Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase

TLDR: The microstructure and the catalytic properties of crosslinked enzyme aggregates of penicillin acylase (PA) obtained under different conditions were investigated in this article, where the period of time left between enzyme precipitation and the cross-linking step was found to influence the structural organization of the resulting enzyme preparation.

Abstract: The microstructure and the catalytic properties of cross-linked enzyme aggregates (CLEA) of penicillin acylase (PA) obtained under different conditions were investigated The period of time left between the enzyme precipitation and the cross-linking step was found to influence the structural organization of the resulting enzyme preparation Confocal fluorescent microscopy of the so-called “fresh” and “mature” CLEAs PA allowed to estimate the “characteristic” diameter of CLEA PA particles, which appeared to be about 16 μm, and revealed that the “mature” type was composed of relatively big particles as compared to the “fresh” type Complementary kinetic studies showed that the “mature” CLEA PA were more effective in both hydrolytic and synthetic reactions It was suggested that the aggregate size might regulate the extent of covalent modification of PA and thereby influence the catalytic properties of CLEA