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Provedor de dados:  BJM
País:  Brazil
Título:  Extracellular proteases of Halobacillus blutaparonensis strain M9, a new moderately halophilic bacterium
Autores:  Santos,Anderson F.
Valle,Roberta S.
Pacheco,Clarissa A.
Alvarez,Vanessa M.
Seldin,Lucy
Santos,André L.S.
Data:  2013-12-01
Ano:  2013
Palavras-chave:  Halobacillus blutaparonensis
Halophilic bacterium
Serine protease
Resumo:  Halophilic microorganisms are source of potential hydrolytic enzymes to be used in industrial and/or biotechnological processes. In the present study, we have investigated the ability of the moderately halophilic bacterium Halobacillus blutaparonensis (strain M9), a novel species described by our group, to release proteolytic enzymes. This bacterial strain abundantly proliferated in Luria-Bertani broth supplemented with 2.5% NaCl as well as secreted proteases to the extracellular environment. The production of proteases occurred in bacterial cells grown under different concentration of salt, ranging from 0.5% to 10% NaCl, in a similar way. The proteases secreted by H. blutaparonensis presented the following properties: (i) molecular masses ranging from 30 to 80 kDa, (ii) better hydrolytic activities under neutral-alkaline pH range, (iii) expression modulated according to the culture age, (iv) susceptibility to phenylmethylsulphonyl fluoride, classifying them as serine-type proteases, (v) specific cleavage over the chymotrypsin substrate, and (vi) enzymatic stability in the presence of salt (up to 20% NaCl) and organic solvents (e.g., ether, isooctane and cyclohexane). The proteases described herein are promising for industrial practices due to its haloalkaline properties.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822013000400039
Editor:  Sociedade Brasileira de Microbiologia
Relação:  10.1590/S1517-83822014005000015
Formato:  text/html
Fonte:  Brazilian Journal of Microbiology v.44 n.4 2013
Direitos:  info:eu-repo/semantics/openAccess
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