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

[Display omitted] •MAT retained MPs properties better than AT and MT.•MAT provided a relatively stable tertiary structure, compared to AT and MT.•MAT showed some changes in MPs aggregation and degradation.•MAT had the capacity to hold water and keep its contents constant by LF-NMR.•Structure and moi...

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Bibliographic Details
Published in:Food chemistry 2021-05, Vol.343, p.128412-128412, Article 128412
Main Authors: Peng, Zeyu, Zhu, Mingming, Zhang, Juan, Zhao, Shengming, He, Hongju, Kang, Zhuangli, Ma, Hanjun, Xu, Baocheng
Format: Article
Language:English
Subjects:
Animals
Back Muscles - chemistry
Convection
Food Storage
Hydrophobic and Hydrophilic Interactions
Microwave combined with air convection thawing
Microwaves
Moisture migration
Muscle Proteins - chemistry
Myofibrillar proteins
Pork Meat
Protein properties
Swine
Tertiary structure
Water - chemistry
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Summary:[Display omitted] •MAT retained MPs properties better than AT and MT.•MAT provided a relatively stable tertiary structure, compared to AT and MT.•MAT showed some changes in MPs aggregation and degradation.•MAT had the capacity to hold water and keep its contents constant by LF-NMR.•Structure and moisture migration of MPs from MAT was closer to that from FM. 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 Ca2+-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.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2020.128412