Protease production, phenylalanine removing and producing bioactive compounds

Protease, an enzyme that hydrolyzes polypeptide and protein chains, is commonly used commercially in detergents, food, pharmaceuticals, and leather industries. Among animal, plant or fungal proteases, bacterial proteases appear to be more suitable for usage in industry because of its activity and cost. For this reason, microorganisms producing proteases for commercial interest have been studied by many researchers. Milk proteins are now a source of various biologically active peptides. These peptides have different biochemical and physiological effects such as inhibition of angiotensin-I converting enzyme (ACE), antimicrobial, antihypertension and antioxidative effect. In this study, after selection of highly active protease producer bacteria in over 200 species, three different bacteria, Virgibacillus panthothenticus, Bacillus megaterium and Burkholderia gladioli, were selected in order to generate different fragments from casein, a milk protein. ACE inhibitory effect and antioxidant activity of fragmented peptides was examined and showed promising activity for usage in medical industry. Phenylketonuria is a hereditary metabolic disorder that causes increased phenylalanine in blood and other body fluids to cause more advanced intelligence disability by destroying the developing brain of the child, since an amino acid called phenylalanine in proteinaceous foods can not be metabolized. In this study pheneylalanine was removed from peptides derived from milk proteins.