Showing papers on "Keratinase published in 1991"
TL;DR: Gymnoascoideus petalosporus showed maximum degradation as compared to remaining isolates when grown on human scalp hair as the sole source of nutrients ‘in vitro’.
Abstract: The ability of five keratinophilic fungi, i.e., Chrysosporium indicum, Geotrichum candidum, Gymnoascoideus petalosporus, Scopulariopsis brevicaulis, and Talaromyces trachyspermus, to digest human hair keratin in stationary culture has been studied. Degradation of human scalp hair was studied by determination of cysteine, cystine, inorganic sulfate, thiosulfate, total protein, keratinase and change in alkalinity of culture filtrate. Gymnoascoideus petalosporus showed maximum degradation as compared to remaining isolates when grown on human scalp hair as the sole source of nutrients ‘in vitro’.
39 citations
TL;DR: The bacterium Dermatophilus congolensis is the causative agent of pitted keratolysis, a skin disease and the extracellular proteolytic activity of this bacterium is considered to be responsible for keratinized tissues being the main sites of infection.
Abstract: The bacterium Dermatophilus congolensis is the causative agent of pitted keratolysis, a skin disease. Infection occurs mainly in keratinized tissues and it is necessary for the organism to produce and excrete exoenzymes which are able to degrade keratin. We investigated the amount of keratinase liberated using Keratinazure as substrate and the fungal protease XI as standard. When compared with uninoculated samples, D. congolensis liberated significant amounts of keratinase during a 12-day incubation period with this substrate. An equivalent of 15 units of protease (keratinase) was produced by 10(7) colony-forming units of D. congolensis during a 12-day period at 37 degrees C. We consider the extracellular proteolytic activity of this bacterium to be responsible for keratinized tissues being the main sites of infection.
32 citations
Patent•
01 Oct 1991TL;DR: A substantially pure protein-degrading B. licheniformis PWD-1 enzyme is described in this article, which is characterized by a molecular weight of 33 kiloDaltons, an isoelectric point of 7.25, an optimum pH of pH 7.5, and thermal stability at low temperatures.
Abstract: A substantially pure keratinaceous material-degrading B. licheniformis PWD-1 enzyme is disclosed. The substantially pure enzyme is characterized by a molecular weight of 33 kiloDaltons, an isoelectric point of 7.25, an optimum pH of 7.5, an optimum temperature of 45°-50° C., and thermal stability at low temperatures.
24 citations
TL;DR: The keratin-degrading actinomycete Streptomyces fradiae was cultured in a bioreactor of novel design in which the wool substrate was wound over a supporting frame partially immersed in salts medium and slowly rotated during the course of fermentation.
Abstract: The keratin-degrading actinomycete Streptomyces fradiae was cultured in a bioreactor of novel design in which the wool substrate was wound over a supporting frame partially immersed in salts medium and slowly rotated during the course of fermentation. Both disulphide reductase and keratinase enzyme activities were detected in culture supernatants and the substrate was almost totally solubilized.
18 citations