Home|Journals|Articles by Year|Audio Abstracts

Original Article

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.

Cited by 0 Articles

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.

Key words: jellyfish; the Antarctic region; serine proteases; isolation; biochemical characterization

Full-text options

Share this Article

Online Article Submission
• ejmanager.com

ejPort - eJManager.com
Refer & Earn
About BiblioMed
License Information
Terms & Conditions
Privacy Policy
Contact Us

The articles in Bibliomed are open access articles licensed under Creative Commons Attribution 4.0 International License (CC BY), which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.