PURIFICATION AND CHARACTERIZATION OF CHYMOTRYPSIN FROM PENAEUS VANNAMEI (CRUSTACEA: DECAPODA) |
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| Authors: | PATRICIA HERNÁNDEZ-CORTÉS JOHN R WHITAKER FERNANDO LUIS GARCÍA-CARREÑO |
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| Affiliation: | Department of Physiological Botany University of Uppsala Villavägen 6, Uppsala, Sweden;Department of Food Science and Technology University of California;Centro de Investigaciones Biologicas del Noroeste P.O. Box 128 La Paz, BCS 23000 Mexico |
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| Abstract: | The purification and characterization of a chymotrypsin from the hepatopan-creas of the white shrimp Penaeus vannamei is described. Only one chymotrypsin was detected in contrast to other shrimp that have two major forms. P. vannamei chymotrypsin has a molecular mass of 33.2 kDa and a pI of 3.1. The molecular mass is high relative to other penaeid chymotrypsins. The proteinase is acid labile and exhibits optimum activity at pH 8. The enzyme is thermostable both at 25 and 37C. It is a serine proteinase. Phenylmethylsulphonyl fluoride and soybean trypsin inhibitor blocked the activity of the enzyme, and it was not affected by chymotrypsin inhibitors such as tosyl-PheCH2Cl or benzyloxycarbonyl-Phe-CH2Cl. Protein profiles of the hepatopancreas from two populations varied |
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