Analysis of whey protein hydrolysates: peptide profile and ACE inhibitory activity

Abstract

The aim of this study was to prepare enzymatic hydrolysates from whey protein concentrate with a nutritionally adequate peptide profile and the ability to inhibit angiotensin-converting enzyme (ACE) activity. The effects of the type of enzyme used (pancreatin or papain), the enzyme:substrate ratio (E:S ratio=0.5:100, 1:100, 2:100 and 3:100) and the use of ultrafiltration (UF) were investigated. The fractionation of peptides was performed by size-exclusion-HPLC, and the quantification of the components of the chromatographic fractions was carried out by a rapid Corrected Fraction Area method. The ACE inhibitory activity (ACE-IA) was determined by Reverse Phase-HPLC. All parameters tested affected both the peptide profile and the ACE-IA. The best peptide profile was achieved for the hydrolysates obtained with papain, whereas pancreatin was more advantageous in terms of ACE-IA. The beneficial effect of using a lower E:S ratio on the peptide profile and ACE-IA was observed for both enzymes depending on the conditions used to prepare the hydrolysates. The beneficial effect of not using UF on the peptide profile was observed in some cases for pancreatin and papain. However, the absence of UF yielded greater ACE-IA only when using papain.

Whey Protein Concentrate as a Novel Source of Bifunctional Peptides with Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Properties: RSM Study

“…At higher DH, a higher ACE inhibitory bioactivity was achieved. This result is in line with the work reported by Silvestre et al [36] and Ghanbari et al [37], in which the ACE-inhibitory activity of protein hydrolysates was affected by the type of enzymes as well as the degree of hydrolysis. Also, the increased level of E/S ratio and alkali pH resulted in high values of DH to indicate the release of potent peptides which further contributed towards the strong ACE-inhibitory activity.…”

Camel Hemorphins Exhibit a More Potent Angiotensin-I Converting Enzyme Inhibitory Activity than Other Mammalian Hemorphins: An In Silico and In Vitro Study

“…From a structure activity point of view of ACE inhibitors, studies have demonstrated that the ACE inhibitory activity of a peptide depends on the presence of specific residues at N and C-termini [8]. The presence of hydrophobic residues, particularly leucine, valine, isoleucine, and glycine, at the N-terminus of a peptide, produced higher ACE inhibitory activity, while aromatic amino acids, such as phenylalanine, proline, tryptophan, and tyrosine, are preferred at the C-terminus [55]. Additionally, the presence of positively charged residues, specifically arginine and lysine, near the C-terminus were also considered to be essential for the ACE inhibitory potential of peptides [56].…”

In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

“…Hayes et al [6] have shown that after fractionation, the 3-kDa boarfish protein hydrolysate generated using protease AP inhibited the ACE by 85.8 % at 1 mg/ml, while the hydrolysate showed an activity of 72.08%. On the other hand, Silvestre et al [11] have reported that the UF process may cause the retention of peptides with structures (aromatic amino acids or proline at the C-terminal position) that favor ACE-inhibitory activity. However, in some cases, UF showed no effect on the enhancement of the ACE-inhibitory activity.…”