Regulation mechanism of arginine on the structure and gelling properties of myofibrillar protein treated with repeated freezing-thawing
DENG Wenhui1, HAN Xinrui2, CHANG Lu2, LI Zhaorui2, LIU Zimeng2, CAO Yungang2*
1(College of Physical Education, Shaanxi University of Science and Technology, Hanzhong 723000, China) 2(School of Food and Biological Engineering, Shaanxi University of Science and Technology, Xi′an 710021, China)
Abstract: The effects of different concentrations of L-arginine (L-Arg, 0.0, 1.0, 3.0, 5.0 and 10.0 mmol/L) on the physicochemical properties and gelation behavior of repeatedly freeze-thawed myofibrillar protein (MP) were studied in order to provide a theoretical basis for the reasonable regulation of gelling properties of freezing damaged meat proteins. The effects of L-Arg at different concentrations on the secondary and tertiary structures of repeatedly freeze-thawed MP were investigated by circular dichroism spectroscopy and intrinsic tryptophan fluorescence of proteins, respectively. The changes of aggregation of MP with L-Arg treatments were analyzed via the test of particle size and solubility. And the effects of L-Arg treatments on the gelling properties of MP were investigated by rheometer and physical property tester. The results revealed that L-Arg significantly changed the spatial structure of repeated freezing thawing MP, mainly manifested as a significant increase in the content of alpha helix. The addition of L-Arg decreased the particle size of repeatedly freeze-thawed MP, significantly increased the solubility and cooking yield, and obviously reduced the storage modulus (G′), gel strength and gel whiteness. The higher the L-Arg concentration, the greater the impact of L-Arg on the gel performance of repeatedly freeze-thawed MP. Therefore, the treatment with L-Arg alone significantly improved the cooking yield of repeatedly freeze-thawed MP, while remarkably reduced the gel strength.
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DENG Wenhui,HAN Xinrui,CHANG Lu,et al. Regulation mechanism of arginine on the structure and gelling properties of myofibrillar protein treated with repeated freezing-thawing[J]. Food and Fermentation Industries, 2021, 47(16): 72-77.
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