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

Abstract

The growing demand for industrial proteases and enzyme-containing products substantiates the search for costeffective 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.

Study of the Antioxidant, Antimicrobial, and Wound Healing Properties of Raw Hydrolyzed Extract from Nile Tilapia Skin (Oreochromis niloticus)

“…In addition, Raksha et al. (2021) [24] determined an effective reduction in NO generation (upper to 33 %) by peptides isolated from Euphausia superba at 2 mg/ml.…”

“…[21,22] Yang et al (2019) [23] demonstrated that the collagen from Tegillarca granosa was capable of producing 50 % inhibition of the ABTS * + free radical in a concentration between 54.40-96.30 μg/ml. In addition, Raksha et al (2021) [24] determined an effective reduction in NO generation (upper to 33 %) by peptides isolated from Euphausia superba at 2 mg/ml. These peptides, in addition to their antioxidant activity, can also have a direct effect on wound healing by exhibiting antimicrobial activity; especially when the skin barrier is compromised, exposing the area to potential pathogenic microorganisms.…”

A protease from Moringa oleifera Lam exhibits plasmin like activity of blood clot solubilization under ex-vivo and in-vitro hydrolysis of fibrin

“…Plasmin an endogenous brinolytic protease also resolved into two protein bands on SDS-PAGE [32]. Serine proteases with brinolytic activity from jelly sh showed 30 and 45 kDa peptides on SDS PAGE and have been suggested as potential thrombolytic agent [33].…”