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Gelation dynamics and rheological properties of stirred yogurt alternatives manufactured from pulse protein isolates and their hydrolysates

Year: 2025

Type: article

Abstract: This study investigated the impact of enzymatic proteolysis of pulse proteins on the gelation dynamics, rheological, and tribology properties of plant-based yogurt alternatives (PBYA). Pea (PPI) and lentil (LPI) protein isolates were partially hydrolyzed to ∼1% degree of hydrolysis. Both protein isolates (PPI and LPI) and their respective hydrolysates (PPH and LPH) were used to manufacture PBYA via fermentation. The fermentation-induced gelation took nearly 5 h to reach pH 4.3 as the target pH. The gel hardness of PPH- and LPH-PBYA gels was reduced compared to PPI- and LPI-PBYA. Hydrophobic interactions dominated in stabilizing the PBYA gel structure, irrespective of the hydrolysis treatment. In contrast, partial hydrolysis increased other intermolecular interactions in PPH- and LPH-PBYA, e.g., electrostatic, hydrogen bonding, and disulfide interactions. Despite such an increase, stirred PPH- and LPH-PBYA exhibited reduced gel particle size and increased syneresis rate. These phenomena may be attributed to the production of smaller-sized polypeptides during hydrolysis. Consequently, an increase in the overall population of reactive components for protein-protein interactions may be expected; this resulted in a more compacted structure of protein aggregates or network, but not necessarily strengthening the gel structure, which is mediated by hydrophobic interactions. PBYA made from hydrolysates (PPH or LPH) showed higher frequency dependence regarding rheological properties tested in LAOS regimes. These findings may direct new product development activities for improving PBYA texture with smoother and softer textural attributes. Future research efforts are recommended to explore approaches for improving PBYA gel phase stability. • Partial hydrolysis induced slower fermentation-induced gelation rate. • Hydrolysis reduced the hardness and enhanced the smoothness of the PBYA gels. • Hydrophobic interactions within PBYA were dominant in stabilizing PBYA gel structure. • PPH- and LPH-PBYA exhibited high frequency dependent rheological behavior. • All the PBYA showed similar friction coefficients at the elastohydrodynamic lubrication regime.

Source: Food Hydrocolloids

DOI: 10.1016/j.foodhyd.2025.112018

Authors: Usman Amin, Haotian Zheng

Institution: North Carolina State University

Language: English

Topic: Proteins in Food Systems

Subfield: Food Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

SDG: Zero hunger

Open Access status: hybrid

Estimated APC paid: $4,990