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. 2020 Apr;57(4):1574-1578.
doi: 10.1007/s13197-020-04253-4. Epub 2020 Feb 20.

Estimating the structure of sarcoplasmic proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field

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Estimating the structure of sarcoplasmic proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field

Guoliang Jia et al. J Food Sci Technol. 2020 Apr.

Abstract

The application of high-voltage electrostatic field (HVEF) is a novel method of thawing. To determine if HVEF thawing could lead to sarcoplasmic proteins denaturation, and to provide a theoretical estimation of the structure of the sarcoplasmic proteins, pork tenderloin was thawed by traditional and HVEF methods. The results from protein solubility analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimeter showed that HVEF thawing did not result in more protein denaturation than those thawed under air or running water. From the principal component analysis of FTIR raw spectra (1700-1600 cm-1, Amide I region), we observed some separations of samples with different thawing treatments. It was found that the proportions of α-helix (1650-1640 cm-1 spectral bands in the original data) could lead to the differences on the PC2 axis of score plots.

Keywords: Denaturation; HVEF; Pork tenderloin; Sarcoplasmic proteins.

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Figures

Fig. 1
Fig. 1
Influence of different thawing methods on the SDS-PAGE patterns of sarcoplasmic proteins extracted from pork
Fig. 2
Fig. 2
DSC thermograms of sarcoplasmic proteins from thawed pork tenderloin. Each data is the average of three replicate samples

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References

    1. Barth A, Zscherp C. What vibrations tell about proteins. Q Rev Biophys. 2002;35(4):369–430. doi: 10.1017/S0033583502003815. - DOI - PubMed
    1. Dalvi-Isfahan M, Hamdami N, Le-Bail A, Xanthakis E. The principles of high voltage electric field and its application in food processing: a review. Food Res Int. 2016;89:48–62. doi: 10.1016/j.foodres.2016.09.002. - DOI - PubMed
    1. DeOliveira DB, Trumble WR, Sarkar HK, Singh BR. Secondary structure estimation of proteins using the amide III region of Fourier transform infrared spectroscopy: application to analyze calcium-binding-induced structural changes in calsequestrin. Appl Spectrosc. 1994;48(11):1432–1441. doi: 10.1366/0003702944028065. - DOI
    1. Grossi A, Olsen K, Bolumar T, Rinnan Å, Øgendal LH, Orlien V. The effect of high pressure on the functional properties of pork myofibrillar proteins. Food Chem. 2016;196:1005–1015. doi: 10.1016/j.foodchem.2015.10.062. - DOI - PubMed
    1. Jackson M, Mantsch HH. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit Rev Biochem Mol Biol. 1995;30(2):95–120. doi: 10.3109/10409239509085140. - DOI - PubMed

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