Purification and properties of β-galactosidase from Tilapia intestine: Digestive enzyme of Tilapia-X |
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| Authors: | Akiko YAMADA TANIGUCHI AND Katsumi TAKANO |
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| Affiliation: | Department of Brewing and Fermentation, Junior College of Tokyo University of Agriculture, Setagaya, Tokyo 156-8502;and Department of Applied Biology and Chemistry, Faculty of Applied Bioscience, Tokyo University of Agriculture, Setagaya, Tokyo 156-8502, Japan |
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| Abstract: | ABSTRACT: β-galactosidase of the intestine of Tilapia nilotica was purified by ammonium sulfate precipitation, followed by PAPTG-Sepharose 4B affinity chromatography, ethylenediamineetetraacetic acid ion-exchange chromatography, polyexchanger PBE 94 chromatofocusing, and Sephadex G-100 gel filtration. β-galactosidase was found to be a single band when examined by poly-acrylamide gel electrophoresis. The purifications of β-galactosidase were 27-fold from the crude extract. β-galactosidase showed optimum activity at pH 5.0 at 40°C, and was specifically found to be able to hydrolyze p -nitrophenyl β-galactopyranoside. It degrades galactan and agarose, and produces galactose. β-galactosidase was strongly inhibited by Hg2+ and PCMB. β-galactosidase is considered to be secreted by the upper and middle parts of the intestine and most of the activity was detected in the intestinal juice. |
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| Keywords: | β-galactosidase digestive enzyme enzymatic properties intestine purification Tilapia |
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