Preparation and scaling up of a low phenylalanine enzymatic hydrolysate of bovine whey proteins

We describe the preparation of pancreatic enzymes hydrolysate of milk whey proteins containing low levels of aromatic amino acids. Pancreatin and trypsin/chymotrypsin (6.3% w/w protein) when used to hydrolyze whey proteins for 27 h at 37±2 oC, released 74% of the Phe, 100% of the Tyr and 100% of the Trp as free amino acids. Most of the free aromatic amino acids present in 2 kg hydrolysate were separated from the remaining peptides and other amino acids by gel filtration on a 15 liter Sephadex G-25 column eluted with 5% acetic acid at 60 liters h1 at 25oC. The product, recovered in 37% yield, contained 0.70 mmol Phe, 0.41 mmol Tyr, and <0.01 mmol Trp/100 mmol recovered amino acids. The hydrolysate had a general amino acid composition similar to the whey proteins from which it was prepared and could be used as a nitrogen source for patients with phenylketonuria or tyrosinemia after the addition of appropriate aromatic amino acids. *Correspondence: