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| Duarte,T.R.; Oliveira,S.S.; Macrae,A.; Cedrola,S.M.L.; Mazotto,A.M.; Souza,E.P.; Melo,A.C.N.; Vermelho,A.B.. |
| Keratinases are enzymes of great importance involved in pathogenic processes of some fungi. They also have a widespread ecological role since they are responsible for the degradation and recycling of keratin. On the one hand, studying them furthers our knowledge of pathogenicity mechanisms, which has important implications for human health, and on the other hand, understanding their ecological role in keratin recycling has biotechnological potential. Here, a wild-type keratinolytic Candida parapsilosis strain isolated from a poultry farm was treated with ethyl methanesulfonate in order to generate mutants with increased keratinase activity. Mutants were then cultured on media with keratin extracted from chicken feathers as the sole source of nitrogen and... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Candida parapsilosis; Keratinase; Ethyl methanesulfonate; Mutants. |
| Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2011000300006 |
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| Swetlana,Nagal; Jain,P. C.. |
| Feather waste is generated in large amounts as a by-product of commercial poultry processing. This residue is almost pure keratin, which is not easily degradable by common proteolytic enzymes. Eight strains of Bacillus, isolated from decomposing feathers were tested for the hydrolysis of feather wastes in the laboratory. Among these strains, Bacillus cereus KB043 was the best feather degrading organism when grown on basal medium containing 1% hen feather as sole source of carbon and nitrogen. It caused 78.16 ± 0.4 % degradation with a significant release of soluble protein (1206.15 ± 14.7 µg mL-1) and cysteine (20.63 ± 0.4 µg mL-1) in the cultivation fluid. The strain also showed the highest level of keratinase activity (39.10 ± 0.4 U mL-1). These data... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Bacillus; Feather degradation; Poultry waste; Soluble protein; Keratinase. |
| Ano: 2010 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822010000100028 |
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