Conformational and Structural Changes in Chickpea Proteins Caused by Simulated Salivary Alterations in the Elderly

Ingrid Contardo*, Fanny Guzmán*, Javier Enrione*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The impact of salivary alterations on chickpea protein structure in the elderly has not been well documented. This study aimed to understand the role of simulated salivary alterations in the conformational properties and secondary structure of the chickpea protein isolate (CPI). Whey protein isolate (WPI) was used as the reference. Protein dispersions (10%) were subjected to in vitro oral processing under simulated salivary conditions in both the elderly and adult subjects. Proteins and their oral counterparts were characterized in terms of their composition, charge, size, solubility, water absorption, molecular weight (MW), and secondary structure (Circular Dichroism and Raman spectroscopy). Under condition of simulated oral digestion in the elderly population, the ordered secondary protein structure was significantly affected, decreasing α-helix by ~36% and ~29% in CPI and WPI compared to the control (adult) population, respectively. An increase in the unordered random coil state was observed. These results could be attributed to an increase in electrolytes in the salivary composition. The structure of CPI is more stable than that of WPI because of its higher MW, more rigid structure, less charged surface, and different amino acid compositions. This study is meaningful in understanding how alterations in the elderly oral system affect protein conformation and is expected to improve the understanding of plant-based protein digestibility.

Original languageEnglish
Article number3668
Pages (from-to)1-14
Number of pages14
JournalFoods
Volume12
Issue number19
DOIs
StatePublished - 5 Oct 2023

Bibliographical note

Publisher Copyright:
© 2023 by the authors.

Keywords

  • chickpea proteins
  • circular dichroism
  • elderly salivary alterations
  • oral electrolytes
  • secondary structure
  • whey proteins

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