Inhibition of glucosidases and galactosidases by polyols

Marianne V. Kelemen, W. J. Whelan

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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