Evidence map›Paper›PMID 35210697›Full record

ReviewTrends in food science & technology2022

Enzyme kinetic approach for mechanistic insight and predictions of

Peter J Butterworth, Balázs H Bajka, Cathrina H Edwards, Frederick J Warren, Peter R Ellis

Abstract readReview
In one paragraph

Review in Trends in food science & technology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Effects of milling on texture andFood chemistry: X · 2023
    Article
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

5 authors.

Peter J ButterworthBiopolymers Group, Departments of Biochemistry and Nutritional Sciences, Faculty of Life Sciences and Medicine, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK.
Balázs H BajkaBiopolymers Group, Departments of Biochemistry and Nutritional Sciences, Faculty of Life Sciences and Medicine, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK.
Cathrina H EdwardsQuadram Institute Bioscience, Rosalind Franklin Road, Norwich Research Park, Norwich, NR4 7UQ, UK.
Frederick J WarrenQuadram Institute Bioscience, Rosalind Franklin Road, Norwich Research Park, Norwich, NR4 7UQ, UK.
Peter R EllisBiopolymers Group, Departments of Biochemistry and Nutritional Sciences, Faculty of Life Sciences and Medicine, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundStarch is a principal dietary source of digestible carbohydrate and energy. Glycaemic and insulinaemic responses to foods containing starch vary considerably and glucose responses to starchy foods are often described by the glycaemic index (GI) and/or glycaemic load (GL). Low GI/GL foods are beneficial in the management of cardiometabolic disorders (e.g., type 2 diabetes, cardiovascular disease). Differences in rates and extents of digestion of starch-containing foods will affect postprandial glycaemia. SCOPE AND APPROACH: Amylolysis kinetics are influenced by structural properties of the food matrix and of starch itself. Native (raw) semi-crystalline starch is digested slowly but hydrothermal processing (cooking) gelatinises the starch and greatly increases its digestibility. In plants, starch granules are contained within cells and intact cell walls can limit accessibility of water and digestive enzymes hindering gelatinisation and digestibility. KEY FINDINGS AND

conclusionsThis review shows how enzyme kinetic strategies can provide explanations for differences in digestion rate of different starchy foods. Michaelis-Menten and Log of Slope analyses provide kinetic parameters (e.g.,

Indexed as

Alpha-amylaseAMY1, human salivary α-amylase geneAMY2, human pancreatic α-amylase geneBMI, body mass indexCE, catalytic efficiencyCVD, cardiovascular diseaseEnzyme kineticsFto, alpha-oxoglutarate-dependent dioxygenase geneGene copy numberGI, glycaemic indexGIT, gastrointestinal tractGL, glycaemic loadGLUT2, glucose transporter 2HI, hydrolysis indexIC50, inhibitor concentration causing 50% inhibitionLOS, logarithm of slope plotMetabolic significanceRDS, rapidly digestible starchResistant starchRS, resistant starchSCFAs, short chain fatty acidsSDS, slowly digestible starchSGLT1, sodium-dependent glucose co-transporterStarch digestionXRD, X-ray diffraction

Identifiers

PMID35210697
PMCPMC8850932

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Registered trials

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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.