Isolation and characterization of an L-amino acid acylase fromAspergillus oryzae
| Autor: | M. K. Malinka, L. S. Lobareva, V. M. Stepanov |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
chemistry.chemical_classification
Ethanol Chromatography biology Size-exclusion chromatography Plant Science General Chemistry Fractionation biology.organism_classification General Biochemistry Genetics and Molecular Biology Amino acid Hydrolysis chemistry.chemical_compound Enzyme chemistry Biochemistry Aspergillus oryzae Sephadex |
| Zdroj: | Chemistry of Natural Compounds. 18:341-349 |
| ISSN: | 1573-8388 0009-3130 |
| DOI: | 10.1007/bf00580465 |
| Popis: | A scheme of isolating a highly purified L-amino acylase fromAspergillus oryzae is described which excludes extraction of the enzyme from the preparation “Amilorizin,” fractionation with ethanol, chromatography on DEAE-cellulose, and gel filtration through Sephadex G-200 and Bio-Gel P-300. The enzyme, as purified 1240-fold, has a molecular weight of 118,000, apparently consists of two subunits with a molecular weight of 60,000, is stable in the pH range of 7–10 and has an optimum pH of 8.9 and a pI of 4.0. Its amino acid composition has been determined and its substrate specificity has been studied. The acylase is a metalloenzyme: Co2+` ions in concentrations of 10−4–5·10−5 M increase the rate of hydrolysis of N-acetyl-L-amino acids three- to fourfold. It shows differences in its molecular and functional properties from acylase I obtained from porcine kidney. |
| Databáze: | OpenAIRE |
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