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1.
J Agric Food Chem ; 69(29): 8227-8235, 2021 Jul 28.
Artículo en Inglés | MEDLINE | ID: mdl-34251195

RESUMEN

The effect of extracts from four types of tea made from Camelia sinensis (green, white, black, and oolong) on in vitro amylolysis of gelatinized starch and the underlying mechanisms were studied. Of the four extracts, black tea extract (BTE) gave the strongest inhibition of starch digestion and on α-amylase activity. Fluorescence quenching and surface plasmon resonance (SPR) showed compounds in BTE bound to α-amylase more strongly than those in the green, white, and oolong tea extracts. Individual testing of five phenolic compounds abundant in tea extracts showed that theaflavins had a greater inhibitory effect than catechins on α-amylase. SPR showed that theaflavins had much lower equilibrium dissociation constants and therefore bound more tightly to α-amylase than catechins. We conclude that BTE had a stronger inhibitory effect on in vitro enzymatic starch digestion than the other tea extracts, mainly due to the higher content of theaflavins causing stronger inhibition of α-amylase.


Asunto(s)
Camellia sinensis , Catequina , Digestión , Extractos Vegetales , Almidón , , Triticum
2.
Food Chem ; 349: 129170, 2021 Jul 01.
Artículo en Inglés | MEDLINE | ID: mdl-33548887

RESUMEN

In this study, potato, lotus seed and wheat starch samples with different degree of gelatinization (DG) were prepared and their in vitro digestibility at low α-amylase activity evaluated by measuring the release of reducing sugar. The hydrolysis rate (k) and the final equilibrium concentration (C∞) of the three starches increased with increasing DG. Kinetic analyses showed that the Michaelis-Menten constant (Km) and the catalytic efficiency (kcat/Km) increased with increasing DG, indicative of the increasing affinity and catalytic efficiency of α-amylase with all three starch samples. Of the three starches, lotus seed starch showed a much greater increase in k and kcat/Km than potato and wheat starches as the DG of starch increased. From this study, we concluded that at low activity of α-amylase, DG is a major determinant for the binding affinity and catalytic efficiency of α-amylase to starch and in turn the digestion rate of starch.


Asunto(s)
Digestión , Almidón/metabolismo , alfa-Amilasas/metabolismo , Catálisis , Cristalización , Gelatina/metabolismo , Hidrólisis , Técnicas In Vitro , Cinética , Lotus/embriología , Semillas/metabolismo , Solanum tuberosum/química , Especificidad por Sustrato
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