Immobilization of alpha-glucosidase in chitosan coated polygalacturonic acid.
Crude alpha-glucosidase from Baker's yeast was immobilized in polygalacturonic acid beads and coated with chitosan. Chemical and physical characterization were performed by using p-nitrophenyl-alpha-D-glucopyranoside (pNPG) as an artificial substrate. Operation, thermal, pH, and strorage stabilities of the free and immobilized enzyme were also examined. The stabilities of immobilized enzyme were found to be better than that of the free enzyme. Furthermore, the hydrolysis rate of the chitosan coated alpha-glucosidase polygalacturonic acid beads were studied. In conclusion, the enzyme beads appear to have good characteristics and offer the prospect that this system may find application in enzyme immobilization, in addition to controlled drug release studies.
Dinçer
Ayse
A
Ege University, Faculty of Science, Biochemistry Department, Bornova, Izmir, Turkey.
Okutucu
Burcu
B
Zihnioğlu
Figen
F
Telefoncu
Azmi
A
D048271:Chitosan / Q000737:chemistry*; D020099:Coated Materials, Biocompatible / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008422:Materials Testing; D010368:Pectins / Q000737:chemistry*; D013696:Temperature; D000520:alpha-Glucosidases / Q000032:analysis* / Q000737:chemistry*
D020099:Coated Materials, Biocompatible; D004800:Enzymes, Immobilized; D010368:Pectins; D048271:Chitosan; D000520:alpha-Glucosidases; C003181:polygalacturonic acid