The properties of invertase, covalently immobilized at activated carbon

Autor:	Rakhimov Mm, D. T. Mirzarakhmetova, D. B. Dekhkonov, S. Kh. Abdurazakova, Z. R. Akhmedova
Rok vydání:	2009
Předmět:	Chromatography Immobilized enzyme Substrate (chemistry) Isoamyl alcohol Applied Microbiology and Biotechnology Biochemistry chemistry.chemical_compound Hydrolysis Invertase chemistry Urea medicine Glutaraldehyde Activated carbon medicine.drug
Zdroj:	Applied Biochemistry and Microbiology. 45:258-261
ISSN:	1608-3024 0003-6838
DOI:	10.1134/s000368380903003x
Popis:	The covalent immobilization of yeast invertase with glutaraldehyde at activated carbon, modified preliminarily by urea and dimethyl formamide treatment, has been established. Some physicochemical properties of the immobilized and native enzyme in water and water-organic solutions have been studied. Hydrolytic, as well as transferase enzyme characteristics have changed after immobilization. The optimal conditions for hydrolytic and transferase activity of immobilized invertase are pH 6.0 and 7.0, respectively. The optimum temperature for the immobilized enzyme is 30°C. The conversion degree of isoamyl alcohol depends on the substrate and enzyme concentrations in medium, holdup time and organic phase quantity in the reaction medium.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::418ff78062bc17ebadcf9da6e9743761 https://doi.org/10.1134/s000368380903003x Zobrazit plný text záznamu Plný text ve formátu PDF