期刊
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
卷 20, 期 10, 页码 1415-1423出版社
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
DOI: 10.4014/jmb.1003.03031
关键词
Fomitopsis pinicola; glycoside hydrolase; purification; thermostability; xylanase
资金
- Korea Forest Service [S210707L010120]
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 mass of the E pinicola xylanase was determined to be 58 kDa by sodium dodecyl sulfate 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 70 degrees C. The enzyme showed a t(1/2) value of 33 h at 70 degrees C and catalytic efficiency (k(cat)=77.4 s(-1), k(cat)/K-m=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 E pinicola xylanase is a member of GH family 10.
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