Molecular and Lumped Products from Hydrothermal Liquefaction of Bovine Serum Albumin

We examined the decomposition of and product formation from a model protein, bovine serum albumin (BSA), under hydrothermal conditions. BSA forms smaller polypeptides as it decomposes, primarily via hydrolytic cleavage of the peptide bonds. It also forms insoluble aggregates in high yields at mild conditions, which subsequently decompose. There were no polypeptides (MW > 5 kDa) remaining after 5 min at 350 °C, but smaller peptides persisted in yields of about 15 wt %. The total yield of free amino acids was typically