Evaluating the effects of low-frequency alternating magnetic field thawing on oxidation, denaturation, and gelling properties of porcine myofibrillar proteins

Mingming Zhu; He Wang; Jiaxing Zong; Juan Zhang; Shengming Zhao; Hanjun Ma

doi:10.1016/j.foodchem.2023.137337

Evaluating the effects of low-frequency alternating magnetic field thawing on oxidation, denaturation, and gelling properties of porcine myofibrillar proteins

Food Chem. 2024 Feb 1:433:137337. doi: 10.1016/j.foodchem.2023.137337. Epub 2023 Aug 29.

Authors

Mingming Zhu¹, He Wang², Jiaxing Zong², Juan Zhang², Shengming Zhao², Hanjun Ma²

Affiliations

¹ School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China; National Pork Processing Technology Research and Development Professional Center, Xinxiang 453003, China. Electronic address: happyzhumingming@126.com.
² School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China.

PMID: 37688826
DOI: 10.1016/j.foodchem.2023.137337

Abstract

The impact of low-frequency alternating magnetic field thawing (LF-MFT) on the physicochemical and gelling properties of porcine myofibrillar proteins (MP) was studied. Results showed that compared to atmosphere thawing (AT), LF-MFT helped in inhibiting the oxidation and denaturation of protein during thawing, thereby maintaining a superior MP gel (P < 0.05). In particular, LF-MFT-4 (LF-MFT at 4 mT) could decrease the oxidation of MP, which might be due to having a higher content of total sulfhydryl and less carbonyl of MP than other thawing treatments. The denaturation of MP was reduced since LF-MFT-4 led to less aggregation and degradation than AT. The gelling properties were also retained, and a compact and homogeneous network structure was formed after LF-MFT-4, resulting in excellent water retention. These findings suggested that LF-MFT-4 improved the gelling properties of MP by inhibiting its oxidation and denaturation, demonstrating a potential application of LF-MFT in meat thawing.

Keywords: Gelling properties; Low-frequency alternating magnetic field thawing; Microstructure; Myofibrillar proteins; Protein denaturation; Protein oxidation.