期刊
BRITISH JOURNAL OF NUTRITION
卷 116, 期 3, 页码 443-450出版社
CAMBRIDGE UNIV PRESS
DOI: 10.1017/S0007114516002221
关键词
Postprandial glucose; Diabetes; alpha-Amylase; alpha-Glucosidase; Polyphenols; Fibre
资金
- Commonwealth Scholarship Commission UK [ZMSC-2012-593]
- National Institute for Scientific and Industrial Research, Zambia
- Nestle
- Florida Department of Citrus
- Nutrilite, USA
- Suntory, UK
Polyphenol- and fibre-rich foods (PFRF) have the potential to affect postprandial glycaemic responses by reducing glucose absorption, and thus decreasing the glycaemic response of foods when consumed together. A randomised, single-blind, cross-over study was conducted on sixteen healthy volunteers to test whether PFRF could attenuate postprandial blood glucose in healthy volunteers when added to a source of carbohydrate (starch in bread). This is the first study to examine the effects of a meal comprised of components to inhibit each stage of the biochemical pathway, leading up to the appearance of glucose in the blood. The volunteers were fasted and attended four visits: two control visits (bread, water, balancing sugars) and two test visits (single and double dose of PFRF) where they consumed bread, water and PFRF. Blood samples were collected at 0 (fasted), 15, 30, 45, 60, 90, 120, 150 and 180 min after consumption. The PFRF components were tested for alpha-amylase and alpha-glucosidase inhibitory potential in vitro. Plasma glucose was lower after consumption of both doses compared with controls: lower dose, change in mean incremental areas under the glucose curves (IAUC)=-27.4 (SD 7.5) %, P< 0.001; higher dose, IAUC =-49.0 (SD 15.3) %, P< 0.001; insulin IAUC was also attenuated by -46.9 (SD 13.4) %, P< 0.01. Consistent with this, the polyphenol components of the PFRF inhibited a-amylase (green tea, strawberry, blackberry and blackcurrant) and alpha-glucosidase (green tea) activities in vitro. The PFRF have a pronounced and significant lowering effect on postprandial blood glucose and insulin response in humans, due in part to inhibition of a-amylase and a-glucosidase, as well as glucose transport.
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