Quantifying the effects of pre-roasting on structural and functional properties of yellow pea proteins

Food Res Int. 2023 Oct:172:113180. doi: 10.1016/j.foodres.2023.113180. Epub 2023 Jun 20.

Abstract

Roasting could modify the protein structure/conformation, contributing to changes in functional properties. Here we investigated the effects of pre-roasting on the extraction efficiency, structural and functional properties of pea protein concentrates and isolates (PPC and PPI) produced from yellow split peas. The shorter roasting times (150 °C, 10 and 20 min) had little effect on protein yields and could increase the solubility of PPC or PPI by ∼ 12% at pH 7 and enhance the solubility of PPI by ∼ 12% (10-min roasting) and ∼ 24% (20-min roasting) at pH 3. However, a longer duration of pre-roasting (150 °C, 30 min) significantly reduced the extraction efficiency of PPC and PPI by ∼ 30% and ∼ 61%, respectively. Meanwhile, pre-roasting had minor effects on SDS-PAGE profiles and the secondary structures of pea proteins but significantly altered tertiary structures by reducing free sulfhydryl groups, increasing disulfide bonds and surface hydrophobicity. As for the emulsifying properties, pre-roasting improved the emulsion ability index (EAI) of PPC and PPI but decreased the emulsion stability index (ESI) of PPC and had no significant effect on PPI. Moreover, PPC and PPI with shorter pre-roasting duration (10 and 20 min) had endothermic peaks and showed a slight decrease in the denaturation temperature (Td) and the onset temperature (To), respectively. Overall, the study demonstrated that controlled pre-roasting at 150 °C for 10 min and 20 min altered protein structures (mainly tertiary structures), improving the solubility and EAI of pea proteins at pH 7, while retaining their thermal properties in comparison to unroasted samples.

Keywords: Extraction; Functionality; Pea protein; Protein structure; Roasting; Solubility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electrophoresis, Polyacrylamide Gel
  • Emulsions
  • Lathyrus*
  • Pea Proteins*
  • Protein Conformation

Substances

  • Emulsions
  • Pea Proteins