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.
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