Angiotensin I-converting Enzyme Inhibitory Activities of Porcine Skeletal Muscle Proteins Following Enzyme Digestion

Abstract

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, α-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and α-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by α-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

Antioxidative and antihypertensive activities of pig meat before and after cooking and in vitro gastrointestinal digestion: Comparison between Italian autochthonous pig Suino Nero Lucano and a modern crossbred pig

“…Meat is mainly taken after cooking, therefore to evaluate the effective biological activity of meat, the analysis of ACE inhibitory activity of denatured protein and their hydrolysates with digestive enzymes was needed. After in vitro gastrointestinal digestion, ACE inhibitory activity of cooked meat has increased greatly (P < 0.001; Table 3), in agreement with what reported by other authors (Ahhmed & Muguruma, 2010;Katayama et al, 2003). In particular, Ahhmed and Muguruma (2010), found an antihypertensive activity of meat hydrolysate (from pork loin steaks) 27 times greater than in undigested meat from the same muscle.…”

Purification and characterization of an angiotensin I‐converting enzyme inhibitory peptide derived from porcine troponin C

“…An ACE inhibitory assay was performed following the method of Cushman and Cheung (1971), with slight modifications (Katayama et al . 2003).…”

“…2001) reported on ACE inhibitory peptides from myosin, actin, and some water‐soluble proteins. Katayama et al . (2002) suggested that ACE inhibitory peptides were generated from not only these proteins but also from regulatory proteins such as tropomyosin and troponin.…”

Application of hydrolyzed proteins of animal origin in processed meat

“…() and Katayama et al. (). The analysis is based on the enzymatic conversion of hippuryl‐L‐histidyl‐L‐leucine (HHL) to hippuric acid (HA).…”