Abstract
This study aimed to determine the ageing-time dependent changes of the angiotensin I-converting enzyme (ACE)-inhibition of protein extracts obtained from LAB-inoculated dry-cured pork loins over 360 days of ageing and their hydrolysates obtained after in vitro hydrolysis and absorption. The increasing ageing time was accompanied by a growth in the ACE inhibitory activity of the water-soluble and salt-soluble protein extracts. Based on the hierarchical cluster analysis, 180 days was indicated as the optimal time for ageing of dry-cured pork loins in terms of ACE inhibition. The effect of the strain used on the ACE inhibition varied over long-term aging. The peptides generated during in vitro hydrolysis have between 6 and 22 amino acids in a sequence; the Pro, Ala, Lys, and Glu molecules comprise the largest share. This study demonstrated that pork muscle proteins may lead to production of numerous peptides with ACE inhibitory properties.
Highlights
Hypertension (HT) or high blood pressure (HBP), defined as the long-term elevation of blood pressure (BP) over 140/90 mmHg, is a leading cause of cardiovascular mortality as identified by the World Health Organization (Chockalingam 2008)
One of the groups (C) was not treated further, while the three other groups were each inoculated with L. rhamnosus LOCK900 (LOCK), L. acidophilus Bauer Ł0938 (BAUER), and B. animalis ssp. lactis BB-12 (BB12), respectively; an initial level of 106–107 CFU/g of meat was aimed at
Treatment and ageing time as well as the interactions between factors demonstrated a significant effect on angiotensin I-converting enzyme (ACE) inhibitory activity of WSF and SSF protein fractions of the dry-cured loins before and after each step of simulated gastrointestinal processes of hydrolysis and absorption
Summary
Hypertension (HT) or high blood pressure (HBP), defined as the long-term elevation of blood pressure (BP) over 140/90 mmHg (systolic/diastolic), is a leading cause of cardiovascular mortality as identified by the World Health Organization (Chockalingam 2008). In a healthy human being, the renin–angiotensin–aldosterone system (RAAS) in plasma is primarily responsible for maintaining normal blood pressure. Its stimulation by low blood pressure or nerve impulses (e.g., in stressful situations) causes the kidneys to release the enzyme renin. The release of renin into the bloodstream results in the cleavage of angiotensin I from angiotensinogen (prohormone), which in turn is converted into the angiotensin II (vasoconstrictor) by ACE. ACE is a dipeptidyl carboxypeptidase (EC 3.4.15.1), which catalyzes the conversion of angiotensin I (decapeptide) to angiotensin. II (octapeptide) via the cleavage of the C-terminal dipeptide His-Leu. The other function of ACE is catalyzing bradykinin (a known vasodilator) degradation (Gallego et al 2017; Wu et al 2017)
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