Produção Nacional
Revisado por pares
Extracellular proteases of Halobacillus blutaparonensis strain M9, a new moderately halophilic bacterium
2013; Springer Nature; Volume: 44; Issue: 4 Linguagem: Inglês
10.1590/s1517-83822014005000015
ISSN1678-4405
AutoresAnderson Fragoso dos Santos, Roberta S. Valle, C.A. Pacheco, Vanessa Marques Alvarez, Lucy Seldin, André Luis Souza dos Santos,
Tópico(s)Protein Hydrolysis and Bioactive Peptides
ResumoHalophilic 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.
Referência(s)