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KMID : 0545119960060040238
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Journal of Microbiology and Biotechnology
1996 Volume.6 No. 4 p.238 ~ p.244
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Purification and Properties of γ-Glutamyl Transpeptidase from Bacillus sp. KUN-17
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HWANG, SE-YOUNG
RYANG, JUN-HWAN/LIM, WANG-JIN/YOO, ICK-DONG/OISHI, KUNIO
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Abstract
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γ-Glutamyl transpeptidase (γ-GTP; EC 2.3.2.2) present in the culture filtrate of Bacillus sp. KUN-17 was purified 400-fold through a consecutive procedure including organic precipitation and column chromatography. The enzyme has an estimated molecular weight of 70,000 and consists of hetero-subunits with molecular weight of 42,000 and 22,000. In vitro optimal conditions for those transfer and hydrolysis reactions appeared to be pH 7.0 at 50℃ and pH 8.4 at 40℃, respectively. The denatured enzyme recovered most of its γ-GTP activity by removing detergents such as sodium dodecyl sulfate (SDS) or urea with dialysis. The enzyme showed higher affinities against a number of amino as γ-glutamyl acceptors than glycylglycine in the following order; L-valine, L-methionine, L-glutamic acid or L-as-paragine, L-alanine. Also, it was shown that L-glutamin was the most suitable γ-glutamyldonor for the transfer reaction among those tested. Amino acids generally inhibited the enzyme activity for the transfer reaction, but not for hydrolysis reaction.
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