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Biotechnological Aspects and Perspective of Microbial Keratinase Production

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      Abstract

      Keratinases are proteolytic enzymes predominantly active when keratin substrates are available that attack disulfide bridges in the keratin to convert them from complex to simplified forms. Keratinases are essential in preparation of animal nutrients, protein supplements, leather manufacture, textile processing, detergent formulation, feather meal processing for feed and fertilizer, the pharmaceutical and biomedical industries, and waste management. Accordingly, it is necessary to develop a method for continuous production of keratinase from reliable sources that can be easily managed. Microbial keratinase is less expensive than conventionally produced keratinase and can be obtained from fungi, bacteria, and actinomycetes. In this overview, the expansion of information about microbial keratinases and important considerations in keratinase production are discussed.

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      Microbial keratinases and their prospective applications: an overview.

      Microbial keratinases have become biotechnologically important since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide "keratin" recalcitrant to the commonly known proteolytic enzymes trypsin, pepsin and papain. These enzymes are largely produced in the presence of keratinous substrates in the form of hair, feather, wool, nail, horn etc. during their degradation. The complex mechanism of keratinolysis involves cooperative action of sulfitolytic and proteolytic systems. Keratinases are robust enzymes with a wide temperature and pH activity range and are largely serine or metallo proteases. Sequence homologies of keratinases indicate their relatedness to subtilisin family of serine proteases. They stand out among proteases since they attack the keratin residues and hence find application in developing cost-effective feather by-products for feed and fertilizers. Their application can also be extended to detergent and leather industries where they serve as specialty enzymes. Besides, they also find application in wool and silk cleaning; in the leather industry, better dehairing potential of these enzymes has led to the development of greener hair-saving dehairing technology and personal care products. Further, their prospective application in the challenging field of prion degradation would revolutionize the protease world in the near future.
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        Biochemical features of microbial keratinases and their production and applications.

        Keratinases are exciting proteolytic enzymes that display the capability to degrade the insoluble protein keratin. These enzymes are produced by diverse microorganisms belonging to the Eucarya, Bacteria, and Archea domains. Keratinases display a great diversity in their biochemical and biophysical properties. Most keratinases are optimally active at neutral to alkaline pH and 40-60 degrees Celsius, but examples of microbial keratinolysis at alkalophilic and thermophilic conditions have been well documented. Several keratinases have been associated to the subtilisin family of serine-type proteases by analysis of their protein sequences. Studies with specific substrates and inhibitors indicated that keratinases are often serine or metalloproteases with preference for hydrophobic and aromatic residues at the P1 position. Keratinolytic enzymes have several current and potential applications in agroindustrial, pharmaceutical, and biomedical fields. Their use in biomass conversion into biofuels may address the increasing concern on energy conservation and recycling.
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          Biodegradation of keratin waste: Theory and practical aspects.

          Keratin-rich by-products, i.e. bristles, horns and hooves, chicken feathers and similar, are a source of nutrients for animals (amino acids) and plants (N, S). Contemporary developments in the management of keratin waste in feeds and fertilizers comply with human and animal health protection regulations and respect the principles of ecological development. Biotechnological methods employing keratinolytic bacteria and microscopic fungi play a key role in processing keratin waste. This study reviews the current knowledge on the ecology and physiology of keratinolytic microorganisms and presents the biodegradation mechanism of native keratin. The structure and chemical composition of keratin proteins are described, and methods of keratin waste biotransformation into products of practical industrial and natural value, especially composts, are discussed. Copyright © 2011 Elsevier Ltd. All rights reserved.
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            Author and article information

            Affiliations
            1Institute of Nano Electronic Engineering (INEE), Universiti Malaysia Perlis, 01000 Kangar, Perlis, Malaysia
            2Advanced Medical & Dental Institute (AMDI), Universiti Sains Malaysia, 13200 Kepala Batas, Penang, Malaysia
            3Department of Oral Biology & Biomedical Sciences and OCRCC, Faculty of Dentistry, University of Malaya, 50603 Kuala Lumpur, Malaysia
            4Department of Biological Engineering, College of Engineering, Inha University, Incheon 402-751, Republic of Korea
            Author notes
            *Subash C. B. Gopinath: subash@ 123456unimap.edu.my and
            *Periasamy Anbu: anbu25@ 123456yahoo.com

            Academic Editor: Bidur P. Chaulagain

            Journal
            Biomed Res Int
            Biomed Res Int
            BMRI
            BioMed Research International
            Hindawi Publishing Corporation
            2314-6133
            2314-6141
            2015
            9 June 2015
            : 2015
            4477050
            10.1155/2015/140726
            Copyright © 2015 Subash C. B. Gopinath et al.

            This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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