Mechanism of "starch blocking" action

The alpha-amylase inhibitors are also called, as "Carbo-blockers" and these compounds are not directly involved in the weight loss process. However, they are indirectly helpful in weight loss due to inhibition of sugar assimilation by inhibiting starch breakdown. With reduced amount of amylase available for break down, the complex carbohydrate has a better chance of traveling through the body without being assimilated, and is eventually excreted from the body instead of being converted into storage fat. An animal model study revealed that amylase inhibitors alter the amount and pattern of food intake and reduce weight gain probably through inducing satiety and increasing carbohydrate delivery to the distal (farthest) part of the small intestine in rats.

Bompard-Gilles,, reported that the alpha-amylase inhibitor from the bean Phaseolus vulgaris is a potent inhibitor of mammalian alpha- amylases and they classified the inhibitor as a "plant defense protein". Nahoum et al observed that the bifunctional alpha-amylase inhibitor (BASI) of Phaseolus vulgaris beans is an endosperm protein, which is relatively abundant, suggesting a role as a storage protein. The BASI protein has a role in the regulation of alpha-amylase activities by binding to the active sites of the enzyme.

 Mechanism of starch blocking action

Koukiekolo investigated the effects of alpha-amylase inhibitor (isolated from Phaseolus vulgaris seeds) on the amylose and maltopentose hydrolysis catalyzed by porcine pancreatic alpha-amylase. Based on a statistical analysis of the data and using the general velocity equation, which is valid at equilibrium for all types of inhibition in a single-substrate reaction, it was concluded that the inhibitory mode is of the mixed non-competitive type. Further they found that the inhibition takes place only when enzyme and inhibitor are preincubated together, before the substrate is added. This shows that the inhibitor and enzyme complex is formed during preincubation period. This model differs from those previously reported for acarbose. The mechanism of action is thus reported to be "mixed non-competitive inhibition"

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