Conformational changes induced by high-pressure homogenization inhibit myosin filament formation in low ionic strength solutions

Conformational changes induced by high-pressure homogenization inhibit myosin filament formation... Myofibrillar proteins (MPs) of chicken breast are generally insoluble in water. We have developed a new method whereby MPs are solubilized in water by applying high-pressure homogenization (HPH) thus potentially enabling greater utilization of meat in various products. To clarify the mechanism of solubilization of MPs by HPH, we investigated their conformation, solubility and filament forming behavior in low ionic strength solutions induced by 15,000psi HPH (103MPa). HPH induces unfolding of MPs which subsequently exposes sulfhydryl and hydrophobic groups to the surface. Our findings, determined by circular dichroism, ATR-FTIR, SDS-PAGE and LC-ESI-MS/MS analysis suggest that HPH leads to unraveling of helical structures and to formation of myosin oligomers through disulfide bond. Due to intermolecular electrostatic repulsion and physical barrier of disulfide bonds in the rod induced by HPH, we suggest that the altered myosin conformation in MPs inhibits filament formation, thus contributing to high solubility of MPs in water. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Food Research International Elsevier

Conformational changes induced by high-pressure homogenization inhibit myosin filament formation in low ionic strength solutions

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Publisher
Elsevier
Copyright
Copyright © 2016 Elsevier Ltd
ISSN
0963-9969
D.O.I.
10.1016/j.foodres.2016.04.011
Publisher site
See Article on Publisher Site

Abstract

Myofibrillar proteins (MPs) of chicken breast are generally insoluble in water. We have developed a new method whereby MPs are solubilized in water by applying high-pressure homogenization (HPH) thus potentially enabling greater utilization of meat in various products. To clarify the mechanism of solubilization of MPs by HPH, we investigated their conformation, solubility and filament forming behavior in low ionic strength solutions induced by 15,000psi HPH (103MPa). HPH induces unfolding of MPs which subsequently exposes sulfhydryl and hydrophobic groups to the surface. Our findings, determined by circular dichroism, ATR-FTIR, SDS-PAGE and LC-ESI-MS/MS analysis suggest that HPH leads to unraveling of helical structures and to formation of myosin oligomers through disulfide bond. Due to intermolecular electrostatic repulsion and physical barrier of disulfide bonds in the rod induced by HPH, we suggest that the altered myosin conformation in MPs inhibits filament formation, thus contributing to high solubility of MPs in water.

Journal

Food Research InternationalElsevier

Published: Jul 1, 2016

References

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