Evidence map›Paper›PMID 28325312›Full record

ArticleCarbohydrate polymers2017

Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch.

Hamung Patel, Paul G Royall, Simon Gaisford, Gareth R Williams, Cathrina H Edwards, Frederick J Warren, Bernadine M Flanagan, Peter R Ellis, Peter J Butterworth

Open access · hybridAbstract read
In one paragraph

Article in Carbohydrate polymers, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
6.9field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 143 citations in OpenAlex.

  1. Trial
  2. Effect of high-amyloseFood & function · 2022
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  4. Trial
  5. Review
  6. Article
  7. Article
  8. Efficacy of Endophytic BacteriumJournal of microbiology and biotechnology · 2025
    Article
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  11. Article
  12. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Hamung PatelKing's College London, Faculty of Life Sciences and Medicine, Diabetes and Nutritional Sciences Division, Biopolymers Group, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom.
Paul G RoyallKing's College London, Faculty of Life Sciences and Medicine, Institute of Pharmaceutical Science, Drug Delivery Group, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom.
Simon GaisfordUCL School of Pharmacy, University College, 29-39 Brunswick Square, London WC1N 1AX, United Kingdom.
Gareth R WilliamsUCL School of Pharmacy, University College, 29-39 Brunswick Square, London WC1N 1AX, United Kingdom.
Cathrina H EdwardsKing's College London, Faculty of Life Sciences and Medicine, Diabetes and Nutritional Sciences Division, Biopolymers Group, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom; Institute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, United Kingdom.
Frederick J WarrenInstitute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, United Kingdom; Excellence in Plant Cell Walls, Centre for Nutrition and Food Sciences, Queensland Alliance for Agriculture and Food Innovation, University of Queensland, St. Lucia, Brisbane, QLD 4072, Australia.
Bernadine M FlanaganExcellence in Plant Cell Walls, Centre for Nutrition and Food Sciences, Queensland Alliance for Agriculture and Food Innovation, University of Queensland, St. Lucia, Brisbane, QLD 4072, Australia.
Peter R EllisKing's College London, Faculty of Life Sciences and Medicine, Diabetes and Nutritional Sciences Division, Biopolymers Group, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom.
Peter J ButterworthKing's College London, Faculty of Life Sciences and Medicine, Diabetes and Nutritional Sciences Division, Biopolymers Group, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom. Electronic address: peter.butterworth@kcl.ac.uk.
King's College London · GBQuadram Institute · GBUniversity College London · GBARC Centre of Excellence for Plant Success in Nature and Agriculture · AU

Funding

Biotechnology and Biological Sciences Research Council BB/H004866/1
6 · The paper itself

Abstract

Retrograded starch is known to be resistant to digestion. We used enzyme kinetic experiments to examine how retrogradation of starch affects amylolysis catalysed by porcine pancreatic amylase. Parallel studies employing differential scanning calorimetry, infra red spectroscopy, X-ray diffraction and NMR spectroscopy were performed to monitor changes in supramolecular structure of gelatinised starch as it becomes retrograded. The total digestible starch and the catalytic efficiency of amylase were both decreased with increasing evidence of retrogradation. A purified sample of retrograded high amylose starch inhibited amylase directly. These new findings demonstrate that amylase binds to retrograded starch. Therefore consumption of retrograded starch may not only be beneficial to health through depletion of total digestible starch, and therefore the metabolisable energy, but may also slow the rate of intestinal digestion through direct inhibition of α-amylase. Such physiological effects have important implications for the prevention and management of type 2 diabetes and cardiovascular disease.

Indexed as

Digestionalpha-AmylasesAmyloseAnimalsKineticsStarchSwinealpha-AmylasesAmyloseStarchAmylase inhibitionFTIR-ATRMC-DSCStarch retrogradationXRD

Identifiers

PMID28325312
PMCPMC5374268
OpenAlexW2573838612

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.