Purification and characterization of a pig intestinal alpha-limit dextrinase.

F. R. Taravel, R. Datema, W. Woloszczuk, J. J. Marshall, William J. Whelan

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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
Pages (from-to)147-153
Number of pages7
JournalEuropean Journal of Biochemistry
Volume130
Issue number1
StatePublished - Jan 17 1983
Externally publishedYes

Fingerprint

Dextrins
Purification
alpha-Glucosidases
Swine
Starch
Hydrolysis
Oligo-1,6-Glucosidase
Glucosidases
Sucrase
Maltose
Ion Exchange
Enzymes
Durapatite
Chromatography
Small Intestine
Gel Chromatography
Gastrointestinal Tract
Ion exchange
Mucous Membrane
Gels

ASJC Scopus subject areas

  • Biochemistry

Cite this

Taravel, F. R., Datema, R., Woloszczuk, W., Marshall, J. J., & Whelan, W. J. (1983). Purification and characterization of a pig intestinal alpha-limit dextrinase. European Journal of Biochemistry, 130(1), 147-153.

Purification and characterization of a pig intestinal alpha-limit dextrinase. / Taravel, F. R.; Datema, R.; Woloszczuk, W.; Marshall, J. J.; Whelan, William J.

In: European Journal of Biochemistry, Vol. 130, No. 1, 17.01.1983, p. 147-153.

Research output: Contribution to journalArticle

Taravel, FR, Datema, R, Woloszczuk, W, Marshall, JJ & Whelan, WJ 1983, 'Purification and characterization of a pig intestinal alpha-limit dextrinase.', European Journal of Biochemistry, vol. 130, no. 1, pp. 147-153.
Taravel, F. R. ; Datema, R. ; Woloszczuk, W. ; Marshall, J. J. ; Whelan, William J. / Purification and characterization of a pig intestinal alpha-limit dextrinase. In: European Journal of Biochemistry. 1983 ; Vol. 130, No. 1. pp. 147-153.
@article{b3b4fabff043428abbd83ed0bf1210fc,
title = "Purification and characterization of a pig intestinal alpha-limit dextrinase.",
abstract = "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.",
author = "Taravel, {F. R.} and R. Datema and W. Woloszczuk and Marshall, {J. J.} and Whelan, {William J.}",
year = "1983",
month = "1",
day = "17",
language = "English",
volume = "130",
pages = "147--153",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "1",

}

TY - JOUR

T1 - Purification and characterization of a pig intestinal alpha-limit dextrinase.

AU - Taravel, F. R.

AU - Datema, R.

AU - Woloszczuk, W.

AU - Marshall, J. J.

AU - Whelan, William J.

PY - 1983/1/17

Y1 - 1983/1/17

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0021106555&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021106555&partnerID=8YFLogxK

M3 - Article

C2 - 6337842

AN - SCOPUS:0021106555

VL - 130

SP - 147

EP - 153

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 1

ER -