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KMID : 1007520120210041129
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Food Science and Biotechnology
2012 Volume.21 No. 4 p.1129 ~ p.1134
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Purification and Characteristics of Serine Protease from the Head of Pacific White Shrimp
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Wu Yan-yan
Wang Ping
Li Lai-hao
Yang Xian-qing
Diao Shi-qiang
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Abstract
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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 40˚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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KEYWORD
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Pacific white shrimp, serine protease, purification, characteristics, enzyme activity
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