Abstract

Marine organisms have been recognized as rich sources of bioactive compounds with valuable biotechnology potential. Enzymes extracted from marine hydrobionts have gained much attention because of their unique quite specific properties that determined their profound applications in chemical, medical, food industries and molecular biology experiments. In this regard, our work focused on investigation of proteolytic potential of marine hydrobionts. At first, tissue extract of Antarctic hydrobiont Parborlasia corrugatus was separated by gel filtration chromatography on a Superdex-75 PG. Further zymography with using gelatin as substrate revealed the presence of clear band that can indicate about active enzymes. It had been shown the presence of collagenolytic activity in all eight fractions obtained after chromatographic separation of tissue extract. Trypsin-like (L-BApNA hydrolyzing) was found only in first fraction. Our results let us assume that P. corrugatus can be regarded as potential source of enzymes for practical use.