Sweet protein stability and sensory evaluation in beverage applications

Overview

This research investigates the acid and heat stability of commercially available sweet proteins, specifically Brazzein and Monellin, and their potential application in beverage formulations. Sweet proteins offer a natural alternative to traditional sweeteners, providing high sweetness intensity without the caloric content of sugar. The study aims to address the limited knowledge around how these proteins perform under typical beverage processing and storage conditions, and how they affect sensory perception.

Technical specifications

Sweet proteins under investigation:

• Brazzein: A protein composed of 54 amino acid residues with a molecular weight of 6.5 kDa. Approximately 2,000-fold sweeter than sucrose on a weight basis, with a taste profile similar to sucrose and a short aftertaste.
• Monellin: A small globular protein with a molecular weight of approximately 11 kDa, consisting of two polypeptide chains (A and B) of 45 and 50 amino acid residues, respectively. Approximately 3,000-fold sweeter than sucrose on a weight basis.

Research approach:

• Evaluate acid and heat stability of Brazzein and Monellin under beverage-relevant conditions
• Match the most suitable sweet protein to specific beverage characteristics
• Monitor protein stability in beverage matrices over a selected storage period
• Conduct consumer panel testing to assess sensory acceptability and organoleptic properties
• Explore stabilization strategies in follow-up studies if shelf-life targets are not met

Technology readiness level

This research is at an early investigative stage. Current gaps include limited in-depth studies on the acid and heat stability of Brazzein and Monellin, and no existing application studies of these proteins in beverages. The planned validation includes stability testing, sensory evaluation through consumer panels, and potential follow-up stabilization studies based on initial findings.