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Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions
Starch–gluten interactions are affected by biopolymer type and processing. However, the differentiation mechanisms for gluten–starch interactions during heating have not been illuminated. The effects of glutens from two different wheat flours (a weak-gluten (Yangmai 22, Y22) and a medium-strong glut...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9368910/ https://www.ncbi.nlm.nih.gov/pubmed/35955657 http://dx.doi.org/10.3390/ijms23158523 |
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author | Yang, Tao Wang, Pei Zhou, Qin Zhong, Yingxin Wang, Xiao Cai, Jian Huang, Mei Jiang, Dong |
author_facet | Yang, Tao Wang, Pei Zhou, Qin Zhong, Yingxin Wang, Xiao Cai, Jian Huang, Mei Jiang, Dong |
author_sort | Yang, Tao |
collection | PubMed |
description | Starch–gluten interactions are affected by biopolymer type and processing. However, the differentiation mechanisms for gluten–starch interactions during heating have not been illuminated. The effects of glutens from two different wheat flours (a weak-gluten (Yangmai 22, Y22) and a medium-strong gluten (Yangmai 16, Y16)) on starch’s (S) structural and physicochemical properties during heating and their molecular interactions were investigated in this study. The results showed that gluten hindered the gelatinization and swelling of starch during heating when temperature was below 75 °C, due to competitive hydration and physical barriers of glutens, especially in Y22. Thus, over-heating caused the long-range molecular order and amylopectin branches of starch to be better preserved in the Y22-starch mixture (Y22-S) than in the Y16-starch mixture (Y16-S). Meanwhile, the starch’s degradation pattern during heating in turn influenced the polymerization of both glutens. During heating, residual amylopectin branching points restricted the aggregation and cross-linking of gluten proteins due to steric hindrance. More intense interaction between Y16 and starch during heating mitigated the steric hindrance in starch–gluten networks, which was due to more residual short-range ordered starch and hydrogen bonds involved in the formation of starch–gluten networks in Y16-S during heating. |
format | Online Article Text |
id | pubmed-9368910 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-93689102022-08-12 Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions Yang, Tao Wang, Pei Zhou, Qin Zhong, Yingxin Wang, Xiao Cai, Jian Huang, Mei Jiang, Dong Int J Mol Sci Article Starch–gluten interactions are affected by biopolymer type and processing. However, the differentiation mechanisms for gluten–starch interactions during heating have not been illuminated. The effects of glutens from two different wheat flours (a weak-gluten (Yangmai 22, Y22) and a medium-strong gluten (Yangmai 16, Y16)) on starch’s (S) structural and physicochemical properties during heating and their molecular interactions were investigated in this study. The results showed that gluten hindered the gelatinization and swelling of starch during heating when temperature was below 75 °C, due to competitive hydration and physical barriers of glutens, especially in Y22. Thus, over-heating caused the long-range molecular order and amylopectin branches of starch to be better preserved in the Y22-starch mixture (Y22-S) than in the Y16-starch mixture (Y16-S). Meanwhile, the starch’s degradation pattern during heating in turn influenced the polymerization of both glutens. During heating, residual amylopectin branching points restricted the aggregation and cross-linking of gluten proteins due to steric hindrance. More intense interaction between Y16 and starch during heating mitigated the steric hindrance in starch–gluten networks, which was due to more residual short-range ordered starch and hydrogen bonds involved in the formation of starch–gluten networks in Y16-S during heating. MDPI 2022-07-31 /pmc/articles/PMC9368910/ /pubmed/35955657 http://dx.doi.org/10.3390/ijms23158523 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Yang, Tao Wang, Pei Zhou, Qin Zhong, Yingxin Wang, Xiao Cai, Jian Huang, Mei Jiang, Dong Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions |
title | Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions |
title_full | Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions |
title_fullStr | Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions |
title_full_unstemmed | Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions |
title_short | Effects of Different Gluten Proteins on Starch’s Structural and Physicochemical Properties during Heating and Their Molecular Interactions |
title_sort | effects of different gluten proteins on starch’s structural and physicochemical properties during heating and their molecular interactions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9368910/ https://www.ncbi.nlm.nih.gov/pubmed/35955657 http://dx.doi.org/10.3390/ijms23158523 |
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