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KMID : 0545119940040010041
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Journal of Microbiology and Biotechnology
1994 Volume.4 No. 1 p.41 ~ p.48
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Purification, Characterization and Chemical Modification of the Xylanase from Alkali-tolerant Bacillus sp. YA-14
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Park, Young Seo
Yum, Do Young/Hahm, Byoung Kwon/Bai, Dong Hoon/Yu, Ju Hyun
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Abstract
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The xylanase from alkali-tolerant Bacillus sp. YA-14 was purified to homogeneity by CM-cellulose, Sephadex G-50, and hydroxyapatite column chromatographies. The molecular weight of the purified enzyme was estimated to be 20,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme slightly hydrolyzed carboxymethyl cellulose and Avicel, but did not hydrolyze soluble starch, dextran, pullulan, and p-nitrophenyl-β-D-xylopyranoside. The maximum degree of hydrolysis by enzyme for birchwood xylan and oat spelts xylan were 47 and 40%, respectively. The Michaelis constants for birchwood xylan and oat spelts xylan were calculated to be 3.03 ㎎/㎖ and 5.0 ㎎/㎖, respectively. The activity of the xylanase was inhibited reversibly by HgCl_2, and showed competitive inhibition by N-bromosuccinimide, which probably indicates the involvement of tryptophan residue in the active center of the enzyme. The Xylanase was identified to be xylose-producing endo-type xylanase and did not show the enzymatic activities which cleave the branch point of the xylan structure.
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