Effect of constant-current pulsed electric field thawing on proteins and water-holding capacity of frozen porcine longissimus muscle

被引:3
|
作者
Yang, Na [1 ,2 ]
Yao, Huangbing [1 ,3 ]
Zhang, Ankun [1 ]
Jin, Yamei [1 ,2 ]
Zhang, Xiao [1 ]
Xu, Xueming [1 ,2 ]
机构
[1] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Peoples R China
[2] Jiangnan Univ, Collaborat Innovat Ctr Food Safety & Qual Control, Wuxi 214122, Peoples R China
[3] 1800 Lihu Ave, Wuxi 214122, Peoples R China
基金
中国国家自然科学基金;
关键词
Electric field thawing; Pork; Water distribution; Protein oxidation; Microstructure; POSTTHAWING QUALITY; MEAT QUALITY; PHYSICOCHEMICAL PROPERTIES; MYOFIBRILLAR PROTEINS; MOISTURE MIGRATION; PORK; OXIDATION; DORSI; MICROSTRUCTURE; ULTRASOUND;
D O I
10.1016/j.foodchem.2024.139784
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
This study explored the effect of constant -current pulsed electric field thawing (CC -T) on the proteins and waterholding capacity of pork. Fresh meat (FM), and frozen meat after constant -voltage thawing (CV -T), air thawing (AT) and water immersion thawing (WT) were considered as controls. The results indicated that CC -T had a higher thawing rate than conventional thawing during ice -crystal melting stage (-5 to -1 degrees C). It also showed a lower water migration and thawing loss, maintaining pH and shear force closer to FM. Meanwhile, CC -T decreased myoglobin oxidation, resulting in a favorable surface color. The results of protein solubility, differential scanning calorimetry, total sulfhydryl, carbonyl and surface hydrophobicity demonstrated that CC -T reduced myofibrillar protein oxidative denaturation by suppressing the formation of disulfide and carbonyl bonds, thus enhancing solubility and thermal stability. Additionally, microstructural observation found that CC -T maintained a relatively intact muscle fiber structure by reducing muscle damage and myosin filament denaturation.
引用
收藏
页数:12
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