Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

Qingxia Xiong; Ying Ren; Yufei Xia; Guanghui Ma; Reiji Noda; Wei Ge

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Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

Biotechnology and Bioengineering | Updated：2026-01-06

- Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface
- Chinese Journal of Chemical Engineering Vol. 50, Issue 10, Pages: 369-378(2022)
- Affiliations：
  
  1. State Key Laboratory of Multiphase Complex Systems, Institute of Process Engineering, Chinese Academy of Sciences,Beijing,China,100190
  2. Division of Environmental Engineering Science, Graduate School of Science and Technology, Gunma University, 1-5-1 Tenjin-cho, Kiryu,Gunma,Japan,376-8515
  3. School of Chemical Engineering, University of Chinese Academy of Sciences,Beijing,China,100049
  4. Innovation Academy for Green Manufacture, Chinese Academy of Sciences,Beijing,China,100190
  5. State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences,Beijing,China,100190
- Author bio：
- Funds：
- DOI：
  CLC：
- Published：2022
- Accepted：
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Qingxia Xiong, Ying Ren, Yufei Xia, Guanghui Ma, Reiji Noda, Wei Ge. Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface[J]. Chinese Journal of Chemical Engineering, 2022, 50(10): 369-378.
DOI：

Qingxia Xiong, Ying Ren, Yufei Xia, Guanghui Ma, Reiji Noda, Wei Ge. Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface[J]. Chinese Journal of Chemical Engineering, 2022, 50(10): 369-378. DOI：

摘要

Abstract

The adsorption of protein molecules to oil/water (O/W) interface is of critical importance for the product design in a wide range of technologies and industries such as biotechnology

food industry and pharmaceutical industry. In this work

with ovalbumin (OVA) as the model protein

the adsorption conformations at the O/W interface and the adsorption stability have been systematically studied

via

multiple simulation methods

including all-atom molecular dynamic (AAMD) simulations

coarse-grained molecular dynamic (CGMD) simulations and enhanced sampling methods. The computational results of AAMD and CGMD show that the hydrophobic tail of OVA tends to be folded under long time relaxation in aqueous phase

and multiple adsorption conformations can exist at the interface due to heterogeneous interactions raising from oil and water respectively. To further study the adsorption sites of the protein

the adsorption kinetics of OVA at the O/W interface is simulated using metadynamics method combined with CGMD simulations

and the result suggests the existence of multiple adsorption conformations of OVA at interface with the head-on conformation as the most stable one. In all

this work focuses on the adsorptio

n behaviors of OVA at squalene/water interface

and provides a theoretical basis for further functionalization of the proteins in emulsion-based products and engineering.

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