Intracellular keratinase of<i>Trichophyton gallinae</i>

Wawrzkiewicz, K; L̷obarzewski, J.; Wolski, T.

doi:10.1080/02681218780000601

Cited by 103 publications

(63 citation statements)

References 19 publications

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“…To test the effects of some sulphur-containing chemicals on the keratinase activity, ammonium sulfamate was firstly utilized in the study, and it had positive effects in both low and high concentrations. DMSO is able to solubilize feather keratin (Wawrzkiewicz et al, 1987), and has positive effects on feather meal hydrolysis in this study. Generally, purified keratinases cannot degrade keratin in vitro without the presence of reducing agents (Böckle et al, 1995;Bressollier et al, 1999;Suh and Lee, 2001;Riffel et al, 2003).…”

Section: Substrate Specificity Of the Keratinasementioning

confidence: 88%

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: Substrate Specificity Of the Keratinasementioning

confidence: 88%

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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“…Akyl sulfatase activity was examined on TSA supplemented with 0.2% (wthol) sodium dodecyl sulfate (SDS) (Sigma); the method used was similar to that described by Kitaura et al (22). Hydrolysis of mucin (Sigma) and hydrolysis of keratin were determined as described previously (29,44). The test to determine hydrolysis of elastin (Sigma) was performed on modified Scharman medium (16).…”

Section: Methodsmentioning

confidence: 99%

Aeromonas encheleia sp. nov., Isolated from European Eels

Esteve

Gutiérrez

Ventosa

1995

International Journal of Systematic Bacteriology

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Four strains isolated from European eels in Valencia, Spain, were found to constitute a DNA relatedness group which is 0 to 50% related to the 13 species and DNA group 11 of the genus Aeromonas. Phenotypically, these strains have all of the properties that define the genus Aeromonas. However, they differ from the previously described Aeromonas species by three or more properties. The strains are positive for motility, growth at 37"C, indole production, and arginine dihydrolase activity. They exhibit negative reactions in tests for growth at 42°C and in thiosulfate-citrate-bile salts-sucrose medium (Oxoid), Simmons citrate tests, and tests for lysine and ornithine decarboxylase activities. They produce acid from salicin but not from L-arabinose, D-cellobiose, or lactose. All four strains hydrolyze esculin and arbutin but not elastin. They use L-serine as a sole carbon and energy source but cannot utilize L-arabinose, L-arginine, D-gluconate, or L-glutamine. The strains are resistant to ampicillin. The guanine-plus-cytosine content of the DNA is 59.4 to 60.8 mol%. The name Aeromonas encheleia sp. nov. is proposed for these strains; strain S181 (= CECT 4342) is the type strain. This new species is generally not pathogenic for eels or mice.The genus Aeromonas was proposed by Kluyver and van Niel in 1936 (23) and comprises a collection of oxidase-and catalase-positive, glucose-fermenting, facultatively anaerobic, gram-negative, rod-shaped bacteria that are resistant to vibriostatic agent OD29 (2,4-diamino-6,7-diisopropyl pteridine) and generally are motile by means of polar flagella (32). Bergey's Manual of Systematic Bacteriology includes four species in the genus Aeromonas, Aerornonas salmonicida, Aerornonas hydrophila, Aerornonas caviae, and Aerornonas sobria, some of which are genotypically heterogeneous (32, 34). Recently, the number of recognized species in the genus Aerornonas has increased from 4 to 13; these species represent clearly differentiated DNA homology groups (2, 6, 7, 13, 14, 38-40). Furthermore, methods for identification of Aeromonas strains at the genus and species levels have undergone major improvements primarily as a result of chemotaxonomic studies (3, 4, During a survey to determine what bacteria are associated with European eels reared in a freshwater farm located in Valencia, Spain, four phenotypically related strains were isolated. These strains could not be identified as members of any previously described Aerornonas species. The purposes of this study were to determine, by DNA-DNA hybridization and extensive phenotypic tests, the taxonomic position of the four eel isolates and to assess by inoculation in animal models the pathological significance of these organisms. In this paper we describe a new species, Aeromonas encheleia, which is generally not pathogenic for eels or mice. 20). MATERIALS AND METHODSBacterial strains. The four strains of A. encheleiu used in this study (S176, S177, S181T [T = type strain], and S191) were recovered from healthy European eels reared in a freshwater ...

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“…This technique of soluble keratin preparation was widely used by numerous researchers, however on laboratory scale, for obtaining a substrate for determination of keratinolytic activity [8].…”

Section: Introductionmentioning

confidence: 99%

“…The highly crosslinked network structure with numerous disulfide and hydrogen bonds, as well as hydrophobic interactions, and tightly packed keratin microfibrils causes that the protein is insoluble in water, solutions of weak alkali and acids, and most organic solvents. Soluble keratin can be received by alkaline, acid, or enzymatic hydrolysis, reduction or oxidation of the disulphide bonds, thermal treatment in some organic solvents and various hydrothermal methods [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

Alternative Methods of Preparation of Soluble Keratin from Chicken Feathers

Sinkiewicz

Śliwińska

Staroszczyk

et al. 2016

Waste Biomass Valor

141

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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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Intracellular keratinase ofTrichophyton gallinae

Cited by 103 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

Aeromonas encheleia sp. nov., Isolated from European Eels

Alternative Methods of Preparation of Soluble Keratin from Chicken Feathers

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