Structural Integrity of Protein Peptides Under High Pressure
Analyzing Denaturation During the Carbonation Cycle
There is a common technical concern regarding whether the pressure required for carbonation ($30$ to $60$ psi) causes the denaturation of the protein chains in Carbonated Protein Drinks. This document utilizes Circular Dichroism (CD) Spectroscopy to analyze the secondary structure of alpha-lactalbumin and beta-lactoglobulin during the carbonation process.
Research indicates that the mechanical pressure of standard carbonation is insufficient to "unfold" the protein. However, the document highlights that the "shear stress" during high-pressure injection can break down long-chain proteins into smaller peptides. While this does not reduce the nutritional value, it can alter the viscosity of the drink. The document details how "gentle carbonation" techniques—using micro-diffusers—preserve the native structure of the protein while still achieving the desired volumes of CO2.