Mechanism of heat-induced gelation for ovalbumin and its N-terminus cleaved form

Takashi Hiroi, Yuya Okazumi, Ken C. Littrell, Yuri Narita, Naoki Tanaka, Mitsuhiro Shibayama

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Heat-induced gelation mechanism of ovalbumin (OVA) in neutral, salt-free aqueous solution was investigated by dynamic light scattering and small-angle neutron scattering. The scattering profiles obtained from OVA solutions/gels showed a correlation peak. It is clarified that the position of the peaks was independent of the concentration after heating. From this fact, we described the gelation mechanism as a percolation of aggregates. In addition to this, the gelation mechanism of pOVA was also investigated and compared with that of OVA, where pOVA is a large OVA fragment lacking in N-terminal short peptide region. Although the primary structures of OVA and pOVA are almost the same, the scattering profiles obtained from pOVA were totally different from that of OVA. This difference can be explained by the difference of their dispersion states in the solution, which is originated from small difference of their primary structures.

Original languageEnglish
Pages (from-to)152-158
Number of pages7
JournalPolymer
Volume93
DOIs
StatePublished - Jun 14 2016

Funding

This work was supported by the US-Japan Cooperative Program on Neutron Scattering ( IPTS-10925 ) and a Grant-In-Aid from the Japanese Ministry of Education, Science, Culture and Sports, Japan . This work has been financially supported by Grant-in-Aids for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology (No. 25248027 ).

FundersFunder number
Japanese Ministry of Education, Science, Culture and Sports, Japan
US-JapanIPTS-10925
Japan Society for the Promotion of Science16H02277
Ministry of Education, Culture, Sports, Science and Technology25248027

    Keywords

    • Gelation
    • Protein
    • Small-angle neutron scattering

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