|
|||||
|
|
Egg white proteins and β-cyclodextrin: effective cryoprotectant mixture against oxidative changes in the myofibrillar proteins of Culter alburnus |
|
| Authors: | Noman Walayat Miguel Ángel Rincón Sobia Niaz Asad Nawaz Nadia Niaz Muhammad Zahid Farooq Ishtiaq Ahmad Pengkai Wang Zhongli Zhang |
| Affiliation: | 1. Department of Food Science and Engineering, College of Ocean, Zhejiang University of Technology, Hangzhou, 310014 China;2. Instituto de Nutrición y Tecnología de los Alimentos (INTA), Universidad de Chile, El Líbano, Macul, 5524 Chile
Contribution: Conceptualization (equal);3. College of Food Science and Technology, Huazhong Agriculture University, Wuhan, 430070 China Contribution: Formal analysis (equal);4. Jiangsu Key Laboratory of Crop Genetics and Physiology, College of Agriculture, Yangzhou University, Yangzhou, 225009 China;5. College of Food Science and Technology, Huazhong Agriculture University, Wuhan, 430070 China Contribution: Visualization (equal);6. Department of Animal Sciences, University of Veterinary and Animal Sciences, Lahore, Pakistan Contribution: Validation (equal);7. College of Food Science and Technology, Huazhong Agriculture University, Wuhan, 430070 China;8. College of Food Science and Technology, Huazhong Agriculture University, Wuhan, 430070 China Contribution: ?Investigation (equal), Software (equal);9. College of Food Science and Technology, Huazhong Agriculture University, Wuhan, 430070 China Contribution: Funding acquisition (supporting), Methodology (equal) |
| Abstract: | The effect of egg white protein (EWP) and β-cyclodextrin (β-CD) mixture was analysed on the myofibrillar proteins (MP) of Culter alburnus during a frozen storage at ?18 °C for 60 days. Different proportions of EWP:β-CD mixture (0%, 2%, 4% and 6%) were added into MP to analyse their effect against oxidative changes. During the study, sulphydryl contents and Ca-ATPase activity (0.297 to 0.136 mmol g?1) decreased. Moreover, protein denaturation also prompted the surface hydrophobicity (11.47 to 32.06 μg) and carbonyls (26.36 to 49 mg.28 nmol mg?1) of control MP. A significant decline was observed in emulsifying properties. Besides, EWP:β-CD showed remarkable stability against oxidative changes, by significantly reducing the carbonyls (26.26 to 37.69 nmol mg?1) and surface hydrophobicity (11.51 to 20.31 μg) and also the decline of Ca-ATPase activity (0.29 to 0.19 mmol g?1). It can be concluded that EWP:β-CD (6%) is an efficient approach against oxidative changes in MP from Culter alburnus. |
| Keywords: | Cryoprotectants myofibrillar proteins frozen storage protein oxidation |