Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidation
This work aimed to investigate the effects of ultrasound assisted enzymatic deamidation by protein-glutaminase (PG) on the dispersion of myofibrillar protein (MP) in low-salt solutions. The solubility, structural characteristics, transmission electron microscopy, asymmetric-flow field-flow fractiona...
Saved in:
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-01-01
|
| Series: | Ultrasonics Sonochemistry |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1350417724004486 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1841546024531787776 |
|---|---|
| author | Yating Liu Zongyun Yang Zhen Li Juan Shen Xia Wang Ru Li Ye Tao Xinglian Xu Peng Wang |
| author_facet | Yating Liu Zongyun Yang Zhen Li Juan Shen Xia Wang Ru Li Ye Tao Xinglian Xu Peng Wang |
| author_sort | Yating Liu |
| collection | DOAJ |
| description | This work aimed to investigate the effects of ultrasound assisted enzymatic deamidation by protein-glutaminase (PG) on the dispersion of myofibrillar protein (MP) in low-salt solutions. The solubility, structural characteristics, transmission electron microscopy, asymmetric-flow field-flow fractionation, steady shear rheological property and multiple light scattering of MP deamidated by PG (MP-PG) and MP pretreated with ultrasound followed by PG deamidation (MP-U-PG) were determined. Molecular docking and molecular dynamics (MD) simulations were used to estimate the interaction between PG and MP. Under ultrasound assistance, the MP deamidated for 16 h (MP-U-PG16) showed the highest solubility (80.1 %) in low-salt conditions, which is attributed to its highest absolute zeta potential and smallest particle size. Although secondary structure analysis showed that MP-PG and MP-U-PG had an increased α-helix ratio and a decreased β-sheet ratio, ultrasonic treatment had a significantly influence on the MD results. The results manifested that hydrogen bond was the primary forces driving the binding between PG and MP, and the hydrogen bond and hydrophobic interaction were the dominant forces responsible the binding between PG and MP pretreated with ultrasound. According to the energy landscapes theory, ultrasound could overcome the energy barriers through external force input and find the best pathway to achieve the final lowest energy state. Our research contributed to the improvement of the colloidal dispersibility of MPs under low-salt conditions and the regulation of protein interaction by ultrasound assistance. |
| format | Article |
| id | doaj-art-efbaaff2e7c64fa09998ccaff06c9a13 |
| institution | Kabale University |
| issn | 1350-4177 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Ultrasonics Sonochemistry |
| spelling | doaj-art-efbaaff2e7c64fa09998ccaff06c9a132025-01-11T06:38:49ZengElsevierUltrasonics Sonochemistry1350-41772025-01-01112107199Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidationYating Liu0Zongyun Yang1Zhen Li2Juan Shen3Xia Wang4Ru Li5Ye Tao6Xinglian Xu7Peng Wang8State key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaState key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaState key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaState key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaState key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaState key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaState key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaState key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCorresponding author.; State key Laboratory of Meat Quality Control and Cultured Meat Development, Key Laboratory of Meat Processing; Jiangsu Innovative Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaThis work aimed to investigate the effects of ultrasound assisted enzymatic deamidation by protein-glutaminase (PG) on the dispersion of myofibrillar protein (MP) in low-salt solutions. The solubility, structural characteristics, transmission electron microscopy, asymmetric-flow field-flow fractionation, steady shear rheological property and multiple light scattering of MP deamidated by PG (MP-PG) and MP pretreated with ultrasound followed by PG deamidation (MP-U-PG) were determined. Molecular docking and molecular dynamics (MD) simulations were used to estimate the interaction between PG and MP. Under ultrasound assistance, the MP deamidated for 16 h (MP-U-PG16) showed the highest solubility (80.1 %) in low-salt conditions, which is attributed to its highest absolute zeta potential and smallest particle size. Although secondary structure analysis showed that MP-PG and MP-U-PG had an increased α-helix ratio and a decreased β-sheet ratio, ultrasonic treatment had a significantly influence on the MD results. The results manifested that hydrogen bond was the primary forces driving the binding between PG and MP, and the hydrogen bond and hydrophobic interaction were the dominant forces responsible the binding between PG and MP pretreated with ultrasound. According to the energy landscapes theory, ultrasound could overcome the energy barriers through external force input and find the best pathway to achieve the final lowest energy state. Our research contributed to the improvement of the colloidal dispersibility of MPs under low-salt conditions and the regulation of protein interaction by ultrasound assistance.http://www.sciencedirect.com/science/article/pii/S1350417724004486UltrasoundMyofibrillar proteinDispersibilityProtein glutaminaseDeamidation |
| spellingShingle | Yating Liu Zongyun Yang Zhen Li Juan Shen Xia Wang Ru Li Ye Tao Xinglian Xu Peng Wang Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidation Ultrasonics Sonochemistry Ultrasound Myofibrillar protein Dispersibility Protein glutaminase Deamidation |
| title | Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidation |
| title_full | Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidation |
| title_fullStr | Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidation |
| title_full_unstemmed | Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidation |
| title_short | Systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low-salt solutions through ultrasound-assisted enzymatic deamidation |
| title_sort | systematic free energy insights into the enhanced dispersibility of myofibrillar protein in low salt solutions through ultrasound assisted enzymatic deamidation |
| topic | Ultrasound Myofibrillar protein Dispersibility Protein glutaminase Deamidation |
| url | http://www.sciencedirect.com/science/article/pii/S1350417724004486 |
| work_keys_str_mv | AT yatingliu systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT zongyunyang systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT zhenli systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT juanshen systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT xiawang systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT ruli systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT yetao systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT xinglianxu systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation AT pengwang systematicfreeenergyinsightsintotheenhanceddispersibilityofmyofibrillarproteininlowsaltsolutionsthroughultrasoundassistedenzymaticdeamidation |