Influence of Proteolysis on the Binding Capacity of Flavor Compounds to Myofibrillar Proteins

Proteolysis occurs extensively during postmortem aging, enzymatic tenderization and fermentation of meat products, whereas less is understood regarding how proteolysis affects meat flavor. Myofibrillar proteins (MP) were extracted from beef longissimus dorsi muscle and subsequently treated with three commercial proteases. The effect of proteolysis on the interactions between the treated MP and butyraldehyde, 2-pentanone, octanal and 2-octanone was investigated. The progress of proteolysis increased the degree of hydrolysis (DH) and the surface hydrophobicity but decreased the turbidity and particle size. Fluorescence-quenching analysis results indicated that the enzymatic treatment generally increased the quenching constant (K-sv) between the treated MP and ketones but decreased the K-sv between the treated MP and aldehydes, and the papain treatment changed the K-sv value to a larger degree than treatment with proteinase K and bromelain. The adsorption assay showed that the proteinase K treatment largely increased the adsorption capacity of the MP to octanal (by 15.8-19.3%), whereas the bromelain treatment significantly reduced the adsorption capacity of the treated MP to butyraldehyde (by 6.0-7.9%) and 2-pentanone (by 9.7-11.9%). A correlation analysis demonstrated a strong positive correlation (0.859, p < 0.05) between the DH of the MP and the adsorption ability of the treated MP to octanal. This study highlighted the significant but complex influence of proteolysis on MP binding capacity to flavor compounds.

Automated summary

Proteolysis has a significant but complex influence on the binding capacity of myofibrillar proteins to flavor compounds.