TY - JOUR
T1 - Kinetic model for oligosaccharide hydrolysis using suspended and immobilized enzymes
AU - Shibasaki-Kitakawa, Naomi
AU - Cheirsilpa, Benjamas
AU - Iwamura, Ken Ichiro
AU - Kushibiki, Masanori
AU - Kitakawa, Akio
AU - Yonemoto, Toshikuni
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1998/6
Y1 - 1998/6
N2 - A novel kinetic model that describes the hydrolysis of oligosaccharide using the suspended enzyme has been constructed by introducing the selectivity of the enzyme for cleaving each α-1,6 glycosidic bond of the substrate. The Michaelis-Menten type kinetic constants, Km and Vmax, and the selectivity coefficient, α, are estimated by fitting the model with the experimental data obtained under various conditions. The new constant, α, is estimated at 0.411, and almost the same as the experimental values. The model has been extended for the immobilized enzyme system by taking into account the intraparticle mass transfer resistance. The model constants are estimated similarly to the case of the suspended enzyme system. αimm (α for the immobilized enzyme system) is a little higher than that in the suspended enzyme system. Kmimm and Vmaximm, are much greater than those for the suspended enzyme system. The estimated values of the effective diffusivities in the support particle are a few order of magnitude smaller than those in aqueous solution. The model well simulates both experimental results obtained in the suspended and immobilized enzyme systems.
AB - A novel kinetic model that describes the hydrolysis of oligosaccharide using the suspended enzyme has been constructed by introducing the selectivity of the enzyme for cleaving each α-1,6 glycosidic bond of the substrate. The Michaelis-Menten type kinetic constants, Km and Vmax, and the selectivity coefficient, α, are estimated by fitting the model with the experimental data obtained under various conditions. The new constant, α, is estimated at 0.411, and almost the same as the experimental values. The model has been extended for the immobilized enzyme system by taking into account the intraparticle mass transfer resistance. The model constants are estimated similarly to the case of the suspended enzyme system. αimm (α for the immobilized enzyme system) is a little higher than that in the suspended enzyme system. Kmimm and Vmaximm, are much greater than those for the suspended enzyme system. The estimated values of the effective diffusivities in the support particle are a few order of magnitude smaller than those in aqueous solution. The model well simulates both experimental results obtained in the suspended and immobilized enzyme systems.
KW - Hydrolysis of oligosaccharide
KW - Immobilized enzyme
KW - Kinetic model
KW - Suspended enzyme
UR - http://www.scopus.com/inward/record.url?scp=0009000985&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0009000985&partnerID=8YFLogxK
U2 - 10.1016/S1369-703X(98)00003-5
DO - 10.1016/S1369-703X(98)00003-5
M3 - Article
AN - SCOPUS:0009000985
VL - 1
SP - 201
EP - 209
JO - Biochemical Engineering Journal
JF - Biochemical Engineering Journal
SN - 1369-703X
IS - 3
ER -