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Mechanism of heat-induced gelation for ovalbumin under acidic conditions and the effect of peptides

Polymer Journal volume 52, pages 1263–1272 (2020)Cite this article

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Abstract

The mechanism of the heat-induced gelation of ovalbumin (OVA) under acidic conditions and the effect of amphiphilic peptide additives on gelation were investigated using dynamic light scattering (DLS) and small-angle neutron scattering (SANS). This combination of techniques provides structural details spanning a wide range of length scales, from micrometer (DLS) to nanometer (SANS). The molecular morphology and structure probed by SANS suggest that the heat-induced gelation of OVA solution forms a phase-separated structure. The addition of an amphiphilic peptide to the system drastically changed the aggregated structure by promoting the formation of OVA clusters. Furthermore, heating of the solution of OVA and the peptide resulted in effective distribution of the peptide in the matrix of the heat-induced OVA gels and endowed the gel with increased strength. This simplistic approach to increase the gel strength can be applied to any protein/peptide gel system to impart the gel system with specific physical properties required by their intended application.

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Acknowledgements

We would like to acknowledge Professor Naoki Tanaka for his sincere support for this project. This manuscript has been authored by UT–Battelle, LLC under Contract No. DE-AC05-00OR22725 with the U.S. Department of Energy. The United States Government retains and the publisher, by accepting the article for publication, acknowledges that the United States Government retains a nonexclusive, paid-up, irrevocable, worldwide license to publish or reproduce the published form of this manuscript or allow others to do so for United States Government purposes. The Department of Energy will provide public access to these results of federally sponsored research in accordance with the DOE Public Access Plan (http://energy.gov/downloads/doe-public-access-plan).

Funding

This work has been supported by the US-Japan Cooperative Program on Neutron Scattering (IPTS-12590) and Grant-in-Aids for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology (No. 25248027). The SANS experiment performed at the Bio-SANS instrument (HFIR) was transferred from SANS-U at the Research Reactor JRR-3 with the approval of Institute for Solid State Physics (ISSP), The University of Tokyo. The Bio-SANS instrument operated through the Center for Structural Molecular Biology (CSMB), a DOE Office of Science, Office of Biological and Environmental Research resource, uses resources at the High Flux Isotope Reactor, a DOE Office of Science, Scientific User Facility operated by Oak Ridge National Laboratory. Oak Ridge National Laboratory is managed by UT–Battelle, LLC, for the U.S. Department of Energy under Contract DE-AC05-00OR22725.

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Authors and Affiliations

  1. International Center for Young Scientists, National Institute for Materials Science, 1-2-1 Sengen, Tsukuba, Ibaraki, 305-0047, Japan

    Takashi Hiroi

  2. Institute for Solid State Physics, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa, Chiba, 277-8581, Japan

    Kazu Hirosawa, Yuya Okazumi & Mitsuhiro Shibayama

  3. Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA

    Sai Venkatesh Pingali

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  1. Takashi Hiroi
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Correspondence to Takashi Hiroi or Mitsuhiro Shibayama.

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Hiroi, T., Hirosawa, K., Okazumi, Y. et al. Mechanism of heat-induced gelation for ovalbumin under acidic conditions and the effect of peptides. Polym J 52, 1263–1272 (2020). https://doi.org/10.1038/s41428-020-0382-1

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