Comprehensive insights into microbial keratinases and their implication in various biotechnological and industrial sectors: A review

Hassan, Mohamed A.; Abol-Fotouh, Deyaa; Omer, Ahmed M.; Tamer, Tamer M.; Abbas, Eman

doi:10.1016/j.ijbiomac.2020.03.116

Cited by 84 publications

(56 citation statements)

References 205 publications

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“…As observed from the study keratinase, more drastic effect of pH on biocatalyst may lead to complete loss of activity. The pH optima of bacterial keratinases have been extensively documented within the range of 7.0 to 9.0 [ 24 , 40 ]. However, some reports on alkalophilic keratinase abound with pH optima ≥11.0 [ 4 ].…”

Section: Discussionmentioning

confidence: 99%

Bacillus sp. CSK2 produced thermostable alkaline keratinase using agro-wastes: keratinolytic enzyme characterization

Nnolim

Nwodo

2020

BMC Biotechnol

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Background Chicken feathers are the most abundant agro-wastes emanating from the poultry processing farms and present major concerns to environmentalists. Bioutilization of intractable feather wastes for the production of critical proteolytic enzymes is highly attractive from both ecological and biotechnological perspectives. Consequently, physicochemical conditions influencing keratinase production by Bacillus sp. CSK2 on chicken feathers formulation was optimized, and the keratinase was characterized. Results The highest enzyme activity of 1539.09 ± 68.14 U/mL was obtained after 48 h of incubation with optimized conditions consisting of chicken feathers (7.5 g/L), maltose (2.0 g/L), initial fermentation pH (5.0), incubation temperature (30 °C), and agitation speed (200 rpm). The keratinase showed optimal catalytic efficiency at pH 8.0 and a temperature range of 60 °C – 80 °C. The keratinase thermostability was remarkable with a half-life of above 120 min at 70 °C. Keratinase catalytic efficiency was halted by ethylenediaminetetraacetic acid and 1,10-phenanthroline. However, keratinase activity was enhanced by 2-mercaptoethanol, dimethyl sulfoxide, tween-80, but was strongly inhibited by Al3+ and Fe3+. Upon treatment with laundry detergents, the following keratinase residual activities were achieved: 85.19 ± 1.33% (Sunlight), 90.33 ± 5.95% (Surf), 80.16 ± 2.99% (Omo), 99.49 ± 3.11% (Ariel), and 87.19 ± 0.26% (Maq). Conclusion The remarkable stability of the keratinase with an admixture of organic solvents or laundry detergents portends the industrial and biotechnological significance of the biocatalyst.

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Section: Discussionmentioning

confidence: 99%

Bacillus sp. CSK2 produced thermostable alkaline keratinase using agro-wastes: keratinolytic enzyme characterization

Nnolim

Nwodo

2020

BMC Biotechnol

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“…The insolubility of some proteinaceous substrates could be prompted by inherent inter-or intramolecular forces such as disulfide bonds that confer mechanical stability to some structural proteins; hence, accessibility of peptide bonds by classical proteases remains impossible (Navone and Speight, 2018). Keratinases, on the other hand, have been naturally endowed with hydrolytic potentials for both soluble and insoluble proteins, and have been adopted, widely as promising candidates in many biotechnological processes (Hassan et al, 2020a). Yamamura et al (2002) reported that the catalytic efficiencies established for subtilisin Carlsberg and proteinase K toward synthetic substrates were similar to those of protease D-1 from Stenotrophomonas sp.…”

Section: Biochemical Properties Of Keratinasementioning

confidence: 99%

“…Limitations associated with proteases derived from wild-type microbial species in industrial applications include low tolerance to some industrial operations and processing conditions such as pH, temperature, presence of organic solvents, salt, detergent, and oxidative agents. These factors drastically diminish the catalytic performance and applicability of the enzymes (Gupta and Ramnani, 2006;Brandelli et al, 2010;Hassan et al, 2020a). Keratinase, on the other hand, displays unique attributes that may be exploited in bioprocessing such as keratin bioconversion to useful products, textile treatment, leather depilation, and other industrial applications (Fang et al, 2013;Kalaikumari et al, 2019).…”

