Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar protein
The study investigated the change in protein structure upon thermo-induced gelation of myofibrillar protein (MP, 2%) under different temperatures (30–80°C) at 0.6 M NaCl and pH 6.2. The results showed that heating from 45°C led to changes in physicochemical properties and intermolecular forces invol...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2019-01-01
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| Series: | International Journal of Food Properties |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/10942912.2019.1656231 |
| _version_ | 1818521562294255616 |
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| author | Mangang Wu Yan Cao Shumin Lei Yang Liu Jiahao Wang Juan Hu Zhikun Li Rui Liu Qingfeng Ge Hai Yu |
| author_facet | Mangang Wu Yan Cao Shumin Lei Yang Liu Jiahao Wang Juan Hu Zhikun Li Rui Liu Qingfeng Ge Hai Yu |
| author_sort | Mangang Wu |
| collection | DOAJ |
| description | The study investigated the change in protein structure upon thermo-induced gelation of myofibrillar protein (MP, 2%) under different temperatures (30–80°C) at 0.6 M NaCl and pH 6.2. The results showed that heating from 45°C led to changes in physicochemical properties and intermolecular forces involved during MP gelation, which are related to each other. During the heating process, the free sulfhydryl content slowly increased and reached the highest value at 45°C (10.23 ± 0.13 μmol/g protein). When the temperature exceeded 50°C, Ellman’s titration and SDS-PAGE results indicated that MP gel began to form with the formation of disulfide bonds, which contributed to stabilize the gel structure. Gel strength of the heat-induced MP gel formed at 60°C was significantly higher than that at other temperatures (P < .05), reaching 1.12 ± 0.02 N. Strictly speaking, myofibrillar protein gelatinized after 60°C, and water-holding capacity of the MP gel decreased from 60-80°C, and reached a relatively low value at 80°C. Furthermore, Raman spectra showed that the α-helix content decreased with increasing temperature, β-sheets and random coil contents increased, and the content of the twist-twist-trans conformation increased steadily. |
| first_indexed | 2024-12-11T01:52:43Z |
| format | Article |
| id | doaj.art-c2adf61f83ed4f76a7ca996108d56dae |
| institution | Directory Open Access Journal |
| issn | 1094-2912 1532-2386 |
| language | English |
| last_indexed | 2024-12-11T01:52:43Z |
| publishDate | 2019-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | International Journal of Food Properties |
| spelling | doaj.art-c2adf61f83ed4f76a7ca996108d56dae2022-12-22T01:24:42ZengTaylor & Francis GroupInternational Journal of Food Properties1094-29121532-23862019-01-012211834184710.1080/10942912.2019.16562311656231Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar proteinMangang Wu0Yan Cao1Shumin Lei2Yang Liu3Jiahao Wang4Juan Hu5Zhikun Li6Rui Liu7Qingfeng Ge8Hai Yu9Yangzhou UniversityYangzhou UniversityYangzhou UniversityYangzhou UniversityYangzhou UniversityYangzhou UniversityYangzhou UniversityYangzhou UniversityYangzhou UniversityYangzhou UniversityThe study investigated the change in protein structure upon thermo-induced gelation of myofibrillar protein (MP, 2%) under different temperatures (30–80°C) at 0.6 M NaCl and pH 6.2. The results showed that heating from 45°C led to changes in physicochemical properties and intermolecular forces involved during MP gelation, which are related to each other. During the heating process, the free sulfhydryl content slowly increased and reached the highest value at 45°C (10.23 ± 0.13 μmol/g protein). When the temperature exceeded 50°C, Ellman’s titration and SDS-PAGE results indicated that MP gel began to form with the formation of disulfide bonds, which contributed to stabilize the gel structure. Gel strength of the heat-induced MP gel formed at 60°C was significantly higher than that at other temperatures (P < .05), reaching 1.12 ± 0.02 N. Strictly speaking, myofibrillar protein gelatinized after 60°C, and water-holding capacity of the MP gel decreased from 60-80°C, and reached a relatively low value at 80°C. Furthermore, Raman spectra showed that the α-helix content decreased with increasing temperature, β-sheets and random coil contents increased, and the content of the twist-twist-trans conformation increased steadily.http://dx.doi.org/10.1080/10942912.2019.1656231myofibrillar proteinthermal-induced gelsulfhydryl changesprotein structure |
| spellingShingle | Mangang Wu Yan Cao Shumin Lei Yang Liu Jiahao Wang Juan Hu Zhikun Li Rui Liu Qingfeng Ge Hai Yu Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar protein International Journal of Food Properties myofibrillar protein thermal-induced gel sulfhydryl changes protein structure |
| title | Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar protein |
| title_full | Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar protein |
| title_fullStr | Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar protein |
| title_full_unstemmed | Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar protein |
| title_short | Protein structure and sulfhydryl group changes affected by protein gel properties: process of thermal-induced gel formation of myofibrillar protein |
| title_sort | protein structure and sulfhydryl group changes affected by protein gel properties process of thermal induced gel formation of myofibrillar protein |
| topic | myofibrillar protein thermal-induced gel sulfhydryl changes protein structure |
| url | http://dx.doi.org/10.1080/10942912.2019.1656231 |
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