Extracellular proteases of Halobacillus blutaparonensis strain M9, a new moderately halophilic bacterium
Braz. j. microbiol
;
44(4): 1299-1304, Oct.-Dec. 2013. ilus
Article
in English
| LILACS
| ID: lil-705290
ABSTRACT
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.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Serine Proteases
/
Halobacillus
Language:
English
Journal:
Braz. j. microbiol
Journal subject:
Microbiology
Year:
2013
Type:
Article
Affiliation country:
Brazil
Institution/Affiliation country:
Universidade Federal do Rio de Janeiro/BR
Similar
MEDLINE
...
LILACS
LIS