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http://dx.doi.org/10.3746/jkfn.2002.31.1.050

Purification and Characterization of the β-Galactosidase from Edible Snail  

윤경영 (영남대학교 식품영양학과)
김광수 (영남대학교 식품영양학과)
Publication Information
Journal of the Korean Society of Food Science and Nutrition / v.31, no.1, 2002 , pp. 50-56 More about this Journal
Abstract
The $\beta$-galactosidase was purified from the internal organs of edible snail by fractionation with ammonium sulfate, ion exchange chromatography on DEAE-Sephadex, Mono Q HR 5/5 and gel filtration on Sephacryl S-200. Superose 12 HR 10/30 chromatography. The specific activity of the purified $\beta$-galactosidase was 18.8 units/mg protein with 31.3 purification fold from crude extract. The $\beta$-galactosidase had native molecular weight of 144,000 dalton and was composed of two subunits of 72,000 dalton. The isoelectric point of the enzyme was determined 4.1. This enzyme was the most active at pH 3.0 and 6$0^{\circ}C$, and was stable in the pH range 2.0~8.0 and below 5$0^{\circ}C$. The enzyme was inhibited by metal ions and sugars such as fructose, glucose, galactose, maltose and xylose.
Keywords
$\beta$-galactosidase; edible snail; purification;
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