Cloning, Expression, and Characterization of a New Xylanase from Alkalophilic Paenibacillus sp. 12-11
| Autor: | Hui Ying Luo, Kun Meng, Huo Qing Huang, Pei Long Yang, Bin Yao, Yan Yu Zhao, Ying Guo Bai, Peng Jun Shi |
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| Rok vydání: | 2011 |
| Předmět: |
Molecular Sequence Data
Gene Expression Alkalies Xylose Biology medicine.disease_cause Applied Microbiology and Biotechnology Substrate Specificity chemistry.chemical_compound Hydrolysis Bacterial Proteins Enzyme Stability Arabinoxylan Glycoside hydrolase family 10 medicine Xylobiose Amino Acid Sequence Cloning Molecular Escherichia coli Endo-1 4-beta Xylanases Sewage Substrate (chemistry) General Medicine Kinetics chemistry Biochemistry Xylanase Paenibacillus Sequence Alignment Biotechnology |
| Zdroj: | Journal of Microbiology and Biotechnology. 21:861-868 |
| ISSN: | 1738-8872 1017-7825 |
| DOI: | 10.4014/jmb.1102.02024 |
| Popis: | A xylanase gene, xyn7c, was cloned from Paenibacillus sp. 12-11, an alkalophilic strain isolated from the alkaline wastewater sludge of a paper mill, and expressed in Escherichia coli. The full-length gene consists of 1,296 bp and encodes a mature protein of 400 residues (excluding the putative signal peptide) that belongs to the glycoside hydrolase family 10. The optimal pH of the purified recombinant XYN7C was found to be 8.0, and the enzyme had good pH adaptability at 6.5-8.5 and stability over a broad pH range of 5.0-11.0. XYN7C exhibited maximum activity at 55 degrees C and was thermostable at 50 degrees C and below. Using wheat arabinoxylan as the substrate, XYN7C had a high specific activity of 1,886 U/mg, and the apparent Km and Vmax values were 1.18 mg/ml and 1,961 μmol/mg/min, respectively. XYN7C also had substrate specificity towards various xylans, and was highly resistant to neutral proteases. The main hydrolysis products of xylans were xylose and xylobiose. These properties make XYN7C a promising candidate to be used in biobleaching, baking, and cotton scouring processes. |
| Databáze: | OpenAIRE |
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