Molecular dynamics study of the effects of static and oscillating electric fields in ovalbumin

WA Muller and JR Sarkis and LDF Marczak and R Muniz, INNOVATIVE FOOD SCIENCE & EMERGING TECHNOLOGIES, 75, 102911 (2022).

DOI: 10.1016/j.ifset.2021.102911

Understand the conformational changes caused by emergent technologies in nutrients is important to assess the total impact of these processes in foodstuff. In this study, molecular dynamics simulations were used to analyze the effects of static and oscillating electric fields in ovalbumin at different temperatures. The results indicate that the protein secondary structure is more thermally stable under electric processing. While molecular size, dipole moment and surface area increased, number of hydrogen bonds decreased under field application. The results agree with experimental observations and were used to discuss the mechanisms of some already reported nonthermal effects of ovalbumin. This paper helps to shed some light on the influence of electric fields in proteins structures and may contribute to the creation of peptides with improved technological properties by alternative processing. Industrial relevance text: Molecular dynamics simulations were used to study the conformational changes caused by continuous and oscillating electric fields in ovalbumin at four temperatures (300, 320, 340 and 360 K), representative of different food processing scenarios. Our results can be used to understand the consequences of electric field treatments in a large peptide and may help to improve functional properties of this protein. The analyzed variables at molecular level can be correlated to experimental observations, helping to explain some of the mechanisms responsible for non-thermal effects in ovalbumin.

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