Angiotensin I-Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Whey Milk, Casein and Egg Albumin by Microbial Enzymes and a Commercial Enzyme

摘要

Hydrolases, particularly proteases, are among the most widely sold enzymes [1]. These enzymes represent approximately 60% of the enzymes sold worldwide [1]. Proteases can be used in different industrial sectors, such as food, detergents, leather, medicines [2], bioremediation [3], and in production of bioactive peptide by enzymatic proteolysis of milk proteins [4]. Bioactive peptides are peptides that have activities similar to drugs or hormones, modulating physiological functions by interacting with specific receptors on target cells inducing answers [5]. Bioactive peptides have emerged on the market in the 70s, when Novartis launched Lypressin?, an analogue of vasopressin. Hypertension affects about one quarter of the world population, it is a major risk factor for cardiovascular disease and related complications [5,6]. The angiotensin I-converting enzyme (ACE) catalyses the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor and has an important role in regulating blood pressure in mammals [6]. Inhibitor peptides of ACE were released from milk casein and whey proteins from goat milk by use of two commercial enzymes subtilisin (Alcalase 2.4 L FG, EC 3.4.21.62) and pancreatic trypsin (PTN 6.0 S Salt free; EC 3.4. 21.4) [7]. The aim of this study was to obtain peptides produced from egg albumin, casein and whey protein, by action of two microbial enzymes and a commercial enzyme, and to evaluate the inhibition of angiotensin I-converting enzyme using fluorescent substrate (Abz-FRK(Dnp)P-OH) in the presence of these hydrolysates.