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Egg white proteins and β‐cyclodextrin: effective cryoprotectant mixture against oxidative changes in the myofibrillar proteins of Culter alburnus
Author(s) -
Walayat Noman,
Rincón Miguel Ángel,
Niaz Sobia,
Nawaz Asad,
Niaz Nadia,
Zahid Farooq Muhammad,
Ahmad Ishtiaq,
Wang Pengkai,
Zhang Zhongli
Publication year - 2021
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.15021
Subject(s) - oxidative phosphorylation , denaturation (fissile materials) , chemistry , cryoprotectant , myofibril , egg white , food science , biochemistry , cyclodextrin , biology , nuclear chemistry , cryopreservation , fishery , embryo
Summary 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 .