Molecular characterization of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1

Mitsuiki, Shinji; Ichikawa, Masayasu; Oka, Takuji; Sakai, Masashi; Moriyama, Yasushi; Sameshima, Yuka; Goto, Minoru; Furukawa, Koichi

doi:10.1016/j.enzmictec.2003.12.011

Cited by 87 publications

(66 citation statements)

References 28 publications

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“…(Riffel et al, 2003) and Nocardiopsis sp. TOA-1 (Mitsuiki et al, 2004). The detergent SDS has positive effects on keratinase activity, which is similar to the keratinase from Streptomyces albidoflavus (Bressollier et al, 1999), but differs from the keratinases from Streptomyces pactum DSM 40530 (Böckle et al, 1995), Chryseobacterium sp.…”

Section: Molecular Mass Of the Keratinasementioning

confidence: 84%

“…Most keratinases possess an activity optimum in the range of 30~80 °C, for example, keratinase from B. pseudofirmus AL-89 is of 60~70 °C (Gessesse et al, 2003), Nocardiopsis sp. TOA-1 is of 60 °C (Mitsuiki et al, 2004), and a few have exceptionally high temperature optimum of 100 °C (Nam et al, 2002). Most keratinases are active in neutral to alkali conditions, from pH 7.0 to pH 9.5.…”

Section: Molecular Mass Of the Keratinasementioning

confidence: 99%

“…(Riffel et al, 2003) and Nocardiopsis sp. TOA-1 (Mitsuiki et al, 2004). Proteases are widely used in the detergent industry, and it is important for the keratinase to be used in the presence of detergents such as SDS.…”

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: Molecular Mass Of the Keratinasementioning

confidence: 84%

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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“…Most keratinases possess an activity optimum in the range of 30-80 °C; for example, keratinase from B. Pseudofirmus AL-89 is of 60~70 °C [33], B.licheniformis [34] and Nocardiopsis sp. TOA-1 [35] is of 60°C and a few have an exceptionally high temperature optimum of 100°C [10]. C. echinulata keratinase has an optimum pH of 4.5 and pH 10.0 signifying that the enzyme can be used at both acidic and basic pH.…”

Section: Discussionmentioning

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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“…IS 1, 2, 8 and 18 grown on medium containing whole raw feather, could utilize feather as a unique carbon and nitrogen source. Plate assays were attempted on keratin powder plates by Nocardiopsis sp.TOA-1 where they formed extremely large ones on the plate (Mitsuiki et al, 2002). Milk agar medium was used for the primary screening of actinobacteria (Riffel and Brandelli, 2006).…”

Section: Discussionmentioning

confidence: 99%

Isolation and description of keratinase producing marine actinobacteria from South Indian Coastal Region

Selvam¹,

Vishnupriya²

2013

Afr. J. Biotechnol.

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A unique standard starch casein medium has been implemented for the isolation of actinobacteria from the south Indian marine sediments. A combination of techniques, morphological, physiological and biochemical tests provided the evidence for the isolated actinobacteria. All the 56 isolates were inoculated on milk agar and soya meal agar plates for the primary proteolytic screening and the proportional study was made by ANOVA. Among the 56 isolates, nine showed proteolytic activity in terms of making clear zone around their colony on the plates. Then, nine isolates were subjected to the secondary screening on feather broth where three isolates (IS -1, 2 and 18) showed degradation of feather between seven and ten days. The keratinolytic characters of crude enzymes were scrutinized by feather keratin as substrate and the protein concentration was determined. Then, the isolates were identified at molecular level by 16S rRNA gene amplification technique.

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Molecular characterization of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1

Cited by 87 publications

References 28 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

Isolation and description of keratinase producing marine actinobacteria from South Indian Coastal Region

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