[Enzyme immobilization via silochromes, modified by transition metal salts]. / Immobilizatsiia fermentov na silokhromakh, modifitsirovannykh soliami perekhodnykh metallov.

The immobilization of pectoawamorine G 10X, pronase E and P, protease from Bac. mesentericus and rat liver microsomal fraction was performed by sylochromes modified by Ti, Zr and Hf salts. The pectinesterase, caseinolytic, esterase and hydroxylating activity of the immobilized preparations, their stability during storage, thermostability and pH optimum are determined. Of greatest interest for practical application are preparations of pectoawamorine. G 10X and pronase E and P immobilized by HfOCl2.

[Pronase E and P immobilization on aminoorganosilica surface]. / Immobilizatsiia pronazy e i p na poverkhnosti aminoorganokremiezema.

Immobilization of pronase E and P was performed on sylochrome modified by gamma-aminopropyltrietoxysilane using cyanuric chloride, 2,4--toluylenediisocyanate, glutaric aldehyde and also on sylochrome by means of titanium tetrachloride. The esterase and caséinolytic activities of the immobilized preparations and their stability during storage were determined. The increased thermostability of the immobilized preparation is established. The influence of the enzyme: carrier ratio on the immobilization process and activity of the enzymes was studied. It is shown that application of glutaric aldehyde favours the best retention of the esterase activity (73%), whereas the caseinolytic activity is better retained (31%) when titanium tetrachloride was used.