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...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2006-06, Vol.70 (6), p.1395-1401
Hauptverfasser:	Namwong, S.(Chulalongkorn Univ., Bangkok (Thailand)), Hiraga, K, Takada, K, Tsunemi, M, Tanasupawat, S, Oda, K
Format:	Artikel
Sprache:	eng
Schlagworte:	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
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	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