Purification, characterization and end product analysis of dextran degrading endodextranase from Bacillus licheniformis KIBGE-IB25
| Autor: | Afsheen Aman, Asma Ansari, Muhammad Samee Haider, Rashida Rahmat Zohra, Shah Ali Ul Qader |
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| Rok vydání: | 2015 |
| Předmět: |
Glycosylation
Bacillus Buffers Biochemistry Catalysis Substrate Specificity chemistry.chemical_compound Hydrolysis Structural Biology RNA Ribosomal 16S Glycoside hydrolase Amino Acid Sequence Bacillus licheniformis Molecular Biology Peptide sequence Phylogeny chemistry.chemical_classification Dextranase Chromatography biology Chemistry Osmolar Concentration Temperature Dextrans General Medicine Hydrogen-Ion Concentration biology.organism_classification Amino acid Enzyme Activation Molecular Weight Dextran |
| Zdroj: | International Journal of Biological Macromolecules. 78:243-248 |
| ISSN: | 0141-8130 |
| Popis: | Degradation of high molecular weight dextran for obtaining low molecular weight dextran is based on the hydrolysis using chemical and enzymatic methods. Current research study focused on production, purification and characterization of dextranase from a newly isolated strain of Bacillus licheniformis KIBGE-IB25. Dextranase was purified up to 36 folds with specific activity of 1405 U/mg and molecular weight of 158 kDa. It was found that enzyme performs optimum cleavage of dextran (5000 Da, 0.5%) at 35 °C in 15 min at pH 4.5 with a Km and Vmax of 0.374 mg/ml and 182 μmol/min, respectively. Relative amino acid composition analysis of purified enzyme suggested the presence of higher number of hydrophobic, acidic and glycosylation promoting amino acids. The N-terminal sequence of dextranase KIBGE-IB25 was AYTVTLYLQG. It exhibited distinct amino acid sequence yet shared some inherent characteristics with glycosyl hydrolases (GH) family 49 and also testified the presence of O-glycosylation at N-terminal end. |
| Databáze: | OpenAIRE |
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