[Influence of UV-radiation on physical-chemical and functional properties of free immobilized glucoamylase from Aspergillus awamori].

The effect of UV light (240-390 nm) at the doses of 151-1510 J/m2 on the catalytic activity of free and im- mobilized glucoamylase from Aspergillus awamori was investigated. It was established that the loss of catalytic activity of the enzyme was associated with photochemical transformations of Trp-120, which is part of the active site of glucoamylase. It was shown that the use of collagen as a carrier for immobilization of glucoamylase reduces the constant photoinactivation of the enzyme.

Computer-aided analysis of spatial structure of some hydrolytic enzymes.

Using the MolScript version 2.1 computer program for protein molecule modeling and X-ray structure analysis data the spatial structures of several hydrolytic enzymes have been compared. These include glucoamylase from Aspergillus awamori and Saccharomycopsis fibuligera and lipases from Rhizopus japonicus.

[The effect of urea, gamma- and UV-irradiation on physico-chemical characteristics of native and immobilized inulinase].

The immobilization of inulinase by ionexchange AB-26 and AB-17-2P has been made by adsorbtion and glutaraldehyde methods. The effect of UV-radiation, carbamide and gamma-rays on the stability of native and immobilized enzyme has been investigated. The stability of inulinase in relation to denaturation agents has been shown to increase with the immobilization of ionexchange.