Purification and identification of Ace-inhibitory peptides from poultry viscera protein hydrolysate

Abstract

Three novel Angiotensin I‐converting enzyme (ACE) inhibitory peptides were isolated from poultry viscera protein hydrolysate (PVPH). The purification steps involved ultrafiltration of PVPH to eliminate the high molecular weight peptides and RP‐HPLC. The ACE inhibitory activity was resolved into three peaks on C18 column with retention times of 15.0, 18.9 and 20.9 min and amino acid sequences of the three peptides were determined to be ARIYH, LRKGNLE and RVWCP, respectively. The peptides exhibited resistance to hydrolysis by gastrointestinal proteases and extreme temperature (100C) and pH (1–12) at least for 2 h. Two of these peptides were competitive inhibitors, while the third was noncompetitive. The in vitro ACE inhibitory activity of PVPH revealed it could be a promising economic source for nutraceutical applications. Practical Applications Poultry viscera is a protein‐rich by‐product of poultry processing industry. The tissue protein and its hydrolysate offer huge potential for different bioactive peptides. In the present study three novel ACE inhibitory peptides were identified and characterized from poultry viscera protein hydrolysate (PVPH). These peptides could be tested further for their in vivo antihypertensive effect and as functional ingredient in foods.

Antihypertensive and bovine plasma oxidation-inhibitory activities of spent hen meat protein hydrolysates

“…As shown in Table , several peptides were matched with fragments of major chicken skeletal muscle proteins, especially actin and MHC, released via specific cleavage by pepsin, trypsin, chymotrypsin, or their combinations. Moreover, release of peptides from unspecific autolysis of poultry meat is also possible (Mane & Jamdar, ). A search of BIOPEP database indicated that none of the predicted peptide sequences has been reported to possess bioactivity.…”

“…However, it is not certain if surface hydrophobicity directly contributed to enzyme inhibition, as bioactivity has only been found to be dependent on molecular hydrophobicity for individual dipeptides (Udenigwe, Li, & Aluko, ) and can also be due to the collective functionality of interacting peptides present in the hydrolysates. ACE and renin inhibiting peptides have been generated from chicken meat processing wastes (Lafarga & Hayes, ; Lafarga, Rai, O'connor, & Hayes, ; Mane & Jamdar, ; Udenigwe & Howard, ). The RAS enzymes are key physiological regulators of blood pressure and have been widely targeted in developing drugs and food‐derived antihypertensive agents.…”

Purification of Angiotensin-I-Converting Enzyme Inhibitory Peptides Derived from Camellia oleifera Abel Seed Meal Hydrolysate

“…Alkaline protease is a kind of serine enzyme that tends to form the peptide with hydrophobic amino acids at the end [9,31]. Furthermore, alkaline protease can cut -CO-NH internal peptide, which makes protein converted into peptides with a smaller molecular weight [7,29]. Vasquez-Villanueva et al used alkaline protease to enzymolyze corn protein and found that the alkaline protease hydrolysate has a high ACE inhibitory rate [30].…”

“…After isolating Sephadex G-25, the component with highest ACE inhibitory rate was dissolved in ultrapure water. After 0.22 µm membrane filtering, RP-HPLC was conducted for further purification with the following conditions: chromatographic column: C 18 column (standard: 4.6 × 100 mm, 5 μm), detection wavelength of 215 nm, and mobile phases A (acetonitrile) and B (ultrapure water containing 0.10% trifluoroacetic acid); elution conditions were 0% A for 5 min and 0-40% A for 5-30 min; sample quantity of 10 μl; and column temperature at 35°C [21,29].…”

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

“…Bioactive ingredients in food can improve health conditions and minimize the dependence on synthetic medicines (Rui, Boye, Simpson, & Prasher, ). In recent years, a number of studies on novel functional ingredients, such as hydrolyzed proteins and bioactive peptides from various food sources, have appeared (Ghassem, Babji, Said, Mahmoodani, & Arihara, ; Girgih, Udenigwe, & Aluko, ; Mane & Jamdar, ; Sae‐Leaw et al, ). Plant protein‐derived peptides have been less researched than those from animal sources, although plants are recognized as cheap sources of protein with many potential functional activities (Aluko, ; Cheng, Xiong, & Chen, ; Jahanbani et al, ; Megías et al, ; Valverde, Orona‐Tamayo, Nieto‐Rendón, & Paredes‐López, ; Vásquez‐Villanueva, Marina, & García, ).…”