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      Fusarium oxysporum and Aspergillus sp. as Keratinase Producers Using Swine Hair From Agroindustrial Residues

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          Abstract

          Technological processes mediated by microorganisms and enzymes are promising alternatives for treatment of recalcitrant residues. Keratinases hydrolyze keratin, the primary component of some wastes generated in many industrial activities. The present study was designed to evaluate strategies for obtaining keratinases produced by fungi using submerged fermentation and two residues as substrates, chicken feathers and swine hair. Two fungi isolated from feather residues showed potential for keratinase production, Fusarium oxysporum and Aspergillus sp. These were subjected to submerged fermentation using chicken feathers and swine hair prepared in three conditions (microbial concentration reduction, sterilization and hydrogen peroxide). The residual mass was quantified and tested for keratinase production. The most potent enzymatic extract was used in the precipitation technique with salts and organic solvents. The best results of enzymatic activity were obtained using F. oxysporum, on the 6thday of fermentation, obtaining 243.25 U mL –1 using sterilized swine hair as the substrate. Aspergillus sp. showed the highest keratinolytic activity on the 9thday, 113.50 U mL –1 using feathers as the substrate. The highest degradation percentage was 59.20% (w/w) in swine hair and the precipitation technique, with relative activities close to 50%. The results are promising for the application of residues and microorganisms in biotechnological processes of economic and environmental interest.

          Graphical Abstract

          Schematic diagram of keratinases production using swine hair from agroindustrial residues.

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          Most cited references52

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          Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration

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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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              Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubility.

              Protein solubility is a problem for many protein chemists, including structural biologists and developers of protein pharmaceuticals. Knowledge about how intrinsic factors influence solubility is limited due to the difficulty of obtaining quantitative solubility measurements. Solubility measurements in buffer alone are difficult to reproduce, because gels or supersaturated solutions often form, making it impossible to determine solubility values for many proteins. Protein precipitants can be used to obtain comparative solubility measurements and, in some cases, estimations of solubility in buffer alone. Protein precipitants fall into three broad classes: salts, long-chain polymers, and organic solvents. Here, we compare the use of representatives from two classes of precipitants, ammonium sulfate and polyethylene glycol 8000, by measuring the solubility of seven proteins. We find that increased negative surface charge correlates strongly with increased protein solubility and may be due to strong binding of water by the acidic amino acids. We also find that the solubility results obtained for the two different precipitants agree closely with each other, suggesting that the two precipitants probe similar properties that are relevant to solubility in buffer alone. Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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                Author and article information

                Contributors
                Journal
                Front Bioeng Biotechnol
                Front Bioeng Biotechnol
                Front. Bioeng. Biotechnol.
                Frontiers in Bioengineering and Biotechnology
                Frontiers Media S.A.
                2296-4185
                11 February 2020
                2020
                : 8
                : 71
                Affiliations
                [1] 1Laboratory of Microbiology and Bioprocess, Federal University of Fronteira Sul , Erechim, Brazil
                [2] 2Department of Chemical and Food Engineering, Federal University of Santa Catarina , Florianópolis, Brazil
                [3] 3Department of Agricultural Science, Agricultural Engineering Post-Graduate Program, Universidade Estadual do Oeste do Paraná , Cascavel, Brazil
                [4] 4Laboratory of Applied Virology, Federal University of Santa Catarina , Florianópolis, Brazil
                Author notes

                Edited by: Saurabh Dhiman, South Dakota School of Mines & Technology, United States

                Reviewed by: Zhen Fang, Jiangsu University, China; Rajni Singh, Amity University, India; Zhangjun Cao, Donghua University, China

                This article was submitted to Bioprocess Engineering, a section of the journal Frontiers in Bioengineering and Biotechnology

                Article
                10.3389/fbioe.2020.00071
                7026017
                ef3eeb9d-d6f9-4fa9-aa9e-406616f4aa44
                Copyright © 2020 Preczeski, Dalastra, Czapela, Kubeneck, Scapini, Camargo, Zanivan, Bonatto, Stefanski, Venturin, Fongaro and Treichel.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 27 November 2019
                : 27 January 2020
                Page count
                Figures: 1, Tables: 1, Equations: 1, References: 55, Pages: 8, Words: 0
                Funding
                Funded by: Conselho Nacional de Desenvolvimento Cientà–fico e Tecnológico 10.13039/501100003593
                Categories
                Bioengineering and Biotechnology
                Original Research

                biotechnology process,agroindustry residues,enzyme precipitation,keratinase,swine hair

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