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Partially purified white bean amylase inhibitor reduces starch digestion in vitro and
inactivates intraduodenal amylase in humans
Layer, P.; Carlson, G. L.; DiMagno, E. P.
JOURNAL NAME- Gastroenterology
VOL. 88
1985 Jun
PP. 1895-902
DOCUMENT TYPE- Journal Article
JOURNAL CODE- 0374630
JOURNAL SUBSET- MEDJSAIM; MEDJSIM
ISSN- 0016-5085
PUBLICATION COUNTRY- UNITED STATES
LANGUAGE- English NDN- 239-0020-4228-2
Whether commercial, bean-derived alpha-amylase inhibitor preparations failed to decrease
starch digestion in humans because of insufficient antiamylase activity, destruction by
gastrointestinal secretions, or decreased activity in the presence of starch is unknown. We
used a simple partial purification procedure to markedly concentrate the inhibitor (sixfold to
eightfold by total protein content, and 30-40-fold by dry weight). Compared with a
commercial preparation and crude bean extract, this partially purified inhibitor inactivated
intraduodenal, intraileal, and salivary amylase in vitro faster and more completely (p less
than 0.001); its specific activity was not affected by exposure to gastric juice and was only
minimally reduced by duodenal juice. Whereas the rate of amylase inhibition by inhibitor was
markedly slowed in the presence of nondietary liquid starch, dietary solid starch had only a
minimal effect. Consequently, the partially purified inhibitor had no effect on liquid starch
digestion, but decreased in vitro digestion of dietary starch in a dose-dependent manner (p
less than 0.001). Perfusion of the partially purified inhibitor (2.0, 3.5, or 5.0 mg/ml at 5
ml/min) into the duodenum of humans rapidly inhibited greater than 94%, greater than 99%,
or greater than 99.9% of intraluminal amylase activity. We conclude that commercial
amylase inhibitors failed to decrease starch digestion in vivo mainly because they have
insufficient antiamylase activity. However, a partially purified inhibitor with increased specific
activity is stable in human gastrointestinal secretions, slows dietary starch digestion in vitro,
rapidly inactivates amylase in the human intestinal lumen, and, at acceptable oral doses,
may decrease intraluminal digestion of starch in humans. Such an inhibitor therefore
deserves study.