Inhibition of glucosidases and galactosidases by polyols

Marianne V. Kelemen, William J. Whelan

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

The hydrolyses of p-nitrophenyl α- and β-galactosides and p-nitrophenyl α- and β-glucosides by an α-galactosidase from Aspergillus fumigatis, an α-glucosidase from germinated barley, and almond β-glucosidase, which also has β-galactosidase activity, have been examined in the presence of glycerol, erythritol, d-threitol, ribitol, xylitol, d-arabitol and dl-butan-1,2,4-triol. The α-galactosidase was best inhibited by d-threitol, while the α-glucosidase was best inhibited by erythritol. Both inhibitions were competitive. The inhibitory character of these compounds may be attributed to their similarity in structure with the glycon of the substrate between C-3, C-4, C-5, and C-6. The β-glucosidase was best inhibited by erythritol, demonstrating a similarity of action between α- and β-glucosidases. However, the best inhibitor of β-galactosidase was erythritol. This observation confirmed the view that in almond emulsin, the glucosidase and galactosidase activities are found in the same enzyme.

Original languageEnglish
Pages (from-to)423-428
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume117
Issue number2
StatePublished - Nov 1 1966
Externally publishedYes

Fingerprint

Galactosidases
Glucosidases
Erythritol
Ribitol
Xylitol
Galactosides
Aspergillus
Glucosides
Hordeum
Glycerol
polyol
Hydrolysis
Substrates
Enzymes

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Inhibition of glucosidases and galactosidases by polyols. / Kelemen, Marianne V.; Whelan, William J.

In: Archives of Biochemistry and Biophysics, Vol. 117, No. 2, 01.11.1966, p. 423-428.

Research output: Contribution to journalArticle

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