[Preparation and characteristics of immobilized collagenase isolated from crab Paralithodes camtschatica]

Collagenolytic protease from hepatopancreas of king crab was immobilized on water-soluble reactive polymers containing N-succinimide units and possessing different hydrophobicity-hydrophilicity balance. The immobilized enzyme displayed higher heat stability, but its proteolytic activity decreased with the increase in the number of the copolymer hydrophobic groups. Highly active thermostable preparations of collagenolytic protease were obtained by copolymerization. The copolymerization did not affect the enzyme activity and increased the protease heat stability to the formation of pseudocross-links of protein molecules in their associates.