Improvement of the newly isolated Bacillus pumilus FH9 keratinolytic activity

El-Refai, Heba A.; Abdel–Naby, Mohamed A.; Gaballa, Ahmed; El-Araby, M.H.; Fattah, Ahmed F. Abdel

doi:10.1016/j.procbio.2004.09.006

Cited by 84 publications

(65 citation statements)

References 22 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%

“…Most keratinases are active in neutral to alkali conditions, from pH 7.0 to pH 9.5. For example, the activity optimum of keratinase from Microbacterium kr10 is pH 7.0 (Thys et al, 2004), B. pumilus FH9 of pH 8.0 (El-Refai et al, 2005), Fervidobacterium islandicum AW-1 of pH 9.0 (Nam et al, 2002), and a (Table 2). Generally, heavy metal ions such as Cu 2+ (Nam et al, 2002;Riffel et al, 2003;Thys et al, 2004), Hg 2+ (Riffel et al, 2003;Thys et al, 2004) and Zn 2+ (Thys et al, 2004) (Nam et al, 2002;Riffel et al, 2003).…”

Section: Molecular Mass Of the Keratinasementioning

confidence: 99%

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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%

Section: Molecular Mass Of the Keratinasementioning

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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“…Bacillus spp. dapat menghasilkan protease alkali yang banyak digunakan sebagai bahan aditif deterjen yang bernilai ekonomis [5] dan keratinase yang sering digunakan dalam penyamakan kulit [6] .…”

Section: Bacillusunclassified

PRODUKSI PROTEASE ALKALI DAN KERATINASE DARI Brevibacillus agri A-03 TERMOFILIK

Agustien¹,

Nurhajati²,

Udin³

et al. 2015

J.Ris.Kim.

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ABSTRAKProtease alkaline and keratinase are a group of protease enzym which have important value in detergen industry and skin tannery. Brevibacillus agri A-03 is thermophilic bacteria isolate that comes from Ambayan Sumatera Barat hot spring and has the ability to produce protease and keratinase. The purpose of this research is to get protease alkaline and thermostable keratinase from Brevibacilus agri-A03. thermostable enzym is produced from enzym production enzym that contains kasein and keratin at various medium pH, inoculum incubation temperature and medium type. Enzym activity is measured by modified Walker methode, protein content is measured by Lowry methode. Protease alkaline is produced at exponential phase, maximum at 18 th hours of incubation and keratinase is produced at stationer phase, maximum at 22 nd hours. Both enzym is produced optimically at medium pH condition 9.0; incubation temperature 55°C, inoculum 5% by using modified Johnvesly and Naik medium with each protease and keratinase specific activity 1.927 and 1.047 U/mg

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“…Têm-se observado que, para muitos microrganismos, a síntese destas enzimas extracelulares pode ser constitutiva ou parcialmente induzida por proteínas ou peptídeos (CHENG et al, 1995, WANG;SHIH, 1999). El-Refai et al (2005) demonstraram que proteases queratinolíticas em Bacillus pumilus são altamente induzidas na presença de queratina e para Chrysosporium keratinophilum a indução é parcial (DOZIE; OKEKE; UNAEZE, 1994), com as proteases queratinolíticas ficando aderidas às células durante expressão constitutiva.…”

Section: Discussionunclassified

“…Existem vários microrganismos queratinolíticos isolados e caracterizados, sendo a maioria deles dermatófitos (TAKIUCHI; HIGUCHI; SEI, 1983, HÄNEL et al, 1991WOLSKI;LOBARZEWSKI, 1991, PAPINI;MANCIANTI, 1996), grampositivos do gênero Bacillus (WILLIAMS et al, 1990;ATALO;GASCHE, 1993;ABDELAZIZ;MOSTAFA, 1998, KIM;, EL-REFAI et al, 2005) …”

Section: Microrganismos Queratinolíticosunclassified

Avaliação de proteases extracelulares de linhagem Chryseobacterium sp. Kr6 e purificação e caracterização de uma metaloprotease queratinolítica

Riffel¹

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Improvement of the newly isolated Bacillus pumilus FH9 keratinolytic activity

Cited by 84 publications

References 22 publications

Purification and characterization of keratinase from a new Bacillus subtilis strain

Purification and characterization of keratinase from a new Bacillus subtilis strain

PRODUKSI PROTEASE ALKALI DAN KERATINASE DARI Brevibacillus agri A-03 TERMOFILIK

Avaliação de proteases extracelulares de linhagem Chryseobacterium sp. Kr6 e purificação e caracterização de uma metaloprotease queratinolítica

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