Isolation and partial characterisation of extracellular keratinase from a wool degrading thermophilic actinomycete strain<i>Thermoactinomyces candidus</i>

Ignatova, Zoya; Gousterova, A.; Spassov, G.; Nedkov, P.

doi:10.1139/w98-230

Cited by 90 publications

(48 citation statements)

References 28 publications

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“…The time required for wool decomposition was however not shortened (data not shown). Our results are in good agreement with previous research [40,41].…”

Section: Bacillus Pumilus Strain Cicchlj Q89supporting

confidence: 94%

A Bacillus Strain Able to Hydrolyze Alpha- and Beta-Keratin

Fellahi

Zaghloul²,

Feuk-Lagerstedt³

et al. 2014

J Bioproces Biotech

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The ability to hydrolyze keratin, a rigid and strongly cross-linked protein in the waste of poultry feather and sheep wool, has made keratinase production by microorganisms highly important to the biotechnological industry. A proteindegrading bacterium (C 4 ) was isolated from compost. Based on morphology and biochemical tests, along with 16S rRNA sequencing, the isolated C 4 was tentatively identified as Bacillus sp. C 4 (2008). The proteolytic activity of the Bacillus sp. C 4 strain was broadly specific; it degraded keratinous and non-keratinous proteins to different degrees. Pea pods as substrate generated the highest protease production, followed by soybean meal and sheep wool. Notwithstanding, using wool keratin as a sole source of carbon and nitrogen yielded the highest level of soluble proteins. Furthermore, the C 4 bacterium grew well, and produced a significant level of keratinase when using wool and feather as substrates. Supplementing the medium with yeast extract and peptone shortened the time required for feather degradation, but delayed the onset of the wool keratin hydrolysis with two days. The predominant amino acids released in feather hydrolysate were tyrosine, phenylalanine, and histidine. In contrast, the wool lysate was rich in aspartic acid, methionine, tyrosine, phenylalanine, histidine, and lysine. Results established that utilizing the C 4 strain for keratin degradation in waste management holds considerable potential.

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“…The time required for wool decomposition was however not shortened (data not shown). Our results are in good agreement with previous research [40,41].…”

Section: Bacillus Pumilus Strain Cicchlj Q89supporting

confidence: 94%

A Bacillus Strain Able to Hydrolyze Alpha- and Beta-Keratin

Fellahi

Zaghloul²,

Feuk-Lagerstedt³

et al. 2014

J Bioproces Biotech

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“…A number of mesophilic Streptomyces (Böckle et al 1995;Jaouadi et al 2010;Bressollier et al 1999;Gushterova et al 2005;Szabo et al 2000;Letourneau et al 1998;Xie et al 2010;Tatineni et al 2008) and thermophic Streptomyces sp. (Chitte et al 1999;Gushterova et al 2005Gushterova et al , 2012Syed et al 2009;Ignatova et al 1999;Vasileva-Tonkova et al 2009a) produced keratinases that break down keratin. Another promising keratinase was isolated from…”

Section: Sources Of Microbial Keratinasesmentioning

confidence: 99%

Microbial keratinases: characteristics, biotechnological applications and potential.

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2016

The Handbook of Microbial Bioresources

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Keratinases are a group of proteolytic enzymes that can catalyse the cleavage and hydrolysis of the highly stable and fibrous proteins: keratins. A diverse range of microorganisms, including fungi, actinomycetes and bacteria, have been reported to produce keratinases that have biotechnological applications and potential. These keratinases have been usefully applied in agricultural, pharmaceutical, leather and textile processes as well as within environmentally friendly waste management solutions. Potential uses of keratinases include the fields of biomedicine, cosmetics, biological control and the generation of green energy. Herein we aim to provide an overview of the properties of this group of versatile enzymes, including the mechanisms of keratin degradation. The diversity of microbial sources of keratinases is discussed and the optimisation of keratianse production examined.We conclude with an assessment of the established biotechnological applications of keratinases in different industries and current research that highlights other promising potential uses.

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“…Thermoactinomyces candidus which could degrade 11% of sheep wool (Ignatova et al, 1999). It is reported that Bacillus sp.…”

Section: Reduction Of Disulfide Bridges Was Observed Formentioning

confidence: 99%

Biosynthesis and Control of Keratinase in Recalcitrant Feather-Degrading Bacillus megaterium F7-1

Jeong¹,

Lee²,

Jeon³

et al. 2010

Journal of Environmental Science International

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This study was performed to investigate the nutritional conditions controlling keratinase activity in Bacillus megaterium F7-1. B. megaterium F7-1 produced keratinase using chicken feather as a sole source of carbon, nitrogen and sulfur. Addition of the feather medium with glucose enhanced keratinase production (68.9 U/ml), compared to control without glucose (63.2 U/ml). The synthesis of keratinase was repressed by addition of NH4Cl in B. megaterium F7-1. The highest keratinase production (70.9 U/ml) was obtained with the feather medium containing glucose and MgSO4·7H2O. Keratinase was produced in the absence of feather (4.9 U/ml), indicating its constitutive synthesis. Feather degradation resulted in free SH group formation. B. megaterium F7-1 effectively degraded chicken feather meal (86%), whereas duck feather, human nail, human hair and sheep wool displayed relatively low degradation rates (8-34%).

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Isolation and partial characterisation of extracellular keratinase from a wool degrading thermophilic actinomycete strainThermoactinomyces candidus

Cited by 90 publications

References 28 publications

A Bacillus Strain Able to Hydrolyze Alpha- and Beta-Keratin

A Bacillus Strain Able to Hydrolyze Alpha- and Beta-Keratin

Microbial keratinases: characteristics, biotechnological applications and potential.

Biosynthesis and Control of Keratinase in Recalcitrant Feather-Degrading Bacillus megaterium F7-1

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