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Purification and Chemical Modification of the Xylanase from Alkali-tolerant Bacillus sp. YA-14

Authors
 Young Seo Park  ;  Do Young Yum  ;  Byoung Kwon Hahm  ;  Dong Hoon Bai  ;  Ju Hyun Yu 
Citation
 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, Vol.4(1) : 41-48, 1994 
Journal Title
 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 
ISSN
 1017-7825 
Issue Date
1994
Abstract
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 ρ−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 mg/ml and 5.0 mg/ml, 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.
Files in This Item:
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Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Neurosurgery (신경외과학교실) > 1. Journal Papers
Yonsei Authors
Kim, Dong Seok(김동석)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/143952
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