Utilization of partially <i>N</i>‐succinylated derivatives of chitosan and glycolchitosan as supports for the immobilization of enzymes

Abstract

Polymer ampholites, partially N-succinylated chitosans (PSC), and partially N-succinylated glycolchitosans (PSGC) were prepared from chitosan (an N-deacetylated chitin) and glycolchitosan (a partially O-2-hydroxyethylated chitosan), and they were utilized as novel supports for the immobilization of enzymes. The immobilization was conducted simultaneously with gelation of PSC and PSGC by reaction with water-soluble carbodiimide in the presence of enzymes. Enzymes were covalently bonded on PSC and PSGC chains. Maximum activity yields of glucoamylase, beta-fructosidase, and D-glucose isomerase were 58.8, 64.3, and 65.2%, respectively. Favorable activity yields of glucoamylase and beta-fructosidase were attained with PSC and PSGC having high degree of N-succinylation, but those of D-glucose isomerase were not affected by the degree of N-succinylation (DS). The activity of immobilized glucoamylase was retained up to 85.5% over 30 batch reactions.