Search citation statements
Paper Sections
Citation Types
Year Published
Publication Types
Relationship
Authors
Journals
Keratin is a fibrous and recalcitrant protein found in feathers, nails, horns, hooves, and the epidermis of the skin. The presence of the high degree of disulfide bonds, hydrogen bonds, and hydrophobic interactions makes them resistant to mechanical stress and are not degraded by common proteases such as trypsin, pepsin, and papain. Due to the slow degradation of keratinous protein, accumulation of solid wastes from the poultry, slaughterhouse, textile, and leather industries leads to solid waste problems and other environmental and health related problems. In this review, efficient biodegradation of keratinous wastes by microorganisms, as a low-cost, environmentally friendly strategy has been discussed. Keratinases are the microbial proteases and hydrolyze the hard keratin. The decomposition of keratin by keratinases maintains the original structure of the final products, including short peptides, amino acids, and organic nitrogen which are deteriorated when traditional or chemical method is implemented. In this article, the role of keratinases producing bacterial and fungal species and their attributes has been elaborated, along with the biochemical characteristics of keratinases, and further, protein engineering approaches has been discussed, with the prospects to enhance keratinases activity for their biotechnological applications.
Keratin is a fibrous and recalcitrant protein found in feathers, nails, horns, hooves, and the epidermis of the skin. The presence of the high degree of disulfide bonds, hydrogen bonds, and hydrophobic interactions makes them resistant to mechanical stress and are not degraded by common proteases such as trypsin, pepsin, and papain. Due to the slow degradation of keratinous protein, accumulation of solid wastes from the poultry, slaughterhouse, textile, and leather industries leads to solid waste problems and other environmental and health related problems. In this review, efficient biodegradation of keratinous wastes by microorganisms, as a low-cost, environmentally friendly strategy has been discussed. Keratinases are the microbial proteases and hydrolyze the hard keratin. The decomposition of keratin by keratinases maintains the original structure of the final products, including short peptides, amino acids, and organic nitrogen which are deteriorated when traditional or chemical method is implemented. In this article, the role of keratinases producing bacterial and fungal species and their attributes has been elaborated, along with the biochemical characteristics of keratinases, and further, protein engineering approaches has been discussed, with the prospects to enhance keratinases activity for their biotechnological applications.
Background: Poultry by-products are a rich protein source that has the potential for recycling valuable products. Considering that poultry by-products are an important problem for the environment, it is necessary to find some ways to convert them into valuable products. Identifying and introducing microbial sources with the appropriate protease ability that can be used in the fermentation and conversion of non-useful waste into beneficial ones are highly important in medical and environmental terms. Objectives: The aim of the present study was to evaluate the antioxidant properties of fermented poultry by-products using proteolytic isolates. Materials and Methods: The samples were collected from a poultry slaughterhouse in Karaj, and proteolytic microorganisms were screened. Finally, two isolates (R and D) with proteolytic activity were selected for fermentation. The fermentation was performed on poultry by-products with 12.5% inoculation, 150 rpm, 1% D-glucose, and 37° C. The antioxidant activity was assessed on fermented poultry protein hydrolysates (FPPH) by some methods, such as scavenging free radicals and the ferric-reducing antioxidant power (FRAP) assay. Results: The results showed that after 24 hours of fermentation, FPPH by D with 37.7% degree of hydrolysis demonstrated 72.3% DPPH scavenging and 7.975 ± 0.36 µmol Fe (II)/L, and after 48 hours, fermented samples with 52.6% degree of hydrolysis represented 95.9% radical scavenging activity and 3.483 ± 0.28 µmol Fe (II)/L in the FRAP assay. In addition, after 24 hours of fermentation, FPPH by R with a 33.7% degree of hydrolysis illustrated 64% DPPH scavenging and 5.992 ± 0.28 µmol Fe (II)/L. After 48 hours, hydrolysates had a 54.4% degree of hydrolysis, and radical scavenging was calculated at 95.3% and 7.286 ± 0.39 µmol Fe (II)/L in the FRAP assay. Conclusion: Since poultry by-products are used for feeding, fermentation is a suitable way to improve the quality of feed.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.