Effect of two-stage low-temperature tempering process assisted by electrostatic field application on physicochemical and structural properties of myofibrillar protein in frozen longissimus dorsi of tan mutton

被引：2

作者：

Zhang, Yuanlv ^{[1
]}

Li, Yang ^{[1
]}

Guo, Jiajun ^{[1
]}

Feng, Yuqin ^{[1
]}

Xie, Qiwen ^{[1
]}

Guo, Mei ^{[1
]}

Yin, Junjie ^{[1
]}

Liu, Guishan ^{[1
]}

机构：

[1] Ningxia Univ, Sch Food Sci & Engn, Yinchuan 750021, Ningxia, Peoples R China

来源：

FOOD CHEMISTRY | 2024年 / 456卷

关键词：

Electrostatic field tempering; Two-stage low-temperature tempering; Myofibrillar protein; Protein structure; Tan mutton; MOISTURE MIGRATION; OXIDATION; MICROWAVE; QUALITY;

D O I：

10.1016/j.foodchem.2024.140001

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The effects of refrigerator tempering, two-stage low-temperature tempering (TLT), and a combination of TLT with electrostatic field tempering (TLT-1500/2000/2500/3000) on the physicochemical and structural properties of the myofibrillar protein (MPs) in Longissimus dorsi of Tan mutton were investigated. The results from differential scanning calorimetry and dynamic rheology indicated that TLT-2000/2500 had the least impact on the thermal stability of MPs. While the carbonyl and dityrosine contents of MPs in TLT-2000/2500 were the lowest, the total sulfhydryl content and Ca 2+ -ATPase activity were the highest, suggesting that TLT-2000/2500 preserved the properties of MPs more effectively. The smaller and uniformly distributed particle size, highest zeta potential, and SDS-PAGE analysis confirmed that TLT-2000/2500 had minimal impact on the aggregation and degradation of MPs. Additionally, results from surface hydrophobicity, Fourier transform infrared spectroscopy, intrinsic fluorescence, and UV second-derivative absorption spectra suggested that TLT-2000/2500 was more conducive to stabilizing the primary, secondary, and tertiary structures of MPs.

引用

页数：12