Determination of heat-set gelation capacity of a quinoa protein isolate (Chenopodium quinoa) by dynamic oscillatory rheological analysis

Elaine Kaspchak; Marco Aurelio Schüler de Oliveira; Fernanda Fogagnoli Simas; Célia Regina Cavicchiolo Franco; Joana Léa Meira Silveira; Marcos Rogério Mafra; Luciana Igarashi-Mafra

doi:10.1016/j.foodchem.2017.04.014

Determination of heat-set gelation capacity of a quinoa protein isolate (Chenopodium quinoa) by dynamic oscillatory rheological analysis

Food Chem. 2017 Oct 1:232:263-271. doi: 10.1016/j.foodchem.2017.04.014. Epub 2017 Apr 5.

Authors

Elaine Kaspchak¹, Marco Aurelio Schüler de Oliveira², Fernanda Fogagnoli Simas³, Célia Regina Cavicchiolo Franco³, Joana Léa Meira Silveira⁴, Marcos Rogério Mafra¹, Luciana Igarashi-Mafra⁵

Affiliations

¹ Department of Chemical Engineering, Federal University of Paraná, Rua Francisco H. dos Santos s/n, Zip Code 81531-980 Curitiba, PR, Brazil.
² Department of Biochemistry, State University of Maringá, Av. Colombo 5790, Zip Code 87020-900 Maringá, PR, Brazil.
³ Cell Biology, Federal University of Paraná, Rua Francisco H. dos Santos s/n, Zip Code 81531-980 Curitiba, PR, Brazil.
⁴ Department of Biochemistry and Molecular Biology, Federal University of Paraná, Rua Francisco H. dos Santos s/n, Zip Code 81531-980 Curitiba, PR, Brazil.
⁵ Department of Chemical Engineering, Federal University of Paraná, Rua Francisco H. dos Santos s/n, Zip Code 81531-980 Curitiba, PR, Brazil. Electronic address: luciana.igarashi@ufpr.br.

PMID: 28490074
DOI: 10.1016/j.foodchem.2017.04.014

Abstract

This work aimed to study the influence of pH (3.5 and 7.0) and CaCl₂ and MgCl₂ addition on heat-set gelation of a quinoa protein isolate at 10% and 15% (w/w). The protein isolate obtained was composed mainly of 11S globulin as was observed by electrophoresis and mass spectrometry analysis. Heat-set gelation occurred at both pH values studied. Nevertheless, the gels formed at pH 3.5 were more viscoelastic and denser than those formed at pH 7.0, that was coarser and presented syneresis. The CaCl₂ and MgCl₂ addition increased the gel strength during rheological analysis at pH 3.5, possibly due to the formation of fiber-like connections in the gel network. At pH 7.0, the divalent salts resulted in weaker gels formed by agglomerates, suggesting a neutralization of the protein surface charges. The differences in quinoa protein gelation were attributed to solubility, and the flexibility of proteins secondary structure at the pH studied.

Keywords: 11S globulin; Divalent ions; Heat-set gelation; Microstructure; Rheology.

MeSH terms

Chenopodium quinoa / chemistry*
Gels
Hot Temperature
Hydrogen-Ion Concentration
Plant Proteins / isolation & purification*
Rheology

Substances

Gels
Plant Proteins