Studies on kinetic parameters and stability of aminoacylase in non-conventional media.

Catalytic properties and conformational stability of aminoacylase (N-acylamino acid amidohydrolase, EC 3.5.1.

The effect of environmental pollution on the function of enzymes of active skeleton muscle. Part 1: An adequate method to study the effect of metal ions on the activity of phosphofructokinase.

The possibilities of exact measuring the effect of metal ions on the activity of phosphofructokinase (PFK) by means of both a heat inactivation and an auxiliary enzyme system were studied. It was found that both methods are suitable for measuring the inhibition of phosphofructokinase by metal ions. It was further found that metal ion concentrations causing 50% deactivation of PFK could not considerably influence the measuring capacity of the auxiliary enzyme system.

Effects of paraquat treatment on fish transaminase molecular subforms.

The effects of paraquat (PQ; 1,1'-dimethyl-4,4'-bipyridylium dichloride) treatment were investigated in carp, silver carp and wels. The serum glutamic-oxalacetic transaminase (GOT; L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.

Factors influencing the operation of a vertical bioreactor segmented with perforated plates.

Factors influencing the operation of a vertical bioreactor segmented with perforated plates supporting immobilized yeast cells were studied. It was found that the most important factors are the length-diameter (L/D) ratio of the reactor and the dilution rate. It was supposed that the optimal L/D ratio is about 1.

Immobilization of pig muscle aldolase on a silica-based support.

Pig muscle aldolase was covalently attached to a silica-based support possessing aldehyde functional groups. The activity of the immobilized enzyme was 37 U/g solid, and the specific activity calculated on a bound protein basis was 1.9 U/mg protein.