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Utilization of partially N ‐succinylated derivatives of chitosan and glycolchitosan as supports for the immobilization of enzymes
Author(s) -
Yamaguchi Ryuji,
Arai Yuji,
Kaneko Takeshi,
Itoh Tatsuro
Publication year - 1982
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260240505
Subject(s) - succinylation , chitosan , chemistry , chitin , immobilized enzyme , enzyme , carbodiimide , organic chemistry , glucose 6 phosphate isomerase , biochemistry , chemical modification , lysine , amino acid
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.