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KMID : 1007519930020010019
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Food Science and Biotechnology
1993 Volume.2 No. 1 p.19 ~ p.21
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Enzymatic Properties of Cyclodextrin Glycosyltransferase from Alkalophilic Bacillus sp. (Ⅱ)
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Chung, Yong-Joon
Yum, Do-Young/Yu, Ju-Hyun
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Abstract
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The effect of various metal ions and chemical reagents for protein modification on the ingibition of the CGTase from alkalophilic Bacillus sp. TC-335 was studied to elucidate some properties of the active site. Among these metals, HgCl₂ reacted with sulfhydryl groups of the enzyme to form the inactive forms of the enzyme. The enzyme was not inhibited by serine inhibitors such as phenyl methyl sulfur fluoride (PMSF) and sulfhydryl reagent such as p-chloromercuribenzoate (p-CMB). The enzyme was found to be inactivated by I₂, iodoacetate and photooxidation, which indicated the possible involvement of tyrosine, histidine residues in the active center of the enzyme.
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