Hydrolysis of xyilans by a thermostable hybrid xylanase expressed in Escherichia coli.
Escherichia coli-expressed a hybrid xylanase, Btx, encoded by a designed hybrid xylanase gene Btx was purified. The molecular mass of the enzyme was estimated to be 22 kDa. The K(m) and k(cat) values for Btx were 1.9 mg/ml and 140 s(-1), respectively. It hydrolyzed xylan principally to xylobiose and xylotriose, and was functionally similar to family 11 xylanases. As some differences were found in the hydrolytic products between birchwood xylan and wheat bran insoluble xylan, the xylan binding domains in xylanase Btx must have different effects on soluble and insoluble xylan.
Department of Biological Science, College of Life Science, Zhejiang University, Hangzhou 310058, PR China.
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Weng
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Sun
D004926:Escherichia coli; D015870:Gene Expression; D006358:Hot Temperature; D006868:Hydrolysis; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D014990:Xylans / Q000737:chemistry* / Q000378:metabolism; D014995:Xylosidases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics
D011993:Recombinant Fusion Proteins; D014990:Xylans; D014995:Xylosidases