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...
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MDPI AG
2023-03-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/6/1249 |
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| author | Miao Zhang Shuran Zhu Qian Li Dejiang Xue Shuai Jiang Yu Han Chunbao Li |
| author_facet | Miao Zhang Shuran Zhu Qian Li Dejiang Xue Shuai Jiang Yu Han Chunbao Li |
| author_sort | Miao Zhang |
| collection | DOAJ |
| 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 (<i>p</i> < 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. |
| first_indexed | 2024-03-11T06:32:21Z |
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| id | doaj.art-c0e7104ad5d3476386afeb5615b6dc8f |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T06:32:21Z |
| publishDate | 2023-03-01 |
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| series | Foods |
| spelling | doaj.art-c0e7104ad5d3476386afeb5615b6dc8f2023-11-17T11:06:46ZengMDPI AGFoods2304-81582023-03-01126124910.3390/foods12061249Effect of Thermal Processing on the Conformational and Digestive Properties of MyosinMiao Zhang0Shuran Zhu1Qian Li2Dejiang Xue3Shuai Jiang4Yu Han5Chunbao Li6Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, Nanjing 210095, ChinaHeat 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 (<i>p</i> < 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.https://www.mdpi.com/2304-8158/12/6/1249myosinstructuredigestibilitypepsinheating |
| spellingShingle | Miao Zhang Shuran Zhu Qian Li Dejiang Xue Shuai Jiang Yu Han Chunbao Li Effect of Thermal Processing on the Conformational and Digestive Properties of Myosin Foods myosin structure digestibility pepsin heating |
| 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 | myosin structure digestibility pepsin heating |
| url | https://www.mdpi.com/2304-8158/12/6/1249 |
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