Characterization of β-galactosidase from an Antarctic <i>Bacillus</i> sp<i>.</i>

Abstract

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Antarctica is the coldest continent on the earth and harbours a variety of microorganisms. One of the bacterial isolates from cyanobacterial mats of Schirmacher Oasis, characterized as <i>Bacillus </i>sp. grew at 5-35^oC with an optima at 25^oC, and produced intracellular cold active <img src='/image/spc_char/beta.gif' border=0>-galactosidase. The maximum activity was recorded at <i>p</i>H 6.8 and 40^oC during late stationary phase. At 5^oC, the enzyme retained 39.7% activity and at 60^oC, became completely inactive within 15 min. The enzyme activity was stimulated by metal ions but was inhibited by ethylene diamine tetra acetic acid. Non-denaturing polyacylamide separation followed by <i>in situ</i> hydrolysis of 5-bromo-4-chloro-3-indolyl-<img src='/image/spc_char/beta.gif' border=0>-galactopyanoside, suggested the presence of isozymes. These properties of <img src='/image/spc_char/beta.gif' border=0>-galactosidase, indicate its potential use in removal of lactose from the milk for lactose intolerant people.

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