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Titolo:
Purification and characterization of an acid trehalase from Acidobacteriumcapsulatum
Autore:
Inagaki, K; Ueno, N; Tamura, T; Tanaka, H;
Indirizzi:
Okayama Univ, Fac Agr, Dept Bioresources Chem, Okayama 7008530, Japan Okayama Univ Okayama Japan 7008530 esources Chem, Okayama 7008530, Japan
Titolo Testata:
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
fascicolo: 2, volume: 91, anno: 2001,
pagine: 141 - 146
SICI:
1389-1723(200102)91:2<141:PACOAA>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; GEN-NOV; ACIDIPHILIUM-ORGANOVORUM; LOBOSPHAERA SP; ISOSCHIZOMER; ENZYME; BACTERIUM; CLONING; FACILIS; MUTANT;
Keywords:
acid trehalase; Acidobacterium capsulatum; glycosidase; enzyme purification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Inagaki, K Okayama Univ, Fac Agr, Dept Bioresources Chem, 2-5-1 Shikata Cho, Okayama 7008530, Japan Okayama Univ 2-5-1 Shikata Cho Okayama Japan 7008530 30, Japan
Citazione:
K. Inagaki et al., "Purification and characterization of an acid trehalase from Acidobacteriumcapsulatum", J BIOSCI BI, 91(2), 2001, pp. 141-146

Abstract

We purified an acid trehalase (EC 3.2.1.28, a,alpha,alpha ' -trehalose glucohydrolase) from an acidophilic bacterium, Acidobacterium capsulatum. The enzyme was homogeneous based on polyacrylamide gel electrophoresis, and wascomposed of a single polypeptide chain with a molecular mass of 57 kDa. Maximum trehalase activity was observed at pH 2.5. The acid trehalase exhibited an apparent K-m of 1.0 mM for trehalose at 30 degreesC and pH 3.0, The trehalase was located in the periplasmic space. The activity of the enzyme was activated by 1.0 mM MnCl2 or CoCl2, and inhibited by 1.0 mM PbCl2, HgCl2, NiCl2, p-chloromercuribenzoate, N-ethylmaleimide, monoiodoacetate, or EDTA. Tile enzyme showed high specificity for trehalose. It was found that an equimolar mixture of alpha -D-glucose and beta -D-glucose was formed on hydrolysis of trehalose by the trehalase.

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Documento generato il 04/04/20 alle ore 02:32:37