摘要
Escherichia colt L - asparaginase was modified with O - carboxymethylated chitosan using glutaraldehyde as a coupling agent. The resulting coujugate retained more than 50% of its original enzyme activity under theprotection of its normal substrate or product and shoWed marked resistance toproteolysis by trypsin and chymotrypsin.
Escherichia colt L - asparaginase was modified with O - carboxymethylated chitosan using glutaraldehyde as a coupling agent. The resulting coujugate retained more than 50% of its original enzyme activity under theprotection of its normal substrate or product and shoWed marked resistance toproteolysis by trypsin and chymotrypsin.
