Characterization of an extreme alkaline-stable keratinase from the draft genome of feather-degrading Bacillus sp. JM7 from deep-sea

Jin, Min; Chen, Chen; He, Xiongfei; Zeng, Runying

doi:10.1007/s13131-019-1350-5

Cited by 17 publications

(7 citation statements)

References 33 publications

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“…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%

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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Section: Biochemical Properties Of Keratinasementioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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“…For the genome of Bacillus sp. JM7, there was only one gene which was predicted to encode a subtilisin-like serine protease after genome sequencing, and this protein was verified experimentally as a keratinase ( Jin et al, 2019 ). According to a review by Vivek ( Salwan and Sharma, 2019 ), eight bacteria, including Actinomadura viridilutea (accession no.…”

Section: Discussionmentioning

confidence: 99%

A Newly Isolated Strain Lysobacter brunescens YQ20 and Its Performance on Wool Waste Biodegradation

Zhang

Zheng

et al. 2022

Front. Microbiol.

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Wool keratin is difficult to degrade as comparing to feathers because of its tough secondary structure. In order to develop an approach for high-value utilization of wool fiber waste by keratinolytic microorganisms, which is produced from shearing, weaving, and industrial processing of wool, screening of wool-degrading bacterium with high degradation efficiency were performed in this study. To this end, Lysobacter brunescens YQ20 was identified and characterized. The optimized conditions for wool degradation were pH 9.0 and 37°C with 20% liquid volume of Erlenmeyer flask. After fermentation, 15 essential amino acids were detected when wool fiber waste was fermented. The total amino acids produced from 1% wool per hour were 13.7 mg/L. The concentration was 8.6-fold higher than that produced by the strain Stenotrophomonas maltophilia BBE11-1, which had previously been reported to have the highest wool-degrading capacity. Our study reports the first Lysobacter strain that exhibits efficient wool degradation and yields higher concentrations of amino acids than previously reported strains. Whole-genome sequencing indicated that there were 18 keratinase-like genes in the genome of YQ20, which exhibited a long evolutionary distance from those of Bacillus. Therefore, L. brunescens YQ20 may have applications in the environmentally friendly management of wool waste as fertilizer in agriculture.

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“…Different methods for determining keratinase activity have been developed based on the choice of different substrates. At present, the most used substrates in keratinase activity determination are azo keratin (Lin et al, 2009a;Huang et al, 2017), azure keratin (Nahar et al, 2016;Pawar et al, 2018), soluble keratin (Fang et al, 2014Su et al, 2017;Wang et al, 2019), and feather powder Gupta et al, 2017;Jin et al, 2019;Yong et al, 2020). It must be pointed out that considering the substrate differences in solubility and composition, as well as substrate preference of keratinase, the activity determined by different substrates may differ greatly.…”

Section: Determination and Definition Of Keratinase Activitymentioning

confidence: 99%

“…Moreover, the keratinase gene of Bacillus sp. JM7 derived from a deep-sea organism was cloned into E. coli BL21(DE3) for keratinase production (Jin et al, 2019). Despite the relatively clear genetic background, as well as traits for fast growth, high cell density, and easy operation, the E. coli expression system still has some problems, such as the formation of inactive inclusion bodies and low secretory efficiency.…”

Section: Escherichia Coli Expression Systemmentioning

confidence: 99%

The tale of a versatile enzyme: Molecular insights into keratinase for its industrial dissemination

Gong

Qin

et al. 2020

Biotechnology Advances

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Characterization of an extreme alkaline-stable keratinase from the draft genome of feather-degrading Bacillus sp. JM7 from deep-sea

Cited by 17 publications

References 33 publications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

A Newly Isolated Strain Lysobacter brunescens YQ20 and Its Performance on Wool Waste Biodegradation

The tale of a versatile enzyme: Molecular insights into keratinase for its industrial dissemination

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