Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus.

Journal of bacteriology ·Vol. 177 ·No. 2 ·1995-01-00 ·Pages 482-5

Rolfsmeier M, Blum P

Abstract

A soluble maltase (alpha-glucosidase) with an apparent subunit mass of 80 kDa was purified to homogeneity from Sulfolobus solfataricus. The enzyme liberates glucose from maltose and malto-oligomers. Maximal activity was observed at 105 degrees C, with half-lives of 11 h (85 degrees C), 3.0 h (95 degrees C), and 2.75 h (100 degrees C). The enzyme was generally resistant to proteolysis and denaturants including aliphatic alcohols. n-Propanol treatment at 85 degrees C increased both Km and Vmax for maltose hydrolysis.

MeSH Terms

Alcohols Endopeptidases Enzyme Stability Hot Temperature Substrate Specificity Sulfolobus/enzymology alpha-Glucosidases/chemistry,isolation & purification,metabolism

Chemicals

Alcohols alpha-Glucosidases Endopeptidases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Rolfsmeier M

School of Biological Sciences, University of Nebraska, Lincoln 68588-0188.

Blum P

References (12)

12 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.177.2.482-485.1995

Published

1995-01-00

Pages

482-5

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC176616

Subset

External Links

PubMed source DOI: 10.1128/jb.177.2.482-485.1995 PMC Full Text View journal details

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Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus.

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