Flaschel, E.Raetz, E.Renken, A.2006-04-182006-04-182006-04-18198210.1002/bit.260241114https://infoscience.epfl.ch/handle/20.500.14299/229327WOS:A1982PM93000013The kinetics of glucose liberation from lactose by b-galactosidase from A. niger was studied in a wide range of the main variables. The anal. shows that the kinetic models proposed so far are not adequate. The main finding is that the reaction rate is not linearly correlated to the enzyme concn.; it increases more than proportionally. This nonlinear relation results because this lactase can distinguish between a- and b-galactose. a-Galactose acts as competitive and anticompetitive inhibitor, whereas b-galactose is a competitive one. The competitive inhibition of the a-anomer is .apprx.12 times more severe than that of the b-anomer. The kinetics, including a simplified model for the mutarotation of galactose is given for a temp. of 50 Deg at a pH of 3.5, the most likely conditions for the application of this lactase in acid whey treatment. [on SciFinder (R)]Whey (lactose hydrolysis in; by enzymic reactor; kinetics of)Kinetics of mutarotationMutarotation (of galactose)KineticsMichaelis constant (of b-galactosidase; of Aspergillus niger)Aspergillus niger (b-galactosidase of; reaction kinetics of)whey lactase reactor kineticsmutarotation galactose lactase kineticsgalactosidasebeta kineticslactoseAspergillustext::journal::journal article::research article