Utilization of partiallyN-succinylated derivatives of chitosan and glycolchitosan as supports for the immobilization of enzymes

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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, β‐fructosidase, and D‐glucose isomerase were 58.8, 64.3, and 65.2%, respectively. Favorable activity yields of glucoamylase and β‐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.

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