IDENTIFICATION AND CHARACTERIZATION OF MATRIX METALLOPROTEINASES FROM THE SARCOPLASMIC FRACTION OF COMMON CARP (CYPRINUS CARPIO) DARK MUSCLE

文献类型： 外文期刊

第一作者： Wu, Jiu-Lin

作者： Wu, Jiu-Lin;Cao, Min-Jie;Fu, Xiao-Ping;Liu, Guang-Ming;Su, Wen-Jin;Zhou, Li-Gen;Hara, Kenji

作者机构：

期刊名称：JOURNAL OF FOOD BIOCHEMISTRY （ 影响因子：2.72； 五年影响因子：2.543 ）

ISSN： 0145-8884

年卷期： 2009 年 33 卷 5 期

页码：

收录情况： SCI

摘要： Two gelatin hydrolyzing proteinases in the sarcoplasmic fraction of common carp muscle were detected using gelatin zymography. A comparative study shows that the gelatin hydrolyzing activity in dark muscle is obviously higher than that in white muscle. The enzymes can transform to their active forms after treated by aminophenylmercuric acetate, an activator of matrix metalloproteinases. Optimum pH and temperature of these enzymes were around 8.0 and 40C using gelatin as substrate. Metalloproteinase inhibitors (ethylenediaminetetraacetic acid and ethylene glycol-bis (2-aminoethylother)-N, N, N', N'-tetraacetic acid) completely suppressed the activities and 1,10-phenanthroline also showed great inhibitory effects. However, other proteinase inhibitors, such as soybean trypsin inhibitor, benzamidine, E-64 and pepstatin A, did not show any effect. Metal ions Ca2+ and Zn2+ are essential for these gelatinolytic activities. All these facts indicate that these proteinases are matrix metalloproteinases. Furthermore, these enzymes hydrolyze collagen effectively and maybe thus proposed to be responsible for the tenderization of fish muscle during the postmortem stage.

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