L‐asparaginase from Escherichia coli II and Erwinia carotovora bound to poly‐(methyl methacrylate)

Abstract

SYNOPSISGasparaginase (ASNase) from Escherichia coli (EC) I1 and Erwiniu carotovoru (Erw. carot.) has been chemically coupled to poly(methy1 methacrylate) (PMMA) via the bifunctional coupling agents y-aminopropyltriethoxysilane and glutaraldehyde.The level of bound activity was about 2 and 6 IU/lOO cm2, respectively. The immobilized asparaginases were successfully used in previously reported in vivo experiments. Certain kinetic characteristics such as pH profile and temperature dependence were unaffected by the immobilization process Both bound asparaginase's apparent K m were greater than the native enzyme's value by approximately an order of magnitude. The apparent K m for the EC ASNase was approximately the same in buffer solutions and in pooled canine blood.