Effect of ultrasound treatment on porcine myofibrillar protein binding furan flavor compounds at different salt concentrations
Copyright © 2024 Elsevier Ltd. All rights reserved..
The effects of ultrasound (500 W) on the interaction of porcine myofibrillar protein (MP) with furan flavor compounds at different salt concentrations (0.6 %, 1.2 % and 2.4 %) were investigated. With the increase of salt concentration, the particle size of MP decreased, and the surface hydrophobicity and active sulfhydryl content increased due to the unfolding and depolymerization of MP. At the same time, ultrasound promoted the exposure of hydrophobic binding sites and hydrogen bonding sites of MP in different salt concentration systems, thus improving the binding ability of MP with furan compounds by 2 % to 22 %, among which MP had the strongest binding capacity of 2-pentylfuran. In conclusion, ultrasound could effectively promote the unfolding of the secondary structure of MP, which was beneficial to the combination of MP and furan flavor compounds under different salt concentrations.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:443 |
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| Enthalten in: |
Food chemistry - 443(2024) vom: 15. Feb., Seite 138427 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Yu, Ying [VerfasserIn] |
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| Links: |
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| Themen: |
451W47IQ8X |
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| Anmerkungen: |
Date Completed 27.02.2024 Date Revised 27.02.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.foodchem.2024.138427 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM367683490 |
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| 520 | |a Copyright © 2024 Elsevier Ltd. All rights reserved. | ||
| 520 | |a The effects of ultrasound (500 W) on the interaction of porcine myofibrillar protein (MP) with furan flavor compounds at different salt concentrations (0.6 %, 1.2 % and 2.4 %) were investigated. With the increase of salt concentration, the particle size of MP decreased, and the surface hydrophobicity and active sulfhydryl content increased due to the unfolding and depolymerization of MP. At the same time, ultrasound promoted the exposure of hydrophobic binding sites and hydrogen bonding sites of MP in different salt concentration systems, thus improving the binding ability of MP with furan compounds by 2 % to 22 %, among which MP had the strongest binding capacity of 2-pentylfuran. In conclusion, ultrasound could effectively promote the unfolding of the secondary structure of MP, which was beneficial to the combination of MP and furan flavor compounds under different salt concentrations | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Furan compounds | |
| 650 | 4 | |a Myofibrillar protein | |
| 650 | 4 | |a Sodium chloride | |
| 650 | 4 | |a Ultrasound | |
| 650 | 7 | |a Sodium Chloride |2 NLM | |
| 650 | 7 | |a 451W47IQ8X |2 NLM | |
| 650 | 7 | |a Sodium Chloride, Dietary |2 NLM | |
| 650 | 7 | |a Muscle Proteins |2 NLM | |
| 700 | 1 | |a Fan, Chaoxia |e verfasserin |4 aut | |
| 700 | 1 | |a Qi, Jun |e verfasserin |4 aut | |
| 700 | 1 | |a Zhao, Xiaocao |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Hui |e verfasserin |4 aut | |
| 700 | 1 | |a Ye, Guoqing |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Mingcheng |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Dengyong |e verfasserin |4 aut | |
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