Abstract
Pectin has been used as a gel strengthening agent, but its role in pea protein gels remains unclear. The present study investigated the effects of low-methyl pectin on the physicochemical and rheological properties of pea protein gels at neutral pH and elucidated underlying gelling mechanisms. Pectin increased the stability and viscosity of pea protein dispersions and induced the formation of large protein aggregates. After heating, the storage modulus of pea protein gel containing 0.5 % pectin increased by nearly six times compared to those without pectin, and the gel microstructures became more heterogeneous and compact. Molecular docking revealed that pectin interacted with proteins via mainly electrostatic and hydrogen-bonding interactions. Solvent extraction found that pectin increased the hydrogen bonding, hydrophobic interactions, and disulfide bonds of the gel systems, thus boosting their strength. The current work provided a practical simple approach to increasing the strength of pea protein gels at a neutral pH.
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