Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism
Effects of the incorporation of ultrasound with varied intensities (0–800 W) into the thermal-induced gelation process on the gelling properties of myofibrillar protein (MP) were explored. In comparison with single heating, ultrasound-assisted heating (<600 W) led to significant increases in gel...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2023-03-01
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| Series: | Ultrasonics Sonochemistry |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1350417723000615 |
| _version_ | 1797867697326784512 |
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| author | Qingling Wang Chen Gu Ranran Wei Yi Luan Rui Liu Qingfeng Ge Hai Yu Mangang Wu |
| author_facet | Qingling Wang Chen Gu Ranran Wei Yi Luan Rui Liu Qingfeng Ge Hai Yu Mangang Wu |
| author_sort | Qingling Wang |
| collection | DOAJ |
| description | Effects of the incorporation of ultrasound with varied intensities (0–800 W) into the thermal-induced gelation process on the gelling properties of myofibrillar protein (MP) were explored. In comparison with single heating, ultrasound-assisted heating (<600 W) led to significant increases in gel strength (up to 17.9%) and water holding capacity (up to 32.7%). Moreover, moderate ultrasound treatment was conducive to the fabrication of compact and homogenous gel networks with small pores, which could effectively impair the fluidity of water and allow redundant water to be entrapped within the gel network. Electrophoresis revealed that the incorporation of ultrasound into the gelation process facilitated more proteins to get involved in the development of gel network. With the intensified ultrasound power, α-helix in the gels lowered pronouncedly with a simultaneous increment of β-sheet, β-turn, and random coil. Furthermore, hydrophobic interactions and disulfide bonds were reinforced by the ultrasound treatment, which was in support of the construction of preeminent MP gels. |
| first_indexed | 2024-04-09T23:44:18Z |
| format | Article |
| id | doaj.art-e7e5c3c4b05c4905b7b20a2fed486d71 |
| institution | Directory Open Access Journal |
| issn | 1350-4177 |
| language | English |
| last_indexed | 2024-04-09T23:44:18Z |
| publishDate | 2023-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Ultrasonics Sonochemistry |
| spelling | doaj.art-e7e5c3c4b05c4905b7b20a2fed486d712023-03-18T04:40:39ZengElsevierUltrasonics Sonochemistry1350-41772023-03-0194106349Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanismQingling Wang0Chen Gu1Ranran Wei2Yi Luan3Rui Liu4Qingfeng Ge5Hai Yu6Mangang Wu7College of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaCollege of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaCorresponding author.; College of Food Science and Engineering, Yangzhou University, Yangzhou, Jiangsu 225127, ChinaEffects of the incorporation of ultrasound with varied intensities (0–800 W) into the thermal-induced gelation process on the gelling properties of myofibrillar protein (MP) were explored. In comparison with single heating, ultrasound-assisted heating (<600 W) led to significant increases in gel strength (up to 17.9%) and water holding capacity (up to 32.7%). Moreover, moderate ultrasound treatment was conducive to the fabrication of compact and homogenous gel networks with small pores, which could effectively impair the fluidity of water and allow redundant water to be entrapped within the gel network. Electrophoresis revealed that the incorporation of ultrasound into the gelation process facilitated more proteins to get involved in the development of gel network. With the intensified ultrasound power, α-helix in the gels lowered pronouncedly with a simultaneous increment of β-sheet, β-turn, and random coil. Furthermore, hydrophobic interactions and disulfide bonds were reinforced by the ultrasound treatment, which was in support of the construction of preeminent MP gels.http://www.sciencedirect.com/science/article/pii/S1350417723000615UltrasoundMyofibrillar proteinGelling propertiesWater stateChemical forces |
| spellingShingle | Qingling Wang Chen Gu Ranran Wei Yi Luan Rui Liu Qingfeng Ge Hai Yu Mangang Wu Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism Ultrasonics Sonochemistry Ultrasound Myofibrillar protein Gelling properties Water state Chemical forces |
| title | Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism |
| title_full | Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism |
| title_fullStr | Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism |
| title_full_unstemmed | Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism |
| title_short | Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism |
| title_sort | enhanced gelling properties of myofibrillar protein by ultrasound assisted thermal induced gelation process give an insight into the mechanism |
| topic | Ultrasound Myofibrillar protein Gelling properties Water state Chemical forces |
| url | http://www.sciencedirect.com/science/article/pii/S1350417723000615 |
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