Thermal Stability of Fructosyltransferase from Aureobasidium pullulans
A. Madlová, M. Antošová, M. Polakovič, and V. Báleš
Department of Chemical and Biochemical Engineering, Faculty of Chemical Technology, Slovak University of Technology, SK-812 37 Bratislava
Received: 19 May 2000
Abstract: The thermal stability of a biocatalyst in the form of whole cells of the fungi Aureobasidium pullulans exhibiting fructosyltransferase activity was investigated during a batch catalytic process of fructooligosaccharide production. The stability of fructosyltransferase was monitored during 8 h with respect to temperature and overall saccharide concentration. A fructosyltransferase activity assay was developed for the monitoring of enzyme activity that was based on the rate of formation of 1-kestose measured by an HPLC method. It was found that the biocatalyst inactivated rather quickly at temperatures above 60ºC even at high saccharide concentrations. The stabilizing effect of saccharide concentration on the fructosyltransferase activity was investigated at 55ºC. A kinetic equation of enzyme inactivation, based on a reversible one-step reaction and simple exponential relationships of the rate constants and on the overall saccharide concentration, was suggested and statistically verified.
Full paper in Portable Document Format: 546aa339.pdf
Chemical Papers 54 (6a) 339–344 (2000)
Monday, September 26, 2016