A new kinetic model of recombinant beta-galactosidase from Kluyveromyces lactis for both hydrolysis and transgalactosylation reactions

Biochem Biophys Res Commun. 2004 Apr 9;316(3):738-43. doi: 10.1016/j.bbrc.2004.02.118.

Abstract

Previous models based on the Michaelis-Menten kinetic equation, that glucose was not used as an acceptor, did not explain our experimental data for lactose conversion by a recombinant beta-galactosidase from Kluyeromyces lactis. In order to create a new kinetic model based on the data, the effects of galactose and glucose on beta-galactosidase activity were investigated. Galactose acted as an inhibitor at low concentrations of galactose and lactose, but did not inhibit the activity of beta-galactosidase at high concentrations of galactose (above 50mM) and lactose (above 100mM). The addition of glucose at concentrations below 50mM resulted in an increased reaction rate. A new model of K. lactis beta-galactosidase for both hydrolysis and transgalactosylation reactions with glucose and lactose as acceptors was proposed. The proposed model was fitted well to the experimental data of the time-course reactions for lactose conversion by K. lactis beta-galactosidase at various concentrations of substrate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Dose-Response Relationship, Drug
  • Escherichia coli / metabolism
  • Galactose / chemistry*
  • Glucose / chemistry
  • Hydrolysis*
  • Kinetics
  • Kluyveromyces / enzymology*
  • Lactose / chemistry
  • Models, Chemical
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry*
  • Time Factors
  • beta-Galactosidase / chemistry*
  • beta-Galactosidase / metabolism

Substances

  • Recombinant Proteins
  • beta-Galactosidase
  • Glucose
  • Lactose
  • Galactose