Enzymatic modification of hydroxyethylcellulose by transgalactosylation with beta-galactosidases.
beta-galactosidases from A. oryzae and a thermophilic CLONEZYME glycosidase library were used to catalyze the transfer of the beta-D-galactopyranosyl moiety from lactose to the hydroxyl groups of hydroxyethylcellulose (HEC) in sodium acetate buffer. The degree of substitution was quantified by using galactose oxidase enzymatic assays. Depolymerization was also observed in the course of the transglycosylation reactions.
Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.
J
J
Li
H N
HN
Cheng
R G
RG
Nickol
P G
PG
Wang
D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins / Q000378:metabolism; D002482:Cellulose / Q000031:analogs & derivatives* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D006031:Glycosylation; D007785:Lactose / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D012275:Oryza / Q000201:enzymology; D011994:Recombinant Proteins / Q000378:metabolism; D012997:Solvents / Q000494:pharmacology; D014783:Viscosity; D001616:beta-Galactosidase / Q000378:metabolism*
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012997:Solvents; D002482:Cellulose; C002283:hydroxyethylcellulose; D001616:beta-Galactosidase; D007785:Lactose