A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: Purification and characterization

A halophilic bacterium was isolated from fish sauce, classified, and named Halobacillus sp. SR5-3. A purified 43-kDa proteinase produced by this bacterium showed optimal activity at 50 deg C and pH 9-10 in 20% NaCl. The activity of the enzyme was enhanced about 2.5-fold by the addition of 20-35% NaC...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2006-06, Vol.70 (6), p.1395-1401
Main Authors: Namwong, S.(Chulalongkorn Univ., Bangkok (Thailand)), Hiraga, K, Takada, K, Tsunemi, M, Tanasupawat, S, Oda, K
Format: Article
Language:English
Subjects:
AISLAMIENTO
Amino Acid Sequence
Bacillaceae - classification
Bacillaceae - enzymology
BACTERIA
Biological and medical sciences
Enzyme Inhibitors - pharmacology
Enzyme Stability - drug effects
FISH PRODUCTS
Fish Products - microbiology
fish sauce
fluorescence resonance energy transfer substrate (FRETS)
Fundamental and applied biological sciences. Psychology
Halobacillus sp
HALOFITAS
HALOPHYTE
HALOPHYTES
Hydrogen-Ion Concentration
ISOLATION
ISOLEMENT
moderately halophilic bacteria
Molecular Sequence Data
PRODUCTOS DERIVADOS DEL PESCADO
PRODUIT A BASE DE POISSON
PROTEASAS
PROTEASE
PROTEASES
PURIFICACION
PURIFICATION
Serine Endopeptidases - chemistry
Serine Endopeptidases - classification
Serine Endopeptidases - isolation & purification
Serine Endopeptidases - metabolism
serine proteinase
Sodium Chloride - pharmacology
Substrate Specificity
Thailand
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Summary:A halophilic bacterium was isolated from fish sauce, classified, and named Halobacillus sp. SR5-3. A purified 43-kDa proteinase produced by this bacterium showed optimal activity at 50 deg C and pH 9-10 in 20% NaCl. The activity of the enzyme was enhanced about 2.5-fold by the addition of 20-35% NaCl, and the enzyme was highly stabilized by NaCl. It was found to be a serine proteinase related to either chymotrypsin or subtilisin. It absolutely preferred Ile at the Psub(2) position of substrates. Thus, the enzyme was found to be a halophilic serine proteinase with unique substrate specificity.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.50658