Characterization and overexpression of a novel keratinase from Bacillus polyfermenticus B4 in recombinant Bacillus subtilis

Dong, Yu-Ze; Chang, Wen-Shous; Chen, Po-Ting

doi:10.1186/s40643-017-0177-1

Cited by 27 publications

(15 citation statements)

References 41 publications

(49 reference statements)

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“…Pressurized cooking or chemical treatment of feathers was the fundamental method of processing used in preparing feather meal. This method of processing involves high energy input, and it, therefore, denatures important heatlabile proteins (Onifade et al, 1998;Dong et al, 2017). The potentials presented by keratinolytic microbes and keratinases are an indication of the possibilities that the bio-recycling process holds for the husbandry sector of the agro-industry (Gegeckas et al, 2018).…”

Section: Livestock Feedmentioning

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: Livestock Feedmentioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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“…Keratin degradation is attracting biotechnological attention since it might provide a substitute way of waste management as well as the production of valuable products (Brandeli andRiffel 2006, Pasupuleti et al, 2010). Bacillus was used for their keratinases production, optimization and characterization (Sahoo et al, 2012, Dong et al, 2017, Arokiyaraj et al, 2019. Tiwary and Gupta (2012) used Bacillus licheniformis to study the conversion of the chicken feather into feather meal.…”

Section: Introductionmentioning

confidence: 99%

Chicken feather waste degradation by Alternaria tenuissima and its application on plant growth

Kumari

Kumar

2020

JANS

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The use of chicken as food is rising day today and as byproduct 8.5 billion tons, poultry feathers are produced worldwide, whereas India contributes about 350 million tons per annum. It is a waste product of poultry industries, are considered a potential high-quality protein supplement owing to their crude protein content of more than 85%. In the present study Alternaria tenuissima a keratinophilic fungus was used for feather degradation in submerged state fermentation and soil. Total Protein releases were studied in submerged state fermentation by A. tenuissima are 122µg/ml and 238µg/ml in 15 and 25 days respectively. Lysine, Methionine, Cysteine and Valine were found 15.8, 6.8, 20.2, 7.5 µg/ml in 25 days, respectively. Chicken feathers were mixed with soil and inoculated with spore suspension for degradation of complex keratin protein into simpler organic forms. A. tenuissima degraded feathers in soil and enhances nutritional value. Five-gram feathers in 250 g soil mixtures were found better growth enhancers and increased height. This work will reduce the solid waste generated in the form of feathers from the poultry industry, and convert it into a simpler organic form that can be used by plants.

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“…Diverse groups of microorganisms are reported to produce keratinases (Kalia and Purohit, 2008 ), such as numerous Bacillus sp. (Gupta and Singh, 2013 ; Gupta et al, 2015 ; Dong et al, 2017 ; Hamiche et al, 2019 ; Nnolim et al, 2020b ; Almahasheer et al, 2022 ; Devi et al, 2022 ; Mazotto et al, 2022 ), Aspergillus oryzae (Farag and Hassan, 2004 ), Paecilomyces marquandii and Doratomyces microsporum (Gradisar et al, 2005 ), Streptomyces sp. (Tatineni et al, 2008 ), Stenotrophomonas maltophilia (Cao et al, 2009 ), Myrothecium verrucaria (Moreira-Gasparin et al, 2009 ), Thermoactinomyces sp.…”

Section: Introductionmentioning

confidence: 99%

Chicken Feather Waste Valorization Into Nutritive Protein Hydrolysate: Role of Novel Thermostable Keratinase From Bacillus pacificus RSA27

et al. 2022

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Microbial keratinases exhibit a momentous role in converting keratin biowastes into exceedingly valuable protein supplements. This study reports a novel, highly stable keratinase from Bacillus pacificus RSA27 for the production of pure peptides rich in essential amino acids from chicken feathers. Purified keratinase showed a specific activity of 38.73 U/mg, 2.58-fold purification, and molecular weight of 36 kDa. Kinetic studies using a chicken feather as substrate report Km and Vmax values of 5.69 mg/ml and 142.40 μg/ml/min, respectively, suggesting significant enzyme-substrate affinity/biocatalysis. Identification and in silico structural-functional analysis of keratinase discovered the presence of distinct amino acid residues and their positions. Besides, keratinase possesses a high-affinity calcium-binding site (Asp128, Leu162, Asn164, Ile166, and Val168) and a catalytic triad of Asp119, His151, and Ser308, known attributes of serine protease (subtilisin family). Furthermore, a scale-up to 5 L fermenter revealed complete feather hydrolysis (94.5%) within 24 h with high activity (789 U/ml) and total amino acid of 153.97 μmol/ml. Finally, cytotoxicity evaluation of protein hydrolysate resulted in negligible cytotoxic effects (1.02%) on the mammalian hepatoblastoma cell line, signifying its potential biotechnological applications.

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Characterization and overexpression of a novel keratinase from Bacillus polyfermenticus B4 in recombinant Bacillus subtilis

Cited by 27 publications

References 41 publications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Chicken feather waste degradation by Alternaria tenuissima and its application on plant growth

Chicken Feather Waste Valorization Into Nutritive Protein Hydrolysate: Role of Novel Thermostable Keratinase From Bacillus pacificus RSA27

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