Covalent Adduct Formation between β-Lactoglobulin and Flavor Compounds under Thermal Treatments That Mimic Food Pasteurization or Sterilization.

Thermal processing (e.g., pasteurization and sterilization) is a critical step ensuring the microbial safety of our foods.

Encapsulation of Orange Oil Using Fluidized Bed Granulation.

The primary objective of this research is to determine how granulation compares to spray drying/agglomeration for producing larger, more dense flavoring particles. Granulation can yield large, dense particles and thereby negate the need for a two-step process (spray drying followed by agglomeration) to achieve improved flow/handling properties of dry flavorings. In this study, a 55% solids slurry (blend of OSAn-modified starch and maltodextrin 15DE) was prepared and then single-fold orange peel oil was added at 20 or 25% of the carrier solids level.

Influence of pH, Temperature, and Water Activity on Covalent Adduct Formation between Selected Flavor Compounds and Model Protein β-Lactoglobulin.

This study investigates the influence of pH, temperature, and water activity on the occurrence of covalent adduct formation between select flavor compounds and a model food protein (β-lactoglobulin). These reactions potentially result in the loss of flavor during processing and storage, reducing consumer acceptability. Foods present a diverse reaction environment encompassing a wide range of , pH, and storage temperature, which potentially influence protein: flavor reaction rates.

Covalent Adduct Formation Between Flavor Compounds of Various Functional Group Classes and the Model Protein β-Lactoglobulin.

The formation of covalent bonds between 47 flavor compounds belonging to 13 different classes of functional groups and β-lactoglobulin (BLG) has been evaluated using electrospray ionization protein mass spectrometry. Covalent bond formation was determined by the appearance of ions in the mass spectra corresponding to BLG + flavor molecule(s). The observed processes for covalent bond formation were Schiff base, Michael addition, and disulfide linkages.

Method To Characterize and Monitor Covalent Interactions of Flavor Compounds with β-Lactoglobulin Using Mass Spectrometry and Proteomics.

This study develops a method to measure the covalent bonds formed between the side chains and terminal amino acids of β-lactoglobulin (BLG) and selected flavor molecules (benzaldehyde, citral, or allyl isothiocyanate) using electrospray ionization mass spectrometry (ESI/MS) and tandem mass spectrometry (MS/MS). This technique made it possible to measure increases in molecular weight of BLG as the reaction takes place (BLG + flavor compound). The observed mass shifts on the reaction corresponded to either Schiff base or Michael addition reactions between the chosen flavor compounds and BLG.