Results 131 to 140 of about 1,116 (171)
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Extremophiles, 2020
A new keratinase producer, Bacillus sp. BK111, isolated from a poultry feather was identified as Bacillus zhangzhouensis, which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical assays.
Roghyeh, Moridshahi +3 more
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A new keratinase producer, Bacillus sp. BK111, isolated from a poultry feather was identified as Bacillus zhangzhouensis, which is the first report for its keratinolytic activity. The keratinase production was optimized, followed by the enzyme purification and characterization using biochemical assays.
Roghyeh, Moridshahi +3 more
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Intracellular keratinase ofTrichophyton gallinae
Medical Mycology, 1987Trichophyton gallinae could grow on agar medium containing chicken feathers as sole sources of carbon and nitrogen, but it could not utilize human or guinea pig hair. The fungus grows rapidly when feather keratin solubilized in dimethyl sulphoxide was included in the growth medium.
K, Wawrzkiewicz +2 more
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Microbial keratinases and their prospective applications: an overview
Applied Microbiology and Biotechnology, 2006Microbial keratinases have become biotechnologically important since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide "keratin" recalcitrant to the commonly known proteolytic enzymes trypsin, pepsin and papain.
Rani, Gupta, Priya, Ramnani
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Biochemical features of microbial keratinases and their production and applications
Applied Microbiology and Biotechnology, 2009Keratinases are exciting proteolytic enzymes that display the capability to degrade the insoluble protein keratin. These enzymes are produced by diverse microorganisms belonging to the Eucarya, Bacteria, and Archea domains. Keratinases display a great diversity in their biochemical and biophysical properties.
Adriano, Brandelli +2 more
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Microbial production and industrial applications of keratinases: an overview
International Microbiology, 2018Massive production of keratinaceous byproducts in the form of agricultural and industrial wastes throughout the world necessitates its justified utilization. Chemical treatment of keratin waste is proclaimed as an eco-destructive approach by various researchers since it generates secondary pollutants.
Imania, Ghaffar +6 more
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Biotechnological applications and prospective market of microbial keratinases
Applied Microbiology and Biotechnology, 2013Keratinases are well-recognized enzymes with the unique ability to attack highly cross-linked, recalcitrant structural proteins such as keratin. Their potential in environmental clean-up of huge amount of feather waste has been well established since long.
Rani, Gupta +3 more
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Stability of a new fungal keratinase
1998Keratinases are proteolytic enzymes which catalyze keratin hydrolisis. They have fifferent characteristics, because they could be produced by different microbial sources. Some keratinases are extracellular enzymes showing a high stability. The selcted non-pathogenic fungal strain was cultivated in submerged aerobic conditions.
Hublin, Andrea, Vasić-Rački, Đurđa
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Characterization of the proteolytic enzyme - keratinase
1998Keratinases are proteolytic enzymes that catalyze degradation of keratin. Preparations of the keratinase have different characteristics, because they could be produced by the different sources. They have molecular weights in the range of 16 - 440 kDa. Most of the keratinases have temperature optimum in the range of 25-40 C. The keratinase are stable at
Hublin, Andrea, Gradišar, Helena
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[Screening of collagenase and keratinase producers].
Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993), 2002The study of the capacity of 310 strains of microorganisms from different taxonomic groups (40 bacilli, 43 yeast, 105 streptomycetes, 12 micromycetes) to hydrolyze collagen and keratin allowed to establish that the highest level of collagenase (KA) and keratinase (KerA) activity is inherent in representatives of streptomycetes.
O V, Ivanko +5 more
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