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  • Interactions of starch with a cyanidin-catechin pigment (vignacyanidin) isolated from Vigna angularis bean.

Interactions of starch with a cyanidin-catechin pigment (vignacyanidin) isolated from Vigna angularis bean.

Food chemistry (2013-07-23)
Umeo Takahama, Ryo Yamauchi, Sachiko Hirota
ABSTRACT

A cyanidin-catechin pigment isolated from adzuki bean (vignacyanidin) interacted with starch. The pigment had absorption maxima at 530 and 540 nm at pH 2.0 and 6.8, respectively, and starch (10 and 100 mg ml(-1)) increased the absorbance, shifting the absorption maxima to longer wavelengths. Nitrite oxidised vignacyanidin at pH 2.0, and the oxidation resulted in the production of nitric oxide (NO). Rates of the oxidation and the NO production were enhanced by starch. Vignacyanidin inhibited α-amylase-catalysed digestion of starch at pH 6.8, and amylose digestion was more effectively inhibited than amylopectin digestion. The above results suggest (i) that binding of the pigment to starch increased the accessibility of nitrous acid to the pigment, and (ii) that the binding reduced the digestibility of starch by α-amylase. Possible functions of the pigment in the stomach and the intestine are postulated, taking the above results into account.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
α-Amylase from Bacillus sp., powder, yellow-brown, ~50 U/mg
Sigma-Aldrich
α-Amylase from Bacillus sp., powder, yellow-brown, ~380 U/mg
Sigma-Aldrich
α-Amylase from Bacillus sp., powder, ≥400 units/mg protein (Lowry)
Sigma-Aldrich
α-Amylase from Bacillus sp., Type II-A, lyophilized powder, ≥1,500 units/mg protein (biuret)
Sigma-Aldrich
α-Amylase from human saliva, Type XIII-A, lyophilized powder, 300-1,500 units/mg protein
Sigma-Aldrich
α-Amylase from human saliva, Type IX-A, lyophilized powder, 1,000-3,000 units/mg protein
Sigma-Aldrich
Cyanidin chloride, ≥95% (HPLC)