Thermostable keratinase from Bacillus pumilus KS12: Production, chitin crosslinking and degradation of Sup35NM aggregates

Rajput, Rinky; Gupta, Rani

doi:10.1016/j.biortech.2013.01.091

Cited by 39 publications

(13 citation statements)

References 37 publications

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“…P5 [45]. Decreased enzyme activity beyond optimum could be a result of the negative impact of accumulated metabolic byproducts and reduction in viable cell population [46]. significantly high when compared to the concentration of 2.89 mM formed in an unoptimized medium [20] and similar studies [5,6,45].…”

Section: Optimization By Response Surface Methodology (Rsm)mentioning

confidence: 78%

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Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1

et al. 2020

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Keratinases are considerably gaining momentum in green technology because of their endowed robustness and multifaceted application potentials, such as keratinous agro-wastes valorization. Therefore, the production of novel keratinases from relatively nonpathogenic bacteria grown in agro-wastes formulated medium is cost-effective, and also imperative for the sustainability of thriving bioeconomy. In this study, we optimized keratinase production by Bacillus sp. Nnolim-K1 grown in chicken feather formulated medium. The produced keratinase (KerBNK1) was biochemically characterized and also, the keratinase-encoding gene (kerBNK1) was amplified and sequenced. The optimal physicochemical conditions for extracellular keratinase production determined were 0.8% (w/v) xylose, 1.0% (w/v) feather, and 3.0% (v/v) inoculum size, pH 5.0, temperature (25 °C) and agitation speed (150 rpm). The maximum keratinase activity of 1943.43 ± 0.0 U/mL was achieved after 120 h of fermentation. KerBNK1 was optimally active at pH and temperature of 8.0 and 60 °C, respectively; with remarkable pH and thermal stability. KerBNK1 activity was inhibited by ethylenediamine tetra-acetic acid and 1,10-phenanthroline, suggesting a metallo-keratinase. The amplified kerBNK1 showed a band size of 1104 bp and the nucleotide sequence was submitted to the GenBank with accession number MT268133. Bacillus sp. Nnolim-K1 and the keratinase displayed potentials that demand industrial and biotechnological exploitations.

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Section: Optimization By Response Surface Methodology (Rsm)mentioning

confidence: 78%

“…P5 [45]. Decreased enzyme activity beyond optimum could be a result of the negative impact of accumulated metabolic byproducts and reduction in viable cell population [46].…”

Section: Optimization By Response Surface Methodology (Rsm)mentioning

confidence: 99%

Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1

et al. 2020

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“…Using this approach, the enzymes critical for feather degradation were analyzed for anaerobic bacterium Serratia marcescens EGD-HP20 (Fuke et al, 2018). This approach might not be sufficient to identify enzymes that are required for feather degradation as the enzymes secreted into the medium are affected by cultural conditions (Rajput and Gupta, 2013). In addition to optimizing fermentation conditions to achieve high feather-degrading efficiencies, identification of secreted enzymes critical for keratin degradation should be carried out using sensitive methods such as mass spectrometry (MS).…”

Section: Perspectivementioning

confidence: 99%

Progress in Microbial Degradation of Feather Waste

2019

Front. Microbiol.

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Feathers are a major by-product of the poultry industry. They are mainly composed of keratins which have wide applications in different fields. Due to the increasing production of feathers from poultry industries, the untreated feathers could become pollutants because of their resistance to protease degradation. Feathers are rich in amino acids, which makes them a valuable source for fertilizer and animal feeds. Numerous bacteria and fungi exhibited capabilities to degrade chicken feathers by secreting enzymes such as keratinases, and accumulated evidence shows that feather-containing wastes can be converted into value-added products. This review summarizes recent progress in microbial degradation of feathers, structures of keratinases, feather application, and microorganisms that are able to secrete keratinase. In addition, the enzymes critical for keratin degradation and their mechanism of action are discussed. We also proposed the strategy that can be utilized for feather degradation. Based on the accumulated studies, microbial degradation of feathers has great potential to convert them into various products such as biofertilizer and animal feeds.

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“…Keratins are considered a biodegradable drug used to treat injuries (10). Keratin has become biocompatible and can be used as fresh and useful life-system materials from a range of sources (11).…”

Section: Results and Discussion:-mentioning

confidence: 99%

Production and Optimization Studies of the Keratinase Enzyme by Bacillus Tequilensis MBR 25

Ramya¹,

Rao²

2020

IJAR

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Feather-degrading bacteria are the enzyme keratinase-degraded community of microorganisms that may degrade feathers. They are omnipresent in the food industry in feather waste. This food sector produces large quantities of feather waste that can hardly be treated using conventional chemical and physical methods. Due to the peculiar biochemical structure of the feather, mediated by beta-keratin and reinforced by several disulfide bonds, the degradation of feather waste is typically the most cost-effective and environmentally friendly process. The present study identified a medium for the development of keratinase by shaking flask culture (Bacillus tequilensis MBR 25). Feather (1%) and maximum keratinase efficiency have been determined for the highest keratinase output. Keratinase efficiency improved when all parameters were optimized simultaneously.

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Thermostable keratinase from Bacillus pumilus KS12: Production, chitin crosslinking and degradation of Sup35NM aggregates

Cited by 39 publications

References 37 publications

Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1

Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1

Progress in Microbial Degradation of Feather Waste

Production and Optimization Studies of the Keratinase Enzyme by Bacillus Tequilensis MBR 25

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