|本期目录/Table of Contents|

[1]陶志鹏,张凌晶,翁凌,等.鲍鱼肌原纤维结合型蛋白酶的初步鉴定[J].集美大学学报(自然科学版),2015,20(2):98-104.
　TAO Zhi-peng,ZHANG Ling-jing,WENG Ling,et al.Characterization of Myofibril-bound Proteinases from the Muscle of Abalone[J].Journal of Jimei University,2015,20(2):98-104.
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《集美大学学报（自然科学版）》[ISSN:1007-7405/CN:35-1186/N]

卷:
第20卷
期数:
2015年第2期
页码:
98-104
栏目:
水产、食品与生物工程
出版日期:
2015-03-25

文章信息/Info

Title:
Characterization of Myofibril-bound Proteinases from the Muscle of Abalone
作者:
陶志鹏1; 2; 张凌晶1; 2; 翁凌1; 2; 刘光明1; 2; 曹敏杰1; 2
1.集美大学食品与生物工程学院，福建 厦门 361021；2.福建省水产品深加工工程研究中心,福建 厦门 361021
Author(s):
TAO Zhi-peng1; 2; ZHANG Ling-jing1; 2; WENG Ling1; 2; LIU Guang-ming1; 2; CAO Min-jie1; 2
1.College of Food and Biological Engineering,Jimei University,Xiamen 361021,China; 2.Engineering Research Center for High Utilization of Aquatic Products,Xiamen 361021,China
关键词:
鲍鱼; 肌原纤维;  降解; 金属蛋白酶; 丝氨酸蛋白酶
Keywords:
abalone; myofibrillar proteins; degradation; metalloproteinase; serine proteinase
分类号:
-
DOI:
-
文献标志码:
A
摘要:
研究了皱纹盘鲍腹足肌肉中肌原纤维结合型蛋白酶对肌原纤维蛋白的降解作用.SDS-PAGE结果显示，肌原纤维在55~60 ℃下，肌球蛋白重链（Myosin Heavy Chain,MHC）和副肌球蛋白（Paramyosin,PM）会发生明显的降解.金属蛋白酶抑制剂EDTA、1，10-phenathroline能够有效抑制MHC和PM的分解.EDTA以及丝氨酸蛋白酶抑制剂benzamidine共同作用几乎可完全抑制蛋白质降解，揭示鲍鱼肌肉中存在肌原纤维结合型金属蛋白酶（Metalloproteinase,MP）和丝氨酸蛋白酶 (Serine proteinase,SP).通过加热、强离子浓度溶液抽提相结合的方式，从肌原纤维蛋白中初步分离出这两种酶.分别利用这两种酶对肌原纤维蛋白进行降解，发现最适温度均在60 ℃左右，与肌原纤维蛋白自身降解的最适温度（55~60 ℃）相吻合.对SP的底物特异性分析结果表明，制备的丝氨酸蛋白酶对P1位为Arg残基的荧光底物有较高的分解作用，而对P1位为Lys残基的底物分解较弱.
Abstract:
The effect of myofibril-bound proteinases on the degradation of myofibrillar proteins of abalone(Haliotis discus hannai) was studied.Myosin heavy chain (MHC) and paramyosin (PM) degraded obviously at 55~60 ℃ as indicated on SDS-PAGE,suggesting the existence of myofibril-bound proteinases in abalone muscle.Metalloproteinase inhibitors (EDTA,1,10phenathroline)effectively inhibited the degradation of MHC and PM.EDTA together with serine proteinase inhibitor benzamidine could completely suppress the degradation of MHC and PM,indicating the existence of metalloproteinase (MP) and serine proteinase (SP) in myofibrillar proteins.By heating treatment together with high ion concentration buffer treatment,MP and SP were extracted from myofibrillar proteins and both effectively degraded MHC and PM at optimal temperature of 60 ℃.Substrate specificity analysis of SP indicated that it hydrolyzed substrates containing arginine residue at P1 while those with lysine residue at P1 were slightly hydrolyzed.

参考文献/References:

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备注/Memo

备注/Memo:
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更新日期/Last Update: 2015-06-01