Cloning of an endoglycanase gene from Paenibacillus cookii and characterization of the recombinant enzyme
| Autor: | Shin Kanamasa, Suguru Shinoda, Motoo Arai |
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| Rok vydání: | 2011 |
| Předmět: |
DNA
Bacterial Molecular Sequence Data Bioengineering macromolecular substances Cellulase Protein Sorting Signals Molecular cloning Applied Microbiology and Biotechnology Substrate Specificity chemistry.chemical_compound Chitin Enzyme Stability Chitosanase Cloning Molecular Cellulose Glucans chemistry.chemical_classification Chitosan Chitosanase activity Sequence Homology Amino Acid biology Temperature Substrate (chemistry) Sequence Analysis DNA General Medicine Hydrogen-Ion Concentration Molecular biology Recombinant Proteins Amino acid Molecular Weight carbohydrates (lipids) chemistry Biochemistry biology.protein Bacillus circulans Paenibacillus Biotechnology |
| Zdroj: | Biotechnology Letters. 34:281-286 |
| ISSN: | 1573-6776 0141-5492 |
| DOI: | 10.1007/s10529-011-0759-5 |
| Popis: | An endoglycanase gene of Paenibacillus cookii SS-24 was cloned and sequenced. This Pgl8A gene had an open reading frame of 1,230 bp that encoded a putative signal sequence (31 amino acids) and mature enzyme (378 amino acids: 41,835 Da). The enzyme was most homologous to a β-1,3-1,4-glucanase of Bacillus circulans WL-12 with 84% identity. The recombinant enzyme hydrolyzed carboxymethyl cellulose, swollen celluloses, chitosan and lichenan but not Avicel, chitin powder or xylan. With chitosan as the substrate, the optimum temperature and hydrolysis products of the recombinant enzyme varied at pH 4.0 and 8.0. This is the first report that characterizes chitosanase activity under different pH conditions. |
| Databáze: | OpenAIRE |
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