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微波联合空气对流解冻处理对猪背最长肌肌原纤维蛋白理化性质和结构的影响。

Physicochemical and structural changes in myofibrillar proteins from porcine longissimus dorsi subjected to microwave combined with air convection thawing treatment.

机构信息

School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China.

School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China; Henan Province Engineering Technology Research Center of Animal Products Intensive Processing and Quality Safety Control, Henan Institute of Science and Technology, Xinxiang 453003, China; National Pork Processing Technology Research and Development Professional Center, Xinxiang 453003, China.

出版信息

Food Chem. 2021 May 1;343:128412. doi: 10.1016/j.foodchem.2020.128412. Epub 2020 Oct 16.

DOI:10.1016/j.foodchem.2020.128412
PMID:33268166
Abstract

The effect of microwave combined with air convection thawing (MAT) on the properties and tertiary structure of myofibrillar proteins (MPs) from porcine longissimus dorsi muscle was investigated and compared with single treatments (air thawing, microwave thawing) and fresh meat (FM). Among the thawing treatments, the carbonyl content, dityrosine content, and surface hydrophobicity of MPs in MAT were the lowest, whereas the total sulfhydryl content, water-holding capacity, and Ca-ATPase activity were the highest, suggesting that MAT retained MPs properties better. MAT possessed a more stable tertiary structure and exhibited slight changes in MPs aggregation and degradation. There was an insignificant difference (P > 0.05) in the immobilized water and free water between the MAT samples and FM, indicating a tighter interaction between water and muscle protein in MAT. Thus, MAT could retain the physicochemical and structural properties of MPs, which provided a combination of thawing treatments for application in meat industry.

摘要

研究了微波联合空气对流解冻(MAT)对猪背最长肌肌原纤维蛋白(MPs)性质和三级结构的影响,并与单一处理(空气解冻、微波解冻)和新鲜肉(FM)进行了比较。在解冻处理中,MAT 中 MPs 的羰基含量、二酪氨酸含量和表面疏水性最低,而总巯基含量、持水能力和 Ca-ATP 酶活性最高,表明 MAT 更好地保留了 MPs 的性质。MAT 具有更稳定的三级结构,MPs 的聚集和降解变化较小。MAT 样品和 FM 之间的固定水和自由水没有显著差异(P > 0.05),表明 MAT 中肌肉蛋白与水之间的相互作用更紧密。因此,MAT 可以保持 MPs 的理化和结构特性,为肉类工业提供了一种解冻处理的组合。

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