Isolation and partial characterization of serine proteases from jellyfish of the Antarctic region

Nataliia Raksha Teyiana Halenova Tetiana Vovk Tetiana Beregova Tetiana Maievska Victor Tomchuk Olexiy Savchuk Ludmila Ostapchenko   

Open Access   

Published:  Nov 11, 2022

DOI: 10.7324/JABB.2023.110214
Abstract

The growing demand for industrial proteases and enzyme-containing products substantiates the search for cost-effective sources of enzymes. The aim of current research was to find a one-step approach for the isolation of the fraction of serine proteases from the jellyfish of the Antarctic region. Given our data, ion-exchange chromatography on diethylaminoethyl-sepharose carboxymethyl-sepharose was ineffective, in contrast to affinity chromatography on benzamidine-sepharose. The isolated fraction consists of enzymes with a molecular weight of more than 30 kDa and isoelectric points at pH = 3.0; 5.0–6.0 and pH = 9.0, which can break down gelatin, casein, and fibrinogen. The maximal proteolytic activity was found at pH = 12.0 and a temperature of +55°C. Serine proteases showed activity against the chromogenic substrate for trypsin and had no activity against substrates for chymotrypsin and elastase indicating that enzymes are trypsin-like proteases. The presence of enzymes with fibrino(geno)lytic activity and the ability of serine proteases from jellyfish to work at high pH and temperatures suggest their potential use as thrombolytics, as well as agents in the industries requiring a highly alkaline conditions.


Keyword:     Jellyfish The Antarctic region Serine proteases Isolation Biochemical characterization


Citation:

Raksha N, Halenova T, Vovk T, Beregova T, Maievska T, Tomchuk V, Savchuk O, Ostapchenko L. Isolation and partial characterization of serine proteases from jellyfish of the Antarctic region. J App Biol Biotech. 2022. https://doi.org/10.7324/JABB.2023.110214

Copyright: Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike license.

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