Hydrolysis of xylans by a thermostable hybrid xylanase expressed in Escherichia coli
| Autor: | J. Y. Sun, X. Y. Weng |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
animal structures
biology Molecular mass Chemistry technology industry and agriculture food and beverages Xylan binding Xylose biology.organism_classification complex mixtures Applied Microbiology and Biotechnology Biochemistry Xylan carbohydrates (lipids) Hydrolysis chemistry.chemical_compound Escherichia Xylobiose Xylanase |
| Zdroj: | Applied Biochemistry and Microbiology. 46:511-514 |
| ISSN: | 1608-3024 0003-6838 |
| DOI: | 10.1134/s000368381005008x |
| Popis: | 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 Km and kcat 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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