RESUMO
Lipase from "Fusarium solani" FS1 was immobilized by covalent attachment to polyacrylamide beads and onto magnetized Dacron, retaining 12(per cent) and 97(per cent) of activity, respectively. Lipase was also entrapped within polyacrylamide beads, retaining 53(per cent) of activity. Investigations of the kinetic characteristics of the immobilized derivates using triolein as substrate showed that lipase immobilized onto polyacrilamide beads and Dracon did not follow Michaelis-Menten kinetics.
Assuntos
Fusarium , Técnicas In Vitro , Lipase , CinéticaRESUMO
Lipase from Fusarium solani FS1 was immobilized by covalent attachment to polyacrylamide beads and onto magnetized Dacron, retaining 12% and 97% of activity, respectively. Lipase was also entrapped within polyacrylamide beads, retaining 53% of activity. Investigations of the kinetic characteristics of the immobilized derivatives using triolein as substrate showed that lipase immobilized onto polyacrilamide beads and Dacron did not follow Michaelis-Menten kinetics.
Lipase de Fusarium solani FS1 foi imobilizada por ligação covalente usando esferas de poliacrilamida e Dacron magnetizado, retendo 12%, e 97% de atividade, respectivamente. A lipase foi também enclausurada em esferas de poliacrilamida e reteve 53% de sua atividade específica. Investigações sobre o comportamento cinético usando trioleína como substrato mostraram que as lipases imobilizadas não seguem a cinética de Michaelis-Menten.