Purification And Characterization Of Protease From Artocarpus Integer Leaf

The presence of a protease in Artocarpus integer leaves, which can be used as a meat tenderiser, was verified by the presence of a band at 69 kDa, using caseinolytic zymography and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE). Purification by temperature-phase partitioning with 6 % (v/v) Triton X-114, 44 % (w/v) ammonium sulphate precipitation and gel filtration chromatography yielded a preparation with a 12-fold increase in enzyme purity and a final specific activity of 76.67 U/mg. The purified protease was maximally active at 40ºC and at pH 10.0

Extraction, Purification And Characterization Of Artocarpus Altilis Latex Protease As A Fibrino(Geno)lytic Agent

The harvesting of Artocarpus altilis (breadfruit) in plantations involves the process of draining the latex to avoid staining of the epicarp. The exudate is not fully utilized and it has no commercial value. Ethnopharmacological applications of the latex in wound healing imply its action on blood coagulation and fibrinolysis. Partial purification of A. altilis latex through HiTrapTM SP Sepharose chromatography had purified a 72 kDa protease by 3.1-fold with 24% recovery and the specific activity of 4.87 U/mg. This serine protease was inhibited by phenylmethanesulfonyl fluoride (PMSF) (1 mM and 10 mM) with 89% and 27% of residual activities respectively. The protease showed maximal activity at pH 10 with casein and bovine serum albumin (BSA) as substrates. The protease’s apparent optimal temperature after 30 minutes of incubation was 80C. The Km and Vmax values on casein were 0.453 ± 0.026 mM and 0.022 ± 0.001 μmol/min, respectively. The protease was stable at a broad pH range (pH 4-11) with no significant reductions were detected after 24h. Thermodynamic parameters like the enthalpy (ΔH), free energy change (ΔG) and entropy (ΔS) of the protease’s inactivation at the temperature of 55-75C were estimated to be in the range of 80.10-80.27 kJ/mol, 108.34-109.32 kJ/mol and 83.97-85.58 J/mol respectively. The energy of inactivation (Ed) was 82.9 kJ/mol. A. altilis protease (0.125 U) had a comparable fibrinogen clotting capacity with thrombin (0.25 U) during the first 75 min of incubation

Optimization Process of the Pepsin-Solubilized Collagen from Lizardfish (Saurida tumbil Bloch, 1795) Skins by-Product

By-products from the marine fish processing are rich in organic compounds that can be converted into value-added products like collagen, and it is thought as an ideal candidate polymer for such research and medical applications. The lizardfish (Saurida tumbil Bloch, 1795) skin collagen had been investigated by our previous work, but an effective extraction method is needed to increase the yield of collagen. The purpose of this study was to optimize the method used to extract pepsin-solubilized collagen (PSC) from lizardfish skin. We employed an approach of one factor at a time (OFAT), along with response surface methodology (RSM) utilizing a central composite design (CCD), to attain the highest possible yield of the extracted collagen. Additionally, its properties were also assessed comparatively. The suggested optimal conditions for extraction were a pepsin concentration of 1.87%, a liquid-solid ratio of 24.90 mL/g, and a hydrolysis period of 38.09 h. Using these conditions resulted in a PSC yield of 21.82 g/100g, which closely matched the predicted collagen value

Zero-waste concept in the seafood industry: enzymatic hydrolysis perspective

The Zero-waste concept in the fish and seafood industry is consistent with the SustainableDevelopment Goal (SDG) 14, which aims to conserve and sustainably use the oceans, seas and marine resources for sustainable development. However, approximately 70% of raw materials in the fish and seafood industries are discarded and go underutilised. The increasing demand for processed fish products is expected to induce larger amounts of by-products in the near future. Fish by-products harbour valuable components like protein and essential amino acids which are potentially converted into high-value products achieved through enzymatic treatment of the by-products

Carbapenem Resistance among Marine Bacteria—An Emerging Threat to the Global Health Sector

The emergence of antibiotic resistance among pathogenic microorganisms is a major issue for global public health, as it results in acute or chronic infections, debilitating diseases, and mortality. Of particular concern is the rapid and common spread of carbapenem resistance in healthcare settings. Carbapenems are a class of critical antibiotics reserved for treatment against multidrug-resistant microorganisms, and resistance to this antibiotic may result in limited treatment against infections. In addition to in clinical facilities, carbapenem resistance has also been identified in aquatic niches, including marine environments. Various carbapenem-resistant genes (CRGs) have been detected in different marine settings, with the majority of the genes incorporated in mobile genetic elements, i.e., transposons or plasmids, which may contribute to efficient genetic transfer. This review highlights the potential of the marine environment as a reservoir for carbapenem resistance and provides a general overview of CRG transmission among marine microbes