Distinctive Processing Effects on Recovered Protein Isolates from Laurel (Bay) and Olive Leaves: A Comparative Study

Abstract

Although there is a well-known awareness of the nutritional potential of plant proteins, their utilization within food formulations is currently limited due to insufficient investigation of the functional properties or processing conditions. In this study, the protein contents of the remaining pulps of laurel (bay) (LL) and olive leaves (OL) after alcoholic washing (representing phenolic compound extraction), heat treatment (representing the usage of the leaves for tea brewing or as cooking aid), and deoiling process (representing oil extraction) were investigated. Bicinchoninic acid assay (BCA) indicated that the best protein yield was achieved with a direct isolation process after hexane oil removal. Both LL and OL isolates contained around 80% protein, but high temperature and alcohol content broke down the protein structure as well as decreased the final protein content (∼40%). Alcohol treatment appears to remove protein-bound phenols and increase fluorescence intensity in OL protein isolates while potentially causing structural alterations in LL proteins. In addition to a dramatic decrease in fluorescence intensity, the absolute zeta potentials of protein extracts of boiling OL and LL increased by 53 and 24%, respectively. The increased zeta potentials along with the decreased fluorescence intensity indicate the changes in the protein conformation and enhanced hydrophilicity of the protein structure, which can influence the functional properties of proteins. Protein extracts of deoiled LL had the highest ΔH value (180 mJ/mg), which is higher than other laurel and all olive protein samples. Laurel protein isolates became more thermally stable after hexane treatment. Moreover, the protein extracts after hexane treatment showed better emulsion capacity from both laurel (71.57%) and olive (61.87%). Water-binding capacity and thermal stability of the protein extracts from deoiled samples were higher than those of the other pretreatments, but the boiled samples showed higher oil-binding capacity due to protein denaturation. These findings indicate the importance of processing conditions in modulating protein properties for various applications.