Peer-Reviewed Journal Details
Mandatory Fields
Neves, AC,Harnedy, PA,O'Keeffe, MB,Alashi, MA,Aluko, RE,FitzGerald, RJ
2017
October
Food Research International
Peptide identification in a salmon gelatin hydrolysate with antihypertensive, dipeptidyl peptidase IV inhibitory and antioxidant activities
Published
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Optional Fields
Salmon gelatin Bioactive peptides Angiotensin converting enzyme Dipeptidyl peptidase IV Oxygen radical absorbance capacity Spontaneously hypertensive rats ANGIOTENSIN-CONVERTING ENZYME SKIN GELATIN WHEY-PROTEIN PURIFICATION EXTRACTION STABILITY SALAR ACID
100
112
120
Salmon gelatin (Salmo salar, SG) enzymatic hydrolysates were generated using Alcalase 2.4 L, Alcalase 2.4 L in combination with Flavourzyme 500 L, Corolase PP, Promod 144MG and Brewer's Clarex. The hydrolysate generated with Corolase PP for 1 h (SG-C1) had the highest angiotensin converting enzyme (ACE, IC50 = 0.13 +/- 0.05 mg mL(-1)) and dipeptidyl peptidase IV (DPP-IV, IC50 = 0.08 +/- 0.01 mg mL(-1)) inhibitory activities, and oxygen radical absorbance capacity (ORAC, 540.94 +/- 9.57 mu mol TE g(-1) d.w.). The in Vitro bioactivities of SG-C1 were retained following simulated gastrointestinal digestion. Administration of SG and SG-C1 (50 mg kg(-1) body weight) to spontaneously hypertensive rats (SHR) lowered heart rate along with systolic, diastolic and mean arterial blood pressure. The SG-C1 hydrolysate was fractionated using semi-preparative RP-HPLC and the fraction with highest overall in vitro bioactivity (fraction 25) was analysed by UPLC-MS/MS. Four peptide sequences (Gly-Gly-Pro-Ala-Gly-Pro-Ala-Val, Gly-Pro-Val-Ala, Pro-Pro and Gly-Phe) and two free amino acids (Arg and Tyr) were identified in this fraction. These peptides and free amino acids had potent ACE and DPP-IV inhibitory, and ORAC activities. The results show that SG hydrolysates have potential as multifunctional food ingredients particularly for the management of hypertension.
10.1016/j.foodres.2017.06.065
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