S. Todisco et al., A KINETIC-MODEL FOR THE PECTIN HYDROLYSIS USING AN ENDO-ACTING PECTINASE FROM RHIZOPUS, Journal of molecular catalysis, 92(3), 1994, pp. 333-346
Enzyme kinetics of pectin hydrolysis reaction catalysed by an endo-pol
ygalacturonase from Rhizopus have been analysed experimentally in a st
irred batch reactor at pH = 4.5 and T = 34 degrees C using a sodium sa
lt of polygalacturonic acid as substrate. The reaction products, consi
sting of oligomers of galitcturonic acid, were classified in four clas
ses of oligomeric fractions employing three hollow fibre ultrafiltrati
on units characterised by different molecular weight cut-off (MW(co)).
On the basis of the time-concentration data, a kinetic model of the r
eacting system has been proposed in terms of a series-side reaction pa
ttern. Identification of kinetic parameters was carried out by a non-l
inear regression optimization procedure based on the Powell's algorith
m of conjugated directions. Finally, the kinetic model was used to pre
dict the best reactor configuration able to control the product distri
bution for a given enzyme/substrate concentration ratio.