食品与发酵工业 >

2021 , Vol. 47 >Issue 2: 78 - 86

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.024125

研究报告

NaCl对添加丝氨酸蛋白酶的肌原纤维蛋白凝胶特性的影响

  • 陆益钡 ,
  • 吕春霞 ,
  • 廖慧琦 ,
  • 胡远辉 ,
  • 雷叶斯 ,
  • 曹少谦 ,
  • 杨华
展开
  • (浙江万里学院 生物与环境学院,浙江 宁波,315100)
硕士研究生(杨华教授为通讯作者,E-mail:yanghua@zwu.edu.cn)

收稿日期: 2020-04-02

  修回日期: 2020-09-03

  网络出版日期: 2021-02-07

基金资助

浙江省基金项目(LY17C200001);宁波市基金项目(2019A610431);国家海洋局项目(NBHY-2017-S2)

收起

Effects of NaCl on gel properties of myofibrillar protein supplemented with serine protease

  • LU Yibei ,
  • LYU Chunxia ,
  • LIAO Huiqi ,
  • HU Yuanhui ,
  • LEI Yesi ,
  • CAO Shaoqian ,
  • YANG Hua
Expand
  • (College of Biological & Environmental Sciences,Zhejiang Wanli University,Ningbo 315100,China)

Received date: 2020-04-02

  Revised date: 2020-09-03

  Online published: 2021-02-07

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摘要

以养殖大黄鱼作为研究对象,探究NaCl对添加了丝氨酸蛋白酶的肌原纤维蛋白凝胶特性的影响。首先对养殖大黄鱼肉经过提取分离纯化得到的丝氨酸蛋白酶进行研究,探讨其最适温度、最适pH以及NaCl对丝氨酸蛋白酶活性的影响。并进一步研究NaCl对含有丝氨酸蛋白酶的肌原纤维蛋白凝胶的质构特性、持水性、白度、拉曼光谱、荧光分析、微观结构等特性的影响。结果发现,丝氨酸蛋白酶的最适温度为50 ℃,最适pH值为7.0。NaCl的添加使肌原纤维蛋白凝胶的二级结构发生改变,蛋白凝胶结构越来越紧密稳定,但荧光强度相对有所下降。在NaCl质量浓度为0~20 g/L时,肌原纤维蛋白凝胶的胶黏性、咀嚼性不断上升,且白度增大。在NaCl添加量为40 g/L时,肌原纤维蛋白凝胶的持水性最强。因此可得出结论,添加NaCl后,丝氨酸蛋白酶的活性受到抑制,使其对肌原纤维蛋白凝胶的破坏减弱,从而改善鱼糜凝胶特性。

关键词： NaCl; 丝氨酸蛋白酶; 肌原纤维蛋白; 凝胶特性; 养殖大黄鱼

本文引用格式

陆益钡 , 吕春霞 , 廖慧琦 , 胡远辉 , 雷叶斯 , 曹少谦 , 杨华 . NaCl对添加丝氨酸蛋白酶的肌原纤维蛋白凝胶特性的影响[J]. 食品与发酵工业, 2021 , 47(2) : 78 -86 . DOI: 10.13995/j.cnki.11-1802/ts.024125

Abstract

Cultured Pseudosciaena crocea was used as the research object to explore the effect of NaCl on the gel properties of myofibrillar protein added with serine protease.Firstly,the serine protease obtained from the meat of cultured P.crocea was studied and the optimum temperature,optimum pH and the effects of NaCl on serine protease activity were analyzed.Furthermore,the effect of NaCl on the texture,water holding capacity,whiteness,Raman spectrum,fluorescence analysis and microstructure of myofibrillar protein gel containing serine protease were further studied.The results showed that the optimum temperature and pH value of serine protease were 50 ℃ and 7.0 respectively.With the addition of NaCl,the secondary structure of myofibrillar protein gel was changed,and the structure of myofibrillar gel became more compact and stable,but the fluorescence intensity decreased.When the addition of NaCl was at 0%-2%,the gumminess and chewiness of myofibrin gel increased continuously,and the whiteness increased.When the addition of NaCl was 4%,myofibrillar protein gel had the strongest water holding capacity.Therefore,it can be concluded that with the addition of NaCl,the activity of serine protease is inhibited,which weakens the damage of serine protease to myofibrillar protein gel,thus improving the gel properties of surimi.

Key words： NaCl; serine protease; myofibrin; gel properties; cultured Pseudosciaena crocea

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