The Effect of CaCl2 on the Gelling Properties of Pea Protein–Pectin Dispersions

The effects of CaCl<sub>2</sub> addition before (PreCa) or after (PostCa) heating pea protein-pectin dispersions on the formed gel's rheological and microstructural properties were investigated. Isothermal titration calorimetry (ITC) revealed that CaCl<sub>2</sub> bound both pea proteins and pectins through a spontaneous exothermic reaction and pectin exhibited a stronger binding affinity to CaCl<sub>2</sub>. In PreCa gels, low levels of CaCl<sub>2</sub> (5 and 10 mM) increased the gel elasticity (increase in the storage modulus, G') and their microstructural compactness. However, higher CaCl<sub>2</sub> levels (15 and 25 mM) decreased gels' elasticity, likely due to diminished hydrogen bonds formed in the cooling stage, resulting in gels with larger voids and fewer interconnections between the protein and pectin phases. In PostCa gels, their elasticity increased with the CaCl<sub>2</sub> content, a rheological change associated with the formation of denser microstructures. The addition of 25 mM CaCl<sub>2</sub> decreased <i>β</i>-sheet and increased <i>α</i>-helix and random coil structures. Hydrogen bonding and electrostatic and hydrophobic interactions contributed to gel formation and stability in both PreCa and PostCa gels, whereas disulfide bonds had negligible effects. This study highlights the role of CaCl<sub>2</sub> in modulating pea protein-pectin gels' properties and microstructures for the development of gel-like foods with diverse textures and mouthfeels.

Authors

Institutions

Publication Details

Journal
Gels
Published
2024-12-31
DOI
https://doi.org/10.3390/gels11010018
Citations
7
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
2.44

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

The Effect of CaCl2 on the Gelling Properties of Pea Protein–Pectin Dispersions

Da Chen, Osvaldo H. Campanella, Dan Zhang
7 citations
Gels
Proteins in Food Systems
2.44
article

The Effect of CaCl2 on the Gelling Properties of Pea Protein–Pectin Dispersions

Da Chen, Osvaldo H. Campanella, Dan Zhang
article en
7 citations

Abstract

The effects of CaCl<sub>2</sub> addition before (PreCa) or after (PostCa) heating pea protein-pectin dispersions on the formed gel's rheological and microstructural properties were investigated. Isothermal titration calorimetry (ITC) revealed that CaCl<sub>2</sub> bound both pea proteins and pectins through a spontaneous exothermic reaction and pectin exhibited a stronger binding affinity to CaCl<sub>2</sub>. In PreCa gels, low levels of CaCl<sub>2</sub> (5 and 10 mM) increased the gel elasticity (increase in the storage modulus, G') and their microstructural compactness. However, higher CaCl<sub>2</sub> levels (15 and 25 mM) decreased gels' elasticity, likely due to diminished hydrogen bonds formed in the cooling stage, resulting in gels with larger voids and fewer interconnections between the protein and pectin phases. In PostCa gels, their elasticity increased with the CaCl<sub>2</sub> content, a rheological change associated with the formation of denser microstructures. The addition of 25 mM CaCl<sub>2</sub> decreased <i>β</i>-sheet and increased <i>α</i>-helix and random coil structures. Hydrogen bonding and electrostatic and hydrophobic interactions contributed to gel formation and stability in both PreCa and PostCa gels, whereas disulfide bonds had negligible effects. This study highlights the role of CaCl<sub>2</sub> in modulating pea protein-pectin gels' properties and microstructures for the development of gel-like foods with diverse textures and mouthfeels.

GelsVol. 11(1)
Purdue University West Lafayette (US), The Ohio State University (US)
Ohio State University
Openalex Percentile: Top 12%
Proteins in Food Systems
2.44
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.