An β-1, 4-Xylanase with Exo-Enzyme Activity Produced by Paenibacillus xylanilyticus KJ-03 and Its Cloning and Characterization
분야
자연과학 > 생물
저자
( Dong Ju Park ) , ( Yong Suk Lee ) , ( Jie Chang ) , ( Shu Jun Fang ) , ( Yong Lark Choi )
발행기관
한국미생물생명공학회(구 한국산업미생물학회)
간행물정보
Journal of Microbiology and Biotechnology 2013년, 제23권 제3호, 397~404페이지(총8페이지)
파일형식
05212234.pdf [무료 PDF 뷰어 다운로드]
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    영문초록
    Paenibacillus xylanilyticus KJ-03 was isolated from soil samples obtained from a field with Amorphophallus konjac plants. A gene encoding xylanase was isolated from KJ-03 and cloned using a fosmid library. The xynA gene encodes xylanase; it consists of 1,035 bp and encodes 345 amino acids. The amino acid sequence deduced from the P. xylanilyticus KJ-03 xylanase showed 81% and 69% identities with those deduced from the P. polymyxa E681 and Paenibacillus sp. HPL-001 xylanases, respectively. The xynA gene comprises a single domain, consisting of a catalytic domain of the glycosyl hydrolase (GH) 10 family. The xynA gene was expressed in Escherichia coli BL21 (trxB), and the recombinant xylanase was purified by Niaffinity chromatography. The purified xylanase showed optimum activity with birchwood xylan as a substrate at 40oC and pH 7.4. Treatment with Mg2+ and Li+ showed a slight decrease in XynA activity; however, treatment with 5 mM Cu2+ completely inhibited its activity. The results of the thin layer chromatography analysis indicated that the major hydrolysis product was xylobiose and small amounts of xylose and xylotriose. XynA showed increased activity with oat spelt xylan and birchwood xylan, but showed only slight activity with locust bean gum.
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