AI Article Synopsis
- An extracellular xylanase enzyme was effectively purified from Fomitopsis pinicola using a series of chromatography methods, leading to a highly purified product.
- The purified enzyme has a molecular weight of 58 kDa, exists as a monomer, and exhibits optimal activity at a pH of 4.5 and a temperature of 70°C.
- The xylanase demonstrates significant hydrolytic efficiency with a half-life of 33 hours and shares amino acid sequence similarities with the hydrolases in glycoside hydrolase family 10, confirming its classification in this family.
Article Abstract
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 70 degreesC. The enzyme showed 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 F. pinicola xylanase is a member of GH family 10.
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| http://dx.doi.org/10.4014/jmb.1003.03031 | DOI Listing |
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