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KMID : 0545120100200101415
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Journal of Microbiology and Biotechnology
2010 Volume.20 No. 10 p.1415 ~ p.1423
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Purification and Characterization of a Thermostable Xylanase from Fomitopsis pinicola
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Shin Keum
Marimuthu Jeya
Lee Jung-Kul
Kim Yeong-Suk
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Abstract
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An extracellular xylanase was purified to homogeneity by sequential chromatography of Fomitopsis pinicola culture supernatants on a DEAE-sepharose column, a gel filtration column, and then on a MonoQ column with fast protein liquid chromatography. The relative molecular weight of F. pinicola xylanase was determined to be 58 kDa by sodium dodecylsulfate polyacrylamide gel electrophoresis and by size exclusion chromatography, indicating that the enzyme is a monomer. The hydrolytic activity of the xylanase had a pH optimum of 4.5 and a temperature optimum of 70oC. The enzyme showed t1/2 value of 33 h at 70oC and catalytic efficiency (kcat = 77.4 s-1, kcat/Km = 22.7 mg/ml/s) for oatspelt xylan. Its internal amino acid sequences showed a significant homology with hydrolases from glycoside hydrolase (GH) family 10, indicating that the F. pinicola xylanase is a member of GH family 10.
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KEYWORD
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Fomitopsis pinicola, glycoside hydrolase, purification, thermostability, xylanase
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