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《集美大学学报（自然科学版）》[ISSN:1007-7405/CN:35-1186/N]

卷:

第18卷

期数:

2013年第4期

页码:

261-266

栏目:

水产科学与生物工程

出版日期:

2013-07-25

文章信息/Info

Title:

Identification and Characterization of a Collagenolytic Proteinase from the Skeletal Muscle of Common Carp(Cyprinus carpio)

作者:

王诚¹; 2; 张超群¹; 2; 吴海龙¹; 2; 黄身镰¹; 2; 曹敏杰¹; 2

(1.集美大学生物工程学院,福建 厦门 361021 ;2.福建省高校水产科学技术与食品安全重点实验室,福建 厦门 361021 )

Author(s):

WANG Cheng¹; 2; ZHANG Chao-qun¹; 2; WU Hai-long¹; 2; HUANG Shen-lian¹; 2; CAO Min-jie¹; 2

(1.College of Biological Engineering,Jimei University,Xiamen 361021,China;2.Key Laboratory of Science and Technology for Aquaculture and Food Safety（Jimei University），Fujian Province，Xiamen 361021，China)

关键词:

丝氨酸蛋白酶; 纯化; 降解; I型胶原蛋白

Keywords:

serine proteinase; purification; degradation; I collagen

分类号:

-

DOI:

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文献标志码:

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摘要:

    利用明胶酶谱法，在鲤鱼肌肉中检测到了一种具有分解胶原蛋白能力的丝氨酸蛋白酶.通过硫酸铵盐析、DEAE-Sephacel和Phenyl-Sepharose等一系列柱层析法，纯化得到了分子质量为70 ku，能够降解胶原蛋白的丝氨酸蛋白酶（Collagenolytic Serine Proteinase，CSP）.性质分析表明，CSP在弱碱性条件下显示活性，最适温度为30 ℃；丝氨酸蛋白酶抑制剂特异抑制CSP的活性.CSP能有效地分解鲤鱼肌肉中的I型胶原蛋白，提示其可能在鱼体死后肌肉胶原蛋白降解中发挥着重要的作用

Abstract:

A collagenolytic serine proteinases (CSP) from common carp muscle was identified and purified to high purity by ammonium sulfate fractionation and chromatographies on DEAE- Sephacel and Phenyl -Sepharose.The molecular mass of the CSP was 70 ku as estimated by SDS-PAGE.CSP revealed high activity at a slightly alkaline pH range and optimum temperature of 30 ℃.Serine proteinase inhibitors such as pefabloc SC ，leupeptin and benzamindine suppressed the activity of CSP specifically.CSP hydrolyzed type I collagen effectively ，indicating CSP was involved in the proteolytic breakdown of collagens in fish muscle during postmortem tenderization.

参考文献/References:

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相似文献/References:

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更新日期/Last Update: 2014-06-28