Purification and characterization of an acid trehalase from Acidobacteriumcapsulatum

Citation
K. Inagaki et al., Purification and characterization of an acid trehalase from Acidobacteriumcapsulatum, J BIOSCI BI, 91(2), 2001, pp. 141-146
Citations number
35
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
1389-1723 → ACNP
Volume
91
Issue
2
Year of publication
2001
Pages
141 - 146
Database
ISI
SICI code
1389-1723(200102)91:2<141:PACOAA>2.0.ZU;2-Q
Abstract
We purified an acid trehalase (EC 3.2.1.28, a,alpha,alpha ' -trehalose gluc ohydrolase) from an acidophilic bacterium, Acidobacterium capsulatum. The e nzyme was homogeneous based on polyacrylamide gel electrophoresis, and was composed of a single polypeptide chain with a molecular mass of 57 kDa. Max imum trehalase activity was observed at pH 2.5. The acid trehalase exhibite d an apparent K-m of 1.0 mM for trehalose at 30 degreesC and pH 3.0, The tr ehalase was located in the periplasmic space. The activity of the enzyme wa s 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 e quimolar mixture of alpha -D-glucose and beta -D-glucose was formed on hydr olysis of trehalose by the trehalase.