Section: Keratinase Catalytic Efficiency Enhancement -A Protein Enginmentioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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The search for novel renewable products over synthetics hallmarked this decade and those of the recent past. Most economies that are prospecting on biodiversity for improved bio-economy favor renewable resources over synthetics for the potential opportunity they hold. However, this field is still nascent as the bulk of the available resources are non-renewable based. Microbial metabolites, emphasis on secondary metabolites, are viable alternatives; nonetheless, vast microbial resources remain under-exploited; thus, the need for a continuum in the search for new products or bio-modifying existing products for novel functions through an efficient approach. Environmental distress syndrome has been identified as a factor that influences the emergence of genetic diversity in prokaryotes. Still, the process of how the change comes about is poorly understood. The emergence of new traits may present a high prospect for the industrially viable organism. Microbial enzymes have prominence in the bio-economic space, and proteases account for about sixty percent of all enzyme market. Microbial keratinases are versatile proteases which are continuously gaining momentum in biotechnology owing to their effective bio-conversion of recalcitrant keratin-rich wastes and sustainable implementation of cleaner production. Keratinase-assisted biodegradation of keratinous materials has revitalized the prospects for the utilization of cost-effective agro-industrial wastes, as readily available substrates, for the production of high-value products including amino acids and bioactive peptides. This review presented an overview of keratin structural complexity, the potential mechanism of keratin biodegradation, and the environmental impact of keratinous wastes. Equally, it discussed microbial keratinase; vis-à-vis sources, production, and functional properties with considerable emphasis on the ecological implication of microbial producers and catalytic tendency improvement strategies. Keratinase applications and prospective high-end use, including animal hide processing, detergent formulation, cosmetics, livestock feed, and organic fertilizer production, were also articulated.

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“…The evaluation of the macro-state of keratinase research, based on the information available from the WoS database, generally showed a trajectory growth pattern of research products. Notably, the recent past decade recorded the highest number of publications and this may be attributed to the involvement of more active researchers, adequate research funding, availability of state-of-the-art facilities and most importantly, the foreseeable application prospects of microbial keratinase in green technology (Rosenbloom et al 2015;Hassan et al 2020). Keywords associated with keratinase research spotlight the hotspots and dimensions of researches over the study period.…”

Section: Discussionmentioning

confidence: 99%

Microbial keratinase and the bio-economy: a three-decade meta-analysis of research exploit

Nnolim

Nwodo

2021

AMB Expr

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Microbial keratinase research has been on an upward trajectory due to the robustness and efficiency of the enzyme toward various green technological processes that promote economic development and environmental sustainability. A compendium of research progression and advancement within the domain was achieved through a bibliometric study to understand the trend of research productivity, scientific impacts, authors' involvement, collaboration networks, and the advancement of knowledge gaps for future research endeavours. A three-decade (1990 to 2019) scholarly published articles were retrieved from the web of science database using a combination of terms "keratinas* or keratinolytic proteas* or keratinolytic enzym*", and subsequently analyzed for bibliometric indicators. A collection of 330 peer-reviewed, research, articles were retrieved for the survey period and authored by 1063 researchers with collaboration index of 3.27. Research productivity was most in 2013 with total research output of 28 articles. The top three authors' keywords were keratinase, keratin and protease with a respective frequency of 188, 26 and 22. India, China and Brazil ranked top in terms of keratinase research outputs and total citation with respective article productivity (total citations) of 85 (1533), 57 (826), and 36 (764). This study evaluated the trend of keratinase research outputs, scientific impact, collaboration networks and biotechnology innovations. It has the potentials to influence positively decision making on future research direction, collaborations and development of products for the bio-economy.

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Comprehensive insights into microbial keratinases and their implication in various biotechnological and industrial sectors: A review

Cited by 84 publications

References 205 publications

Bacillus sp. CSK2 produced thermostable alkaline keratinase using agro-wastes: keratinolytic enzyme characterization

Bacillus sp. CSK2 produced thermostable alkaline keratinase using agro-wastes: keratinolytic enzyme characterization

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial keratinase and the bio-economy: a three-decade meta-analysis of research exploit

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