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Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin
Heat treatment affects the structural properties of meat proteins, which in turn leads to changes in their sensitivity to digestive enzymes, further affecting the nutritional value of meat and meat products. The mechanism of changes in the structure and digestive properties of myosin under different...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10048447/ https://www.ncbi.nlm.nih.gov/pubmed/36981174 http://dx.doi.org/10.3390/foods12061249 |
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author | Zhang, Miao Zhu, Shuran Li, Qian Xue, Dejiang Jiang, Shuai Han, Yu Li, Chunbao |
author_facet | Zhang, Miao Zhu, Shuran Li, Qian Xue, Dejiang Jiang, Shuai Han, Yu Li, Chunbao |
author_sort | Zhang, Miao |
collection | PubMed |
description | Heat treatment affects the structural properties of meat proteins, which in turn leads to changes in their sensitivity to digestive enzymes, further affecting the nutritional value of meat and meat products. The mechanism of changes in the structure and digestive properties of myosin under different heating conditions were studied. An increase in heating temperature led to the exposure of internal groups to a polar environment, but to a decrease in the sturdy α-helix structure of myosin (p < 0.05). The results of tryptophan fluorescence verified that the tertiary structure of the protein seemed to be unfolded at 70 °C. Higher protein denaturation after overheating, as proven by the sulfhydryl contents and turbidity, caused irregular aggregate generation. The excessive heating mode of treatment at 100 °C for 30 min caused myosin to exhibit a lower degree of pepsin digestion, which increased the Michaelis constant (Km value) of pepsin during the digestion, but induced the production of new peptides with longer peptide sequences. This study elucidates the effects of cooking temperature on the conformation of myosin and the change in digestibility of pepsin treatment during heating. |
format | Online Article Text |
id | pubmed-10048447 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-100484472023-03-29 Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin Zhang, Miao Zhu, Shuran Li, Qian Xue, Dejiang Jiang, Shuai Han, Yu Li, Chunbao Foods Article Heat treatment affects the structural properties of meat proteins, which in turn leads to changes in their sensitivity to digestive enzymes, further affecting the nutritional value of meat and meat products. The mechanism of changes in the structure and digestive properties of myosin under different heating conditions were studied. An increase in heating temperature led to the exposure of internal groups to a polar environment, but to a decrease in the sturdy α-helix structure of myosin (p < 0.05). The results of tryptophan fluorescence verified that the tertiary structure of the protein seemed to be unfolded at 70 °C. Higher protein denaturation after overheating, as proven by the sulfhydryl contents and turbidity, caused irregular aggregate generation. The excessive heating mode of treatment at 100 °C for 30 min caused myosin to exhibit a lower degree of pepsin digestion, which increased the Michaelis constant (Km value) of pepsin during the digestion, but induced the production of new peptides with longer peptide sequences. This study elucidates the effects of cooking temperature on the conformation of myosin and the change in digestibility of pepsin treatment during heating. MDPI 2023-03-15 /pmc/articles/PMC10048447/ /pubmed/36981174 http://dx.doi.org/10.3390/foods12061249 Text en © 2023 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 Zhang, Miao Zhu, Shuran Li, Qian Xue, Dejiang Jiang, Shuai Han, Yu Li, Chunbao Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin |
title | Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin |
title_full | Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin |
title_fullStr | Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin |
title_full_unstemmed | Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin |
title_short | Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin |
title_sort | effect of thermal processing on the conformational and digestive properties of myosin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10048447/ https://www.ncbi.nlm.nih.gov/pubmed/36981174 http://dx.doi.org/10.3390/foods12061249 |
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