Feather-degrading Bacillus species from poultry waste

Kim, J.M; Lim, Woo Jin; Suh, Hyung Joo

doi:10.1016/s0032-9592(01)00206-0

Cited by 197 publications

(115 citation statements)

References 19 publications

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“…B. subtilis strains had been widely utilized for enzyme production, including the keratinases (Lal et al, 1999;Suh and Lee, 2001;Kim et al, 2001;Macedo et al, 2005). Other Bacillus species including B. licheniformis, B. pumilis, B. cereus, B. halodurans and B. pseudofirmus (Williams et al, 1990;Takami et al, 1999;Rozs et al, 2001;Kim et al, 2001;Gessesse et al, 2003;El-Refai et al, 2005) had also been reported for their keratinolytic activity. Among these strains, B. subtilis KD-N2 degraded feathers more quickly than any other reported until now, except for B. licheniformis RG1, which degraded feathers completely in 24 h (Ramnani and Gupta, 2004).…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of keratinase from a new Bacillus subtilis strain

Cai

Chen

et al. 2008

J. Zhejiang Univ. Sci. B

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Abstract:The aim of this study was to purify and characterize a keratinase produced by a new isolated Bacillus subtilis KD-N2 strain. The keratinase produced by the isolate was purified using ammonium sulphate precipitation, Sephadex G-75 and DEAE (diethylaminoethyl)-Sepharose chromatographic techniques. The purified enzyme was shown to have a molecular mass of 30.5 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The optimum pH at 50 °C was 8.5 and the optimum temperature at pH 8.5 was 55 °C. The keratinase was partially inactivated by some metal ions, organic solvents and serine protease inhibitor phenylmethanesulfonyl fluoride (PMSF). Sodium dodecyl sulfate (SDS) and ethylene diamine tetraacetic acid (EDTA) had positive effect on the keratinase activity. Reducing agents including dithiothreitol (DTT), mercaptoethanol, L-cysteine, sodium sulphite, as well as chemicals of SDS, ammonium sulfamate and dimethylsulfoxide (DMSO) stimulated the enzyme activity upon a feather meal substrate. Besides feather keratin, the enzyme is active upon the soluble proteins ovalbumin, bovine serum albumin (BSA), casein and insoluble ones as sheep wool and human hair. Calf hair, silk and collagen could not be hydrolyzed by the keratinase.

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of keratinase from a new Bacillus subtilis strain

Cai

Chen

et al. 2008

J. Zhejiang Univ. Sci. B

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“…Mycelium was removed by filtration, the filtrate was centrifuged at 10000 x g for 10 min, and the supernatant was used as a crude enzyme preparation [8,15,16].…”

Section: Production Of Keratinasementioning

confidence: 99%

Purification and properties of a novel fungal alkaline keratinase from Cunninghamella echinulata

More¹,

Divyalakshmi²,

Prakash³

et al. 2013

Turk J Bioch

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“…The keratinases capable of keratin degradation are extracellular serine proteases or metallo-proteases. Mesophilic fungi and actinomycetes [11], and also some species of Bacillus [12] produce these enzymes as the response to the presence of keratin. Enzymatic hydrolysis runs under mild conditions during which low energy is used, but it must be assisted by chemical reducing agents degrading keratin's disulphide bonds [13].…”

Section: Introductionmentioning

confidence: 99%

Alternative Methods of Preparation of Soluble Keratin from Chicken Feathers

Sinkiewicz

Śliwińska

Staroszczyk

et al. 2016

Waste Biomass Valor

139

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Huge amount of keratinous waste, especially birds' feathers, demands more value-added application instead of dumping. The present work reports the results of experiments aimed at preparing soluble keratin useful for novel bioproduct formation. The effect of thermo-chemical treatments with various reducing agents, i.e. 2-mercaptoethanol, dithiothreitol, sodium m-bisulphite, and sodium bisulphite, as well as sodium hydroxide, on the yield of keratin extracted from chicken feathers was determined. It was shown that after 2-h reduction with 2-mercaptoethanol and sodium bisulphite, the yield of soluble keratin was about equal and amounted to 84 and 82 %, respectively. The cheaper and harmless sodium bisulphite additionally decreased the extraction time to 1 h with the same yield. Moreover, treatment of the feathers with 2.5 % NaOH further improved the extraction effectiveness by increasing the yield up to 94 %. The results of the study demonstrate the viability of hydrolytic processes to obtain soluble keratin useful for biodegradable film formation for food application, that are harmless and more effective than solubilization by reduction of the disulphide bonds. Graphical Abstract

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Feather-degrading Bacillus species from poultry waste

Cited by 197 publications

References 19 publications

Purification and characterization of keratinase from a new Bacillus subtilis strain

Purification and characterization of keratinase from a new Bacillus subtilis strain

Purification and properties of a novel fungal alkaline keratinase from Cunninghamella echinulata

Alternative Methods of Preparation of Soluble Keratin from Chicken Feathers

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