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.
