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Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch
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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Applied Science Publishers
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5374268/ https://www.ncbi.nlm.nih.gov/pubmed/28325312 http://dx.doi.org/10.1016/j.carbpol.2017.01.040 |
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author | Patel, Hamung Royall, Paul G. Gaisford, Simon Williams, Gareth R. Edwards, Cathrina H. Warren, Frederick J. Flanagan, Bernadine M. Ellis, Peter R. Butterworth, Peter J. |
author_facet | Patel, Hamung Royall, Paul G. Gaisford, Simon Williams, Gareth R. Edwards, Cathrina H. Warren, Frederick J. Flanagan, Bernadine M. Ellis, Peter R. Butterworth, Peter J. |
author_sort | Patel, Hamung |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5374268 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Elsevier Applied Science Publishers |
record_format | MEDLINE/PubMed |
spelling | pubmed-53742682017-05-15 Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch Patel, Hamung Royall, Paul G. Gaisford, Simon Williams, Gareth R. Edwards, Cathrina H. Warren, Frederick J. Flanagan, Bernadine M. Ellis, Peter R. Butterworth, Peter J. Carbohydr Polym Article 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. Elsevier Applied Science Publishers 2017-05-15 /pmc/articles/PMC5374268/ /pubmed/28325312 http://dx.doi.org/10.1016/j.carbpol.2017.01.040 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Patel, Hamung Royall, Paul G. Gaisford, Simon Williams, Gareth R. Edwards, Cathrina H. Warren, Frederick J. Flanagan, Bernadine M. Ellis, Peter R. Butterworth, Peter J. Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch |
title | Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch |
title_full | Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch |
title_fullStr | Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch |
title_full_unstemmed | Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch |
title_short | Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch |
title_sort | structural and enzyme kinetic studies of retrograded starch: inhibition of α-amylase and consequences for intestinal digestion of starch |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5374268/ https://www.ncbi.nlm.nih.gov/pubmed/28325312 http://dx.doi.org/10.1016/j.carbpol.2017.01.040 |
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