鲤鱼肌肉中胶原蛋白酶的分离纯化与性质分析 |
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引用本文: | 王诚,张超群,吴海龙,黄身镰,曹敏杰.鲤鱼肌肉中胶原蛋白酶的分离纯化与性质分析[J].厦门水产学院学报,2013(4):261-266. |
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作者姓名: | 王诚 张超群 吴海龙 黄身镰 曹敏杰 |
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作者单位: | [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 |
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基金项目: | 国家自然科学基金资助项目(31071519) |
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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.
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关 键 词: | 丝氨酸蛋白酶 纯化 降解 I型胶原蛋白 |
Identification and Characterization of a Collagenolytic Proteinase from the Skeletal Muscle of Common Carp (Cyprinus carpio) |
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Authors: | WANG Cheng ZHANG Chao-qun WU Hai-long HUANG Shen-lian CAO Min-jie |
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Institution: | 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) |
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Abstract: | A collagenolytic serine proteinases (CSP) from common carp muscle was identified and puri-fied 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 activ-ity at a slightly alkaline pH range and optimum temperature of 30 ℃. Serine proteinase inhibitors such as pe-fabloc 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 dur-ing postmortem tenderization. |
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Keywords: | serine proteinase purification degradation Ⅰ collagen |
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