[Role of the molecular environment in chlorophyllase functioning during its immobilization on organic carriers].

Immobilization of chlorophyllase was performed on aminohexadecyl sepharose, aminoundecyl sepharose and heptyl sepharose. The enzyme activity lowers considerably and is rather close for all carriers. Essential differences are manifested in stability of the preparation during storage. On aminohexadecyl sepharose, the most hydrophobic carrier, the activity of chlorophyllase is 1.4 times as low for a month, on aminoundecyl sepharose for the same period it is 2.1 times as low and on heptyl sepharose--4.8 times as low. The covalent binding of chlorophyllase with sepharose activated by bromo-cyanogen with the subsequent fixation of diethyl amine or dodecyl amine possessing different hydrophobic properties showed that diethyl amine favours to a greater extent manifestation of the chlorophyllase activity and stabilization of the enzyme in time than dodecylamine. The data obtained evidence for a considerable role of the enzyme sstate and its molecular environment in manifestation of its functional activity and in providing its stability.