Back to Search Start Over

Low-voltage electrostatic field enhances the frozen force of −12 ℃ to suppress oxidative denaturation of the lamb protein during the subsequent frozen storage process after finishing initial freezing.

Authors :
Yang, Chuan
Wu, Guangyu
Liu, Yunhe
Li, Yingbiao
Zhang, Chunhui
Liu, Chengjiang
Li, Xia
Source :
Food Chemistry. Apr2024, Vol. 438, pN.PAG-N.PAG. 1p.
Publication Year :
2024

Abstract

• Low-voltage electrostatic field (LVEF) is directly used to assist frozen lamb meat to storage. • LVEF enhances frozen force at −12 °C achieving the same inhibition of the oxidative denaturation of protein as conventional frozen. • During 90–––150 d, the effect of LVEF assisting frozen storage at −9 °C disappears. The effect of low-voltage electrostatic field (LVEF) assisted −9 °C (LVEF-9) and −12 °C (LVEF-12) frozen, non-LVEF-assisted −9 °C (NLVEF-9) and −12 °C (NLVEF-12) frozen, and conventional frozen (CF-18, −18 °C) storage on the muscle microstructure and the oxidative denaturation of the lamb protein during the subsequent frozen storage process after finishing initial freezing was investigated. Compared with NLVEF-9, LVEF-9, and NLVEF-12, LVEF-12 maintained the better integrity of muscle microstructure, demonstrated by smaller holes, more complete Z-line and M-line, and no significant difference with CF-18 (P > 0.05). Furthermore, LVEF-12 effectively inhibited protein oxidative denaturation as shown by the lower carbonyl content, surface hydrophobicity, and higher total/active sulfhydryl groups and Ca2+-ATPase activity. Moreover, LVEF-12 effectively maintained the integrity of the secondary and tertiary structure of proteins, reduced cross-linking aggregation of proteins, and sustained better functional properties, as shown by higher α -helix content, fluorescence intensity, protein solubility, and lower R-value, disulfide bonds. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
03088146
Volume :
438
Database :
Academic Search Index
Journal :
Food Chemistry
Publication Type :
Academic Journal
Accession number :
174388230
Full Text :
https://doi.org/10.1016/j.foodchem.2023.138055