Catalytic properties of glucoamylase immobilized on synthetic carbon material Sibunit

Autor:	G. V. Plaksin, T. G. Terent’eva, G. A. Kovalenko, L. V. Perminova
Rok vydání:	2007
Předmět:	chemistry.chemical_classification Chromatography Immobilized enzyme Starch fungi Substrate (chemistry) Applied Microbiology and Biotechnology Biochemistry Catalysis Hydrolysis chemistry.chemical_compound Adsorption chemistry Chemical engineering Dextrin Thermostability
Zdroj:	Applied Biochemistry and Microbiology. 43:374-378
ISSN:	1608-3024 0003-6838
Popis:	Glucoamylase (commercial preparation Glucavamorin) was immobilized by sorption on a carbon support Sibunit. Starch saccharification by the resulting biocatalyst (dextrin hydrolysis) was studied. Investigation of the effect of adsorptional immobilization on kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, showed that immobilization of Glucavamorin on Sibunit resulted in a thousandfold increase in glucoamylase stability in comparison with the dissolved enzyme. Presence of the substrate (dextrins) in the reaction mixture had a considerable stabilizing effect. Increase in dextrin concentration increases the thermostability of the immobilized enzyme. The overall factor of glucoamylase stabilization adsorbed on Sibunit with the presence of 53% dextrin solutions in comparison with the dissolved enzyme approximated 10(5). The biocatalyst for starch saccharification made on the base of Subunit-adsorbed Glucavamorin had a high operational stability. Its half-inactivation time at 60 degrees C exceeded 30 days.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::61a18041b9ffee923e26150e371b328f https://doi.org/10.1134/s0003683807040023 Zobrazit plný text záznamu Plný text ve formátu PDF