Kinetics of lactose hydrolysis by beta-galactosidase of Kluyveromyces lactis immobilized on cotton fabric.
A mathematic model for describing the Michaelis-Menten-type reaction kinetics with product competitive inhibition and side-reaction is proposed. A multiresponse nonlinear simulation program was employed to determine the coefficients of a four-parameter rate expression. The rate expression was compared with the conventional Michaelis-Menten reaction rate models with and without product inhibition. Experimental data were obtained using beta-galactosidase of Kluyveromyces lactis immobilized on cotton fabric in a batch system at a temperature of 37 degrees C and at various initial concentrations of dissolved lactose ranging from 3-12.5% (w/v). The reaction is followed by concentration changes with time in the tank. Samples were obtained after the outlet stream of the packed bed reactor is mixed in a well-stirred tank. High-performance liquid chromatography (HPLC) was applied to monitor the concentrations of all the sugars (reactants as well as products). The four-parameter rate model is featured with a term to describe the formation of trisaccharides, a side-reaction of the enzymatic hydrolysis. The proposed model simulates the process of lactose hydrolysis and the formation of glucose and galactose, giving better accuracy compared with the previous models.
Zhou
Quinn Zhengkun
QZ
Food and Bioproduct Processing Research Cluster, Department of Chemical & Materials Engineering, The University of Auckland, New Zealand.
Chen
Xiao Dong
XD
Li
Xuemei
X
D019149:Bioreactors; D002851:Chromatography, High Pressure Liquid; D032561:Cotton Fiber; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D007716:Kluyveromyces / Q000201:enzymology* / Q000378:metabolism; D007785:Lactose / Q000378:metabolism*; D008962:Models, Theoretical; D013696:Temperature; D001616:beta-Galactosidase / Q000378:metabolism*
D004800:Enzymes, Immobilized; D001616:beta-Galactosidase; D007785:Lactose