Papadopoulos, M. C. (1989). Effect of processing on high-protein feedstuffs: a review. Biol. Wastes 29, 123–138. doi: 10.1016/0269-7483(89)90092-X Betzel, C., Gourinath, S., Kumar, P., Kaur, P., Perbandt, M., Eschenburg, S., et al. (2001). Structure of a serine protease proteinase K from Tritirachium album limber at 0.98 Å resolution. Biochemistry 40, 3080–3088. doi: 10.1021/bi002538n Omrane Benmrad, M., Mechri, S., Zaraî Jaouadi, N., Ben Elhoul, M., Rekik, H., Sayadi, S., et al. (2019). Purification and biochemical characterization of a novel thermostable protease from the oyster mushroom Pleurotus sajor-caju strain CTM10057 with industrial interest. BMC Biotechnol. 19:43. doi: 10.1186/s12896-019-0536-4 Pinski, A., Zur, J., Hasterok, R., and Hupert-Kocurek, K. (2020). Comparative genomics of Stenotrophomonas maltophilia and Stenotrophomonas rhizophila revealed characteristic features of both species. Int. J. Mol. Sci. 21:4922. This conditioner is gorgeous! Bought the shampoo too and my hair is the best it’s been for years. Smells lovely too.

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Busk, P. K., and Lange, L. (2015). Classification of fungal and bacterial lytic polysaccharide monooxygenases. BMC Genomics 16:368. doi: 10.1186/s12864-015-1601-6 Although many keratinase producers have been isolated and identified ( Cavello et al., 2020; Jagadeesan et al., 2020; Moridshahi et al., 2020; Nnolim et al., 2020b; Reis et al., 2020), the isolation and characterization of keratinase-producing microorganisms are still an important task. The keratin degradation efficiency can be improved when more keratinases are applied ( Peng et al., 2019). Therefore, a mixture of microorganism-microbial consortia might have great potential in converting keratin-rich waste into valuable products ( Kang et al., 2020; Nasipuri et al., 2020). It is challenging to have a microbial consortium because the amount of the organism in the system will be affected under different conditions. It is also possible to set up a microbial consortium to improve keratin degradation by mixing several microorganisms which have been well characterized. This is a feasible method in industrial applications. Keratin Degradation by Keratinases Ramnani, P., Singh, R., and Gupta, R. (2005). Keratinolytic potential of Bacillus licheniformis RG1: structural and biochemical mechanism of feather degradation. Can. J. Microbiol. 51, 191–196. doi: 10.1139/w04-123Wait to wash. You’ll have to wait 3 to 4 days post-keratin treatment to get your hair wet, so if you’re not a person who likes skipping wash day, then this treatment may not be right for you, and some people report a musty smell even after washing.

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Keratinous wastes are rich in amino acids ( Qiu et al., 2020) and could affect the atmosphere, water sources, and soil if they are not treated properly ( Hassan et al., 2020). On the other hand, this type of wastes serves as a low-cost resource for amino acids or can be converted into animal feeds and fertilizers ( Pettett and Ipek, 2004; Gurav and Jadhav, 2013). Compared with other natural polymers such as cellulose, starch, and collagen, extraction of keratin is a challenging process. Quite a few strategies such as physical, chemical, and biological methods are applied in keratin extraction. Although chemical and physical treatments are efficient strategies to treat keratinous wastes, a large amount of energy is needed and amino acids were destroyed during treatment. As keratin does not accumulate in nature, microorganisms are playing the major role in its degradation and recycling. Therefore, keratinous wastes threatening the environment can be converted into value-added products by using microbial treatment ( de Menezes et al., 2021; Nnolim and Nwodo, 2021). Extensive studies have been carried out to search suitable microorganisms and obtain optimized processes to make full use of keratinous wastes ( Gradišar et al., 2000; Sangali and Brandelli, 2000; Kim et al., 2001; Rai and Mukherjee, 2011). It has been shown that wastes such as feathers can be degraded by bacteria and fungi to produce other important products such as amino acids or proteins with added values ( Callegaro et al., 2018; Shanmugasundaram et al., 2018; Bohacz, 2019; Tamreihao et al., 2019; Chaudhary et al., 2021). Therefore, conversion of the wastes using microorganisms is the most environmentally friendly method while more studies are still needed to improve the degradation efficiency of keratins. As the amount of keratin-containing wastes is increasing rapidly due to various reasons, keratin derived from the wastes should be fully utilized by serving as a source of proteins, amino acids, and a low-cost resource for producing other products. Tatineni, R., Doddapaneni, K. K., Potumarthi, R. C., and Mangamoori, L. N. (2007). Optimization of keratinase production and enzyme activity using response surface methodology with streptomyces sp7. Appl. Biochem. Biotechnol. 141:187. doi: 10.1007/bf02729061 Keratin is a rich resource in nature, and the amount of keratin-rich wastes is increasing annually. Keratinases play important roles in keratin recycle and have diverse applications in different fields. Studies need to be carried out to obtain active enzymes and enlarge their applications. Microbiology, molecular biology, structural biology, computation and biochemistry will play important roles in the research field of keratinases. Author ContributionsDeniz, I., Demir, T., Oncel, S. S., Hames, E. E., and Vardar-Sukan, F. (2021). Effect of agitation and aeration on keratinase production in bioreactors using bioprocess engineering aspects. Protein J. doi: 10.1007/s10930-021-09978-5