组织蛋白酶 L 参与鲤鱼（Cyprinus carpio）鱼糜凝胶的调制现象。

Participation of cathepsin L in modori phenomenon in carp (Cyprinus carpio) surimi gel.

机构信息

Department of Food Science and Nutrition, Zhejiang University, Hangzhou 310058, Zhejiang Province, China.

出版信息

Food Chem. 2012 Oct 15;134(4):2014-20. doi: 10.1016/j.foodchem.2012.04.060. Epub 2012 Apr 19.

DOI:10.1016/j.foodchem.2012.04.060

Abstract

Cathepsin L (Cat L) in carp (Cyprinus carpio) dorsal muscles was purified and its molecular weight determined by SDS polyacrylamide gel electrophoresis (SDS-PAGE) was 36 kDa. Its optimal temperature and pH were 50 °C and 5.5, respectively. The results of the effects of specific substrates, activators and inhibitors on the enzymatic activity showed that Cat L belongs to the family of cysteine proteinases containing thiol. Compared to the control, the gel strength of surimi with the addition of purified Cat L decreased significantly by 24.33% while that of surimi with both purified Cat L and inhibitors increased by 13.7% and 21.6%, respectively, suggesting the participation of Cat L in the modori phenomenon occurring in carp surimi. Both the SDS-PAGE electrophoretic pattern and microstructure figure revealed that Cat L could hydrolyse the main protein in carp surimi and was one of the enzymes involved in the modori phenomenon.

摘要

鲤鱼（Cyprinus carpio）背肌组织中的组织蛋白酶 L（Cat L）经 SDS 聚丙烯酰胺凝胶电泳（SDS-PAGE）纯化后，其分子量为 36 kDa。其最适温度和 pH 值分别为 50°C 和 5.5。特异性底物、激活剂和抑制剂对酶活性影响的结果表明，Cat L 属于含巯基的半胱氨酸蛋白酶家族。与对照组相比，添加纯化的 Cat L 的鱼糜凝胶强度显著降低了 24.33%，而同时添加纯化的 Cat L 和抑制剂的鱼糜凝胶强度分别增加了 13.7%和 21.6%，这表明 Cat L 参与了鲤鱼鱼糜发生的 gel 劣化现象。SDS-PAGE 电泳图谱和微观结构图像均表明，Cat L 可以水解鲤鱼鱼糜中的主要蛋白，是参与 gel 劣化现象的酶之一。