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Purification and characteristics of serine protease from the head of pacific white shrimp

文献类型: 外文期刊

作者: Wu, Yanyan 1 ; Wang, Ping 2 ; Li, Laihao 1 ; Yang, Xianqing 1 ; Diao, Shiqiang 1 ;

作者机构: 1.Chinese Acad Fishery Sci, S China Sea Fisheries Res Inst, Key Lab Aquat Prod Proc, Minist Agr, Guangzhou 510300, Guangdong, Peoples R China

2.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China

关键词: Pacific white shrimp;serine protease;purification;characteristics;enzyme activity

期刊名称:FOOD SCIENCE AND BIOTECHNOLOGY ( 影响因子:2.391; 五年影响因子:2.108 )

ISSN: 1226-7708

年卷期: 2012 年 21 卷 4 期

页码:

收录情况: SCI

摘要: Serine protease from the head of Pacific white shrimp was purified by the following techniques: ammonium sulfate fractionation, Q-Sepharose HP ion exchange chromatography, and Sephadex G-100 gel filtration. The molecular weight was estimated as 32.8 kDa using SDSPAGE. The optimum pH and temperature of the enzyme for the hydrolysis of casein were determined to be 10.0 and 40A degrees C. It was stable at pH range from 8.0 to 11.0 and had good thermal stability. Pb2+, Ca2+, Mg2+, Cu2+, and Mn2+ could active the enzyme certainly when Zn2+ and Hg2+ strongly inhibited the activity. The enzyme was inhibited by the general serine protease inhibitor (PMSF) and the specific trypsin inhibitors (TLCK, SBTI). The modification of various amino acid modifiers for the purified enzyme determined that the enzyme active center included tryptophan, histidine, and serine, moreover, arginine had a certain relationship with the enzyme activity.

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