Coimmobilization of glucoamylase and glucose isomerase by molecular deposition technique for one-step conversion of dextrin to fructose.
Glucose isomerase was immobilized by itself with adsorption and coimmobilized with glucoamylase by molecular deposition technique using macroporous trimethylamine polystyrene beads. Approximately 77.5% of the enzyme added was immobilized. The pH-activity curve of the immobilized glucose isomerase was broadened, resulting in 75% retention of its maximum activity at pH 6.2. The Km of the immobilized glucose isomerase was 1.28-fold that of the soluble one. When the two enzymes were immobilized together, the system was found capable of functioning at pH 6.0 to produce fructose from starch and dextrin. At this pH, the total fructose output of the coimmobilized enzyme system after 24 h was 1.9 times that of the free enzyme system.
Ge
Y
Y
Biomacromolecular Research Laboratory, College of Life Science, Jilin University, Changchun, People's Republic of China.
Wang
Y
Y
Zhou
H
H
Wang
S
S
Tong
Y
Y
Li
W
W
D019747:Aldose-Ketose Isomerases / Q000737:chemistry* / Q000378:metabolism; D001709:Biotechnology / Q000379:methods; D003912:Dextrins / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D005632:Fructose / Q000096:biosynthesis*; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008863:Microspheres; D011137:Polystyrenes / Q000737:chemistry; D013696:Temperature