文献类型：期刊文献

中文题名：凡纳滨对虾内源蛋白酶对肌原纤维蛋白的降解作用

英文题名：Degradation of myofibrillar protein by endogenous proteases from Litopenaeus vannamei

作者：陈诗妍[1];吉宏武[1,2,3];李承勇[1,3];苏伟明[1,3];郝记明[1];黄杰恒[1]

机构：[1]广东海洋大学食品科技学院,广东湛江524088;[2]水产品深加工广东省普通高校重点实验室,广东湛江524088;[3]广东省水产品加工与安全重点实验室,广东湛江524088

年份：2015

卷号：36

期号：5

起止页码：149

中文期刊名：食品工业科技

外文期刊名：Science and Technology of Food Industry

收录：CSTPCD、、北大核心2014、北大核心、CSCD_E2015_2016、CSCD

基金：国家虾产业技术体系建设专项资金(CARS-47);广东省海洋渔业科技攻关重大项目(A201008102);广东省科技团队项目(2011A020102005);广东海洋渔业科技推广专项科技攻关与研发项目(A201209C02)

语种：中文

中文关键词：凡纳滨对虾;内源蛋白酶;肌原纤维蛋白;肌肉软化;胰蛋白酶

外文关键词：Litopenaeus vannamei; endogenous proteases; myofibrillar protein ; muscle softening ; trypsin

中文摘要：为确定引起凡纳滨对虾自溶的主要酶类及分布部位,本文测定了凡纳滨对虾各内源蛋白酶的活性,分析主要内源蛋白酶贮藏期间的变化,并比较主要内源蛋白酶对虾肌原纤维蛋白的降解作用。结果显示,虾头蛋白酶活达90.17U/mg,是虾肉的300倍。虾头中的胰蛋白酶活性最高,达13.59U/mg。全虾贮藏4d后虾肉总酶活和胰蛋白酶活增加,于第8d虾肉第一腹节总酶活增至1.66U/mg,胰蛋白酰胺酶和酯酶活分别达到0.97U/mg和1.84U/mg。SDSPAGE结果显示,随贮藏温度和时间的增大,内源酶对肌原纤维蛋白的肌球蛋白重链(MHC)和肌动蛋白(Actin)降解程度越大,其中虾头中胰蛋白酶对肌原纤维蛋白的降解作用最强。因此凡纳滨对虾胰蛋白酶很可能是肌肉软化的主要作用酶。

外文摘要：In order to determine the endogenous protease that results in muscle softening and its distribution in Litopenaeus vannamei, different endogenous proteases activities from the shrimp were examined,as well as the changes of main proteases during ice storage and the proteolytic degradation of myofibrillar protein by endogenous proteases were monitored in this study.Results showed that proteolytic activity in the shrimp head was up to 90.17U/mg, 300 times higher than that in muscle. In shrimp head, the trypsin was the most important proteinase,with 13.59U/rag activities. In addition, the increase of total proteolytic and trypsin activities in shrimp muscle were detected after 4 days of storage, and the total proteolytic activity in first segments increased to 1.66U/mg after 8 days of storage,while trypsin activities were 0.97U/mg and 1.84U/mg when BApNA and TAME were used as substrate, respectively.In the results of SDS-PAGE,the degradation of MHC and Actin in myofibrillar protein by endogenous proteases was enhanced with increasing storage temperature and time.Among them,the trypsin had the most remarkable effect on the degradation of myofibrillar protein.Therefore,these results indicated that the release of trypsin from Litopenaeus vannamei shrimp head was most likely responsible for the undesirable softening of the shrimp muscle during post-mortem storage.