对精氨酸或赖氨酸残基羧基端特异分解的底物特异性,因此,该蛋白酶有望开发成为一种新颖的工具酶应用于蛋白质质谱鉴定等研究领域。

关键词: 肌原纤维结合型丝氨酸蛋白酶, 分离纯化, 酶学特性, 分子克隆, 重组表达

Abstract:

This paper reviews the recent progress in the purification, characterization, molecular cloning and recombinant
expression of myofibril-bound serine proteinases (MBSP) from different species of fish. As a weakly alkaline proteinase,
MBSP is extensively found in fish skeletal muscles. The degradation of myofibrillar proteins by MBSP is mainly resposible
for the modori phenomenon during fish surimi production. From this reviwe, we conclude that fish-derived MBSP hold great
promise as a novel tool in mass spectrometric identification of proteins due to their excellent stablity to heat and substrate
specificity to decompose the carboxyl chains of arginine or lysine residues.

Key words: myofibril-bound serine proteinase, purification, characterization, molecular cloning, recombination expression

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