Reducing Agents Aid in the Texturization of Pea Protein Isolate During High Moisture Extrusion

Area of Science:

• Food Science
• Protein Chemistry
• Material Science

Background:

• Plant protein texturization is crucial for meat analog production.
• Disulfide bond formation is a hypothesized mechanism in protein texturization during extrusion.
• Understanding protein crosslinking is key to optimizing meat analog properties.

Purpose of the Study:

• To investigate the role of disulfide bonds in plant protein texturization.
• To evaluate the impact of reducing agents on pea protein extrusion.
• To determine optimal conditions for high-moisture meat analog production.

Main Methods:

• Pea protein was extruded using a twin-screw extruder at 130°C and 150°C.
• Reducing agents (sodium metabisulfite, cysteine, glutathione) were added at varying concentrations.
• Extrudates were analyzed for protein size, disulfide/thiol bonds, integrity, and anisotropy.

Main Results:

• Reducing agents cleaved disulfide bonds, affecting extrudate structure and texture.
• Glutathione (0.05%) at 150°C produced the best high-moisture meat analog.
• Protein crosslinking was significantly impacted by reducing agents, influencing physical characteristics.

Conclusions:

• Disulfide bond cleavage by reducing agents plays a major role in plant protein texturization.
• Reducing agents significantly alter the physical properties and texture of high-moisture meat analogs.
• Specific reducing agents and extrusion temperatures optimize meat analog characteristics.