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《Journal of Jimei University(Natural Science)》 2010-04
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Purification and Characterization of Serine Proteinase from Pacific White Shrimp

WENG Ling1,LI Teng2,YIN Li-hua1,SUN Le-chang1,SU Wen-jin1,CAO Min-jie1 (1. School of Biotechnology Engineering,Jimei University,Xiamen 361021,China; 2. College of Food Science and Technology,Shanghai Ocean University,Shanghai 201306,China)  
A serine proteinase from the hepatopancreas of Pacific white shrimp was purified by a series of procedures,including ammonium sulfate precipitation,column chromatographies on DEAE-Sepharose, Phenyl-Sepharose,Hydroxyapatite and Superdex 75. Purified serine proteinase revealed a single band on SDS-PAGE. The molecular weight was about 28 ku,The optimum pH and temperature of the enzyme were 9. 0 and 40 ℃,respectivety. The enzyme was stable up to 35 ℃ and in the pH range from 7. 0 to 10. 0. Substrate specificity and inhibitor sensitivity experiments suggested that the enzyme was a trypsin-type serine proteinase. Kinetic constants of Km was 0. 69 μmol/L,Kcat was 0. 33 S-1 and Kcat /Km was 4. 78 × 105 (mol/ L)-1S-1 using Boc-Phe-Ser-Arg-MCA as substrate.
【Fund】: 十一五国家科技支撑计划重大项目(2008BAD94B01);; 福建省高校水产科学技术与食品安全重点实验室基金资助项目(2008J401)
【CateGory Index】: S917.4
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