Journal Article

·2007

PRODUCT INHIBITION OF WHEY LACTOSE HYDROLYSIS

Elçin Demırhan YTU , Dilek Kılıç Apar YTU , Belma Özbek YTU

Chemical Engineering Communications

Abstract

Abstract In the present study, glucose and galactose inhibition effects for β-galactosidase hydrolyzing lactose recovered from whey were investigated. The experiments were carried out in 250 mL of 25 mM phosphate buffer solution containing 1, 1.5, 2, 4, and 6% (w/v) lactose recovered from whey by using a commercial β-galactosidase produced from Kluyveromyces marxianus lactis at a constant temperature of 37°C, pH 6.5, and enzyme concentration of 1 mL/L, in a batch reactor system. The amounts of glucose and galactose added to the reaction solution were 6.25, 12.5, and 25 g/L. A second-order kinetic expression effectively simulated the data of residual lactose concentration with respect to processing time for each experimental condition examined. The Lineweaver-Burk plots showed that the inhibition effects of glucose and galactose were uncompetitive. The inhibition constants (Ki) obtained for glucose and galactose (10.32 g/L and 13.03 g/L, respectively) showed that the glucose was the most effective inhibitor for β-galactosidase. Keywords: β-GalactosidaseHydrolysisInhibition kineticWhey lactose Acknowledgment Elçin Demirhan gratefully acknowledges TUBITAK (The Scientific and Technological Research Council of Turkey) for scholarship. Notes a Hydrolysis kinetic constant (L/g·min). a Hydrolysis kinetic constant (L/g·min). a Hydrolysis kinetic constant (L/g·min).

Keywords

Lactose Chemistry Hydrolysis Galactose Kluyveromyces marxianus Product inhibition Kluyveromyces lactis Uncompetitive inhibitor Chromatography Nuclear chemistry Non-competitive inhibition Enzyme Biochemistry Yeast

Subject Areas

Enzyme Catalysis and Immobilization ·Molecular Biology ·Life Sciences
Enzyme Production and Characterization ·Biotechnology ·Life Sciences
Protein Hydrolysis and Bioactive Peptides ·Molecular Biology ·Life Sciences

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