Preheat-induced soy protein particles with tunable heat stability

Food Chem. 2021 Jan 30:336:127624. doi: 10.1016/j.foodchem.2020.127624. Epub 2020 Jul 25.

Abstract

Recently, there is a growing interest in developing protein-enriched beverages with improved nutritional and functional properties. However, this is challenged by heat-induced aggregation and gelation of edible proteins, which limits their practical applications in high protein systems. In this study, soy protein particles (SPPs) with tunable heat stability were prepared by simply preheating soy proteins suspensions (pH 6.4 and 1% (w/v) concentration) at different temperatures and times. Results showed that heat-stabled SPPs were successfully obtained at high preheating temperatures with prolonged time. The SPPs structures were found to be highly unfolded, denatured, and compact. In addition, these particles exhibited lower viscosities and higher flow behavior index without gelation, whereas those prepared at lower preheating temperatures were found to readily gel after reheating. These results provide useful insights on how heat stable SPPs can be prepared, which extends their further application in protein-enriched beverages and relevant products.

Keywords: Conformational changes; Heat stability; High protein system; Protein particles; Soy proteins; Structural feature.

MeSH terms

  • Gels / chemistry
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Particle Size
  • Protein Aggregates
  • Protein Denaturation
  • Protein Stability
  • Rheology
  • Soybean Proteins / chemistry*
  • Sulfhydryl Compounds / chemistry
  • Viscosity

Substances

  • Gels
  • Protein Aggregates
  • Soybean Proteins
  • Sulfhydryl Compounds