Isolation and purification of Bacillus thuringiensis var. israelensis IМV В-7465 peptidase with specificity toward elastin and collagen
| Autor: | V. O. Chernyshenko, L. D. Varbanets, N. А. Nidialkova |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0106 biological sciences
0301 basic medicine Bacillus thuringiensis 01 natural sciences Biochemistry Microbiology Substrate Specificity lcsh:Biochemistry Serine 03 medical and health sciences chemistry.chemical_compound Hydrolysis Bacterial Proteins 010608 biotechnology Enzyme Stability medicine lcsh:QD415-436 Ammonium Enzyme Assays chemistry.chemical_classification biology Chemistry Elastase Hydrogen-Ion Concentration biology.organism_classification Chromatography Ion Exchange Elastin Molecular Weight 030104 developmental biology Enzyme Ammonium Sulfate biology.protein Collagenase Chromatography Gel Collagen medicine.drug Peptide Hydrolases |
| Zdroj: | Ukrainian Biochemical Journal, Vol 88, Iss 3, Pp 18-28 (2016) |
| ISSN: | 2409-4943 |
| Popis: | Peptidase of Bacillus thuringiensis var. israelensis IМV В-7465 was isolated from culture supernatant using consecutive fractionations by an ammonium sulphate (60% saturation), ion-exchange chromatography and gel-filtration on the TSK-gels Toyoperl HW-55 and DEAE 650(M). Specific elastase (442 U∙mg of protein-1) and collagenase (212.7 U∙mg of protein-1) activities of the purified enzyme preparation were 8.0- and 6.1-fold, respectively higher than ones of the culture supernatant. Peptidase yields were 33.5% for elastase activity and 30.1% for collagenase activity. It was established that the enzyme is serine metal-dependent alkaline peptidase with Mr about 37 kDa. Maximal hydrolysis of elastin and collagen occurs at the optimum pH 8.0 and t° – 40 and 50 °С, respectively. The purified preparation has high stability at pH in the range of 7.0 to 10.0 and 40-50 °С. |
| Databáze: | OpenAIRE |
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