Kinetics of in vitro renin and angiotensin converting enzyme inhibition by chicken skin protein hydrolysates and their blood pressure lowering effects in spontaneously hypertensive rats. (April 2015)

• Record Type: Journal Article
• Authors: Onuh, John O.; Girgih, Abraham T.; Malomo, Sunday A.; Aluko, Rotimi E.; Aliani, Michel
• Is Part Of: Journal of functional foods. Volume 14(2015)
• Page Start: 133
• Page End: 143
• Publication Date: 2015-04
• Subjects: Chicken skin -- Protein hydrolysates -- Renin -- Angiotensin converting enzyme -- Antihypertensive peptides -- Spontaneously hypertensive rats; Functional foods -- Analysis -- Periodicals; Food -- Biotechnology -- Periodicals; Nutrition -- Periodicals; 613.2
• DOI: 10.1016/j.jff.2015.01.031
• Languages: English
• ISSNs: 1756-4646

Abstract

Highlights: Short-chain chicken skin peptides had better ACE inhibition than long-chain peptides. Kinetics of ACE and renin inhibition showed mainly mixed-type mechanism. The hydrolysates had the strongest blood pressure-lowering effect in spontaneously hypertensive rats. Blood pressure-lowering effect contrasted with observed in vitro ACE inhibition. In vitro renin inhibition was consistent with blood pressure-lowering effect. Abstract: Chicken skin protein hydrolysates (CSPHs) and their membrane ultrafiltration fractions were investigated for their blood pressure lowering effects. Chicken skins from thigh or breast muscles were hydrolyzed with 3% Alcalase or 1% pepsin/pancreatin, respectively; hydrolysates were then fractionated into <1, 1–3, 3–5, and 5–10 kDa peptide sizes. Chicken breast skin hydrolysate (CBSH) and peptide fractions inhibited angiotensin converting enzyme (ACE) with IC50 values of 0.36–0.64 mg/mL, which were significantly (p < 0.05) higher than the 0.42–0.75 mg/mL values obtained for chicken thigh skin hydrolysate (CTSH) and peptide fractions. Results suggest that a high content of branched-chain amino acids contributed to the significantly (p < 0.05) higher ACE-inhibition by <1 kDa peptide fraction. All the samples with exception of the CBSH 3 kDa fraction had similar renin inhibitory values. Kinetics studies revealed that enzyme inhibition pattern was mostly of the mixed-type for ACE and renin. Oral administration of 100 mg peptides/kg body weight to spontaneously hypertensive rats led to maximum systolic blood pressure reduction of −32.67 and −31.33 mmHg after 6 h for CTSH and CBSH, respectively. We conclude that the CSPHs have potential use as active ingredients to formulate antihypertensive functional foods and nutraceuticals.