A Novel Alkaliphilic Xylanase from the Newly Isolated Mesophilic Bacillus sp MX47: Production, Purification, and Characterization

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A newly isolated bacterial strain, Bacillus sp. MX47, was actively producing extracellular xylanase only in xylan-containing medium. The xylanase was purified from the culture broth by two chromatographic steps. The xylanase had an apparent molecular weight of 26.4 kDa with an NH2-terminal sequence (Gln-Gly-Gly-Asn-Phe) distinct from that of reported proteins, implying it is a novel enzyme. The optimum pH and temperature for xylanase activity were 8.0 and 40 A degrees C, respectively. The enzyme activity was severely inhibited by many divalent metal ions and EDTA at 5 mM. The xylanase was highly specific to beechwood and oat spelt xylan, however, not active on carboxymethyl cellulose (CMC), avicel, pectin, and starch. Analysis of the xylan hydrolysis products by Bacillus sp. MX47 xylanase indicated that it is an endo-beta-1,4-xylanase. It hydrolyzed xylan to xylobiose as the end product. The K (m) and V (max) values toward beechwood xylan were 3.24 mg ml(-1) and 58.21 mu mol min(-1) mg(-1) protein, respectively.
Publisher
HUMANA PRESS INC
Issue Date
2012-10
Language
English
Article Type
Article
Keywords

SP-NOV.; PUMILUS; SUBTILIS; SEQUENCE

Citation

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, v.168, no.4, pp.899 - 909

ISSN
0273-2289
DOI
10.1007/s12010-012-9828-z
URI
http://hdl.handle.net/10203/102995
Appears in Collection
CBE-Journal Papers(저널논문)
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