Analysis of Porcine Bone Extract Soup

Abstract

Compounds at the surface of oil droplets in a porcine bone extract soup were investigated. Adsorbed proteins and phospholipids from the cream phase were analyzed. Amino acid analysis revealed that the proteins contained a higher amount of hydrophobic amino acids than gelatin. Enzymatic hydrolysis of the protein and sequencing analysis revealed that the peptide had sequences such as Val-Phe-Pro and Val-Tyr-Pro. As a result of homology searching with the protein database (Pub-Med, NCBI), Val-Phe-Pro corresponded with proteins in myosin heavy chain or α-actin, and Val-Tyr-Pro corresponded with that in hemoglobin. Phospholipids were detected with molybdenum blue reagent on thin-layer chromatography. It was revealed that the phospholipids consisted of phosphatidilcholine, lyso-phosphatidilcholine and sphingomyelin. A model emulsification experiment was then performed in which a gelatin containing soy lechithin was obtained from an oil-in-water emulsification under boiling conditions.