Purification and Characterization of a Pig Intestinal α‐Limit Dextrinase

Francois R. TARAVEL, Roelf DATEMA, Wolfgang WOLOSZCZUK, J. John MARSHALL, William J. WHELAN

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Mucosa from the duodenal and jejunal regions of pig small intestine was repeatedly freeze-thaw treated to solubilize an enzyme preparation, enriched in maltase, glucoamylase and alpha-limit dextrinase activities; isomaltase and sucrase remained essentially insoluble during the treatment. Chromatographic procedures, including ion-exchange, gel filtration and hydroxylapatite chromatography of the solubilized preparation, brought to homogeneity an alpha-glucosidase active towards maltose, alpha-limit dextrins and starch in decreasing order, with only a very weak capacity to hydrolyse alpha-1,6-linkages. Michaelis constants and maximal velocities, as well as relative rates of hydrolysis of several substrates, including maltodextrins and alpha-limit dextrins, were determined and served to characterize what seems to be a rather specific alpha-1,4-glucosidase. The participation of this enzyme in the hydrolysis of alpha-limit dextrins and more generally in pathways for starch breakdown in the pig digestive tract is examined and discussed.

Original languageEnglish (US)
Pages (from-to)147-153
Number of pages7
JournalEuropean Journal of Biochemistry
Issue number1
StatePublished - Jan 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


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