Biochemical characterisation and application of keratinase from Bacillus thuringiensis MT1 to enable valorisation of hair wastes through biosynthesis of vitamin B-complex

Hassan, Mohamed A.; Taha, Tarek H.; Hamad, Gamal M.; Hashem, Mohamed; Alamri, Saad; Mostafa, Yasser S.

doi:10.1016/j.ijbiomac.2020.03.032

Cited by 48 publications

(31 citation statements)

References 52 publications

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“…However, some reports on alkalophilic keratinase abound with pH optima ≥11.0 [ 4 ]. The pH stability of the keratinase may be likened to that demonstrated by the alkaline keratinase from B. thuringiensis MT1 [ 12 ] and Bacillus subtilis RSE163 [ 41 ]. Conversely, Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

“…However, all this approach is expensive and not environmentally friendly. On a similar note, the physical-mechanical valorization approach always, is, saddled with loss of essential constituents in the feather meal [ 12 ].…”

Section: Introductionmentioning

confidence: 99%

“…Keratinases have potential applications in various sectors including the leather production, detergent formulation, pharmaceuticals and biomedicine [ 12 , 14 ], not only because of their catalytic efficiency, but also due to sustainable production on a cost-effective renewable resource. The ability of keratinases to hydrolysis both the soluble and insoluble proteinaceous stains; and robustness in the presence of chemical agents promoted their industrial significance as bio-additive for detergent formulation [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

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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%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Nnolim

Nwodo

2020

BMC Biotechnol

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“…However, a few extremely alkalophilic keratinases with optimum pH between 10 and 13 were previously reported (Friedrich and Antranikian, 1996;Letourneau et al, 1998;Mitsuiki et al, 2006;Jaouadi et al, 2008Jaouadi et al, , 2010Tatineni et al, 2008;Benkiar et al, 2013;Paul et al, 2014b;Gong et al, 2015;Tian et al, 2019). The optimum temperature reported for the activity of several microbial keratinases was between 37 and 65 • C (Hossain et al, 2007;Bach et al, 2011;Jaouadi et al, 2013;Wu et al, 2017;Hassan et al, 2020b), whereas thermophilic keratinolytic proteases already characterized function optimally between 70 and 100 • C (Nam et al, 2002;Jaouadi et al, 2010;Kuo et al, 2012;Benkiar et al, 2013;Paul et al, 2014b;Gong et al, 2015). Many keratinases, irrespective of the sources, have been found to be catalytically active and stable over a temperature and pH range of 20 to 100 • C, and 4 to 13, respectively (Jaouadi et al, 2008(Jaouadi et al, , 2010Paul et al, 2014b;Gong et al, 2015;Jin et al, 2019).…”

Section: Biochemical Properties Of Keratinasementioning

confidence: 99%

“…An overview of various reports on keratinolytic proteases of microbial sources shows different molecular weight range from 17 to 240 kDa (Friedrich and Antranikian, 1996;Bressollier et al, 1999;Nam et al, 2002;Bernal et al, 2006;Mitsuiki et al, 2006;Kim, 2007;Tatineni et al, 2008;Benkiar et al, 2013;Fang et al, 2013;Jaouadi et al, 2013;Hamiche et al, 2019;Hassan et al, 2020b). Keratinases from S. maltophilia BBE11-1 (Fang et al, 2013) and S. albidoflavus (Bressollier et al, 1999) have so far been documented to have low molecular weights of 17 and 18 kDa, respectively.…”

Section: Biochemical Properties Of Keratinasementioning

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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Engineered pro‐peptide enhances the catalytic activity of keratinase to improve the conversion ability of feather waste

Peng

Zhang

Song

et al. 2021

Biotech & Bioengineering

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Keratinase is an attractive industrial enzyme that can specifically catalyze keratin waste to obtain value-added products. A challenge to the application of keratinase is improving catalytic capacity to achieve efficient hydrolysis. In this study, we effectively expressed the keratinase gene from Bacillus licheniformis BBE11-1 in Bacillus subtilis WB600 based on pro-peptide engineering. Partial deletion of the pro-peptide sequence and the substitution of amino acid at the pro-peptide cleavage site (P1) suggested that the "chaperone effect" and "cleavage efficiency" of the pro-peptide determine the activity of the mature enzyme. Subsequently, seven target sites that can increase the activity of the mature enzyme by 16%-66% were obtained through the multiple sequence alignment of pro-peptides and site-directed mutation. We further performed combinatorial mutations at six sites based on the design principle of three-codon saturation mutations and obtained mutant 2-D12 (236.8 KU/mg) with a mature enzyme activity of 186% of the original (127.6 KU/mg). Finally, continuous fermentation was carried out in a 5-L bioreactor for 22 h, and the activity of the 2-D12 mature enzyme was increased to 391.6 KU/mg. Most importantly, 2-D12 could degrade more than 90% of feather waste into amino acids and peptides within 12 h with the aid of sulfite.

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Biochemical characterisation and application of keratinase from Bacillus thuringiensis MT1 to enable valorisation of hair wastes through biosynthesis of vitamin B-complex

Cited by 48 publications

References 52 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

Engineered pro‐peptide enhances the catalytic activity of keratinase to improve the conversion ability of feather waste

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