Stomach extract of Atlantic herring Clupea harengus, Atlantic salmon Salmo salar, cod Gadus morhua, redfish Sebastes marinus, and plaice Pleuronectes platessa, degraded human epidermal keratin effectively in vitro. The keratin-degrading activity of all extracts showed a pH optimum around 3.3-3.4, and sheets of plantar callus were degraded with about the same efficacy as keratin. Pepstatin sensitivity, heat lability, and the acidic pH optimum demonstrated that the keratin-degrading activity was pepsin. The keratin-degrading activity of cod stomach extract had a temperature optimum of around 42 degrees C at optimal pH, and showed a similar pH dependency with collagen as with keratin as substrate. The keratin-degrading activity of pepsin I and pepsin II purified from cod showed a pH optimum of 3.7 and 3.1, respectively, similar to that obtained with hemoglobin as substrate. Pig pepsin showed a pH optimum of about 2 with keratin, hemoglobin, and collagen as substrates. The present investigation demonstrates that fish pepsin is effective in degrading human epidermal keratin in vitro, and in a contemporary study the same was shown with fish trypsin. This may suggest a possible mechanism for the development of irritative hand eczema caused by exposure to fish and acidified fish material.
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Heliyon
May 2024
Department of Biotechnology and Food Technology, Faculty of Science, University of Johannesburg, Doornfontein Campus, PO Box 17011, Doornfontein, Johannesburg, 2028, South Africa.
Research on proteases and secondary metabolites from endophytes is an area that requires attention from researchers. In this study, proteases from sp. strain MHSD16 and sp.
View Article and Find Full Text PDFFront Microbiol
May 2023
Department of Animal Science, Ilam University, Ilam, Iran.
The keratin-degrading bacterium secretes a keratinase with potential industrial interest. Here, the Keratinase gene was intracellularly expressed in BL21(DE3) using pET-21b (+) vector. Phylogenetic tree analysis showed that KRLr1 is closely related to keratinase that belongs to the serine peptidase/subtilisin-like S8 family.
View Article and Find Full Text PDFMol Genet Genomics
March 2023
Institute of Sustainable Processes, Dr. Mergelina S/N, 47011, Valladolid, Spain.
Keratin-rich wastes, mainly in the form of feathers, are recalcitrant residues generated in high amounts as by-products in chicken farms and food industry. Polylactic acid (PLA) is the second most common biodegradable polymer found in commercial plastics, which is not easily degraded by microbial activity. This work reports the 3.
View Article and Find Full Text PDFSci Total Environ
November 2022
Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China; Science Center for Future Foods, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China. Electronic address:
Keratinase-catalyzed degradation of keratin waste has been shown to be a promising recycling method. Although the recombinant KerZ1 derived from Bacillus subtilis has shown the highest activity among the keratinases reported so far, the low thermal stability caused by the unstable flexible loops limited its keratin-degrading ability. To this end, the flexible loops of KerZ1 were engineered to be more hydrophobic and rigid through B-factor calculations, molecular dynamics simulations, and β-turn redesign.
View Article and Find Full Text PDFJ Genet Eng Biotechnol
May 2022
Centro de Investigación y Desarrollo en Fermentaciones Industriales, Facultad de Ciencias Exactas (CINDEFI, CCT La Plata-CONICET, UNLP), Universidad Nacional de la Plata, Calle 47 y 115, (B1900ASH), 1900, La Plata, Argentina.
Background: Antarctica is one of the harshest environments in the world. Despite this fact, it has been colonized by microorganisms, which had to develop different adaptations in order to survive. By studying their enzymes, we can harness these adaptations in order to use them in various industrial processes.
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