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

M. Rolfsmeier, P. Blum

Research output: Contribution to journalComment/debate

90 Citations (Scopus)

Abstract

A soluble maltase (α-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°C, with half-lives of 11 h (85°C), 3.0 h (95°C), and 2.75 h (100°C). The enzyme was generally resistant to proteolysis and denaturants including aliphatic alcohols. n-Propanol treatment at 85°C increased both K(m) and V(max) for maltose hydrolysis.

Original languageEnglish (US)
Pages (from-to)482-485
Number of pages4
JournalJournal of bacteriology
Volume177
Issue number2
StatePublished - Jan 1 1995

Fingerprint

Sulfolobus solfataricus
alpha-Glucosidases
Maltose
Glucosidases
1-Propanol
Enzymes
Proteolysis
Hydrolysis
Alcohols
Glucose

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus. / Rolfsmeier, M.; Blum, P.

In: Journal of bacteriology, Vol. 177, No. 2, 01.01.1995, p. 482-485.

Research output: Contribution to journalComment/debate

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