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      Effective multi-functional biotechnological applications of protease/keratinase enzyme produced by new Egyptian isolate ( Laceyella sacchari YNDH)

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          Abstract

          Background

          Due to a multitude of industrial applications of keratinolytic proteases, their demands are increasing. The present investigation studied the production and monitoring of the most possible multi-functional applications of YNDH thermoalkaline keratin-degrading enzyme.

          Results

          This work is considered the first that reported YNDH strain closely related to Laceyella sacchari strain; YNDH is a producer of protease/keratinase enzyme and able to degrade natural keratin such as feathers, wool, human hairs, and nails. Experimental design Plackett-Burman (PBD) was applied to evaluate culture conditions affecting the production of thermoalkaline protease/keratinase. Afterwards, Box-Behnken design (BBD) was applied to find out the optimum level of significant variables namely, NH 4Cl, yeast extract, and NaNO3 with a predicted activity of 1324.7 U/ml. Accordingly, the following medium composition and parameters were calculated to be optimum (%w/v): NH4Cl, 0.08; feather, 1; yeast extract, 0.04; MgSO 4.7H 2O, 0.02; NaNO 3, 0.016; KH 2PO 4, 0.01; K 2HPO 4, 0.01; pH, 8; inoculum size; 5%, cultivation temperature (Temp.) 45 °C and incubation time 48 h. The studied enzyme can degrade keratin-azure, remove proteinaceous materials, and is able to remove hairs from goat hides. These interesting characteristics make this enzyme a good candidate in many applications especially in detergent (Det.), in leather industries, and in pharmaceuticals particularly in nail treatment.

          Conclusion

          The promising properties of the newly keratin-degrading protease enzyme from Laceyella sacchari strain YNDH would underpin its efficient exploitation in several industries to cope with the demands of worldwide enzyme markets.

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          Most cited references37

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          Some New Three Level Designs for the Study of Quantitative Variables

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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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              A review: Potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources

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                Author and article information

                Contributors
                doaa.rashid@yahoo.com
                arbassiouny@gmail.com
                nihadabdelmonem@gmail.com
                nadiastuttgart@yahoo.com
                yasser1967@yahoo.com
                Journal
                J Genet Eng Biotechnol
                J Genet Eng Biotechnol
                Journal of Genetic Engineering & Biotechnology
                Springer Berlin Heidelberg (Berlin/Heidelberg )
                1687-157X
                2090-5920
                2 July 2020
                2 July 2020
                December 2020
                : 18
                : 23
                Affiliations
                [1 ]GRID grid.420020.4, ISNI 0000 0004 0483 2576, Bioprocess Development Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), , City of Scientific Research and Technological Applications (SRTA-City), ; New Burg El-Arab City, Universities and Research Institutes Zone, Alexandria, Post 21934 Egypt
                [2 ]Biochemistry Department, Faculty of Science, Alexandria, Egypt
                Article
                37
                10.1186/s43141-020-00037-7
                7332587
                32617705
                470956f5-a6a3-481f-9ea0-dfaf3e5f5036
                © The Author(s) 2020

                Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 15 March 2020
                : 4 June 2020
                Categories
                Research
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                © The Author(s) 2020

                protease,keratinolytic activity,experimental design,laceyella sacchari yndh

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