Maqola

The properties of invertase, covalently immobilized at activated carbon

Dilbar MirzarakhmetovaNational of University Uzbekistan, Tashkent, 100174, UzbekistanDavron DekhkonovNational of University Uzbekistan, Tashkent, 100174, UzbekistanМ. М. РахимовNational of University Uzbekistan, Tashkent, 100174, UzbekistanS. Kh. AbdurazakovaTashkent Chemical-Techological Institute, Tashkent, 100011, UzbekistanЗ. Р. АхмедоваInstitute of Microbiology AcSci RUz, Tashkent, 100128, Uzbekistan

Applied Biochemistry and Microbiologyjournal2009en

ABI

Annotatsiya

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.

Mavzular

Enzyme Catalysis and Immobilization Electrochemical sensors and biosensors Enzyme function and inhibition

Identifikatorlar

DOI: 10.1134/s000368380903003x

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