Production of antioxidant and ACE-inhibitory peptides from Kluyveromyces marxianus protein hydrolysates: Purification and molecular docking

Abstract

Kluyveromyces marxianus protein hydrolysates were prepared by two different sonicated-enzymatic (trypsin and chymotrypsin) hydrolysis treatments to obtain antioxidant and ACE-inhibitory peptides. Trypsin and chymotrypsin hydrolysates obtained by 5 h, exhibited the highest antioxidant and ACE-inhibitory activities. After fractionation using ultrafiltration and reverse phase high performance liquid chromatography (RP-HPLC) techniques, two new peptides were identified. One fragment (LL-9, MW = 1180 Da) with the amino acid sequence of Leu-Pro-Glu-Ser-Val-His-Leu-Asp-Lys showed significant ACE inhibitory activity (IC = 22.88 μM) while another peptide fragment (VL-9, MW = 1118 Da) with the amino acid sequence of Val-Leu-Ser-Thr-Ser-Phe-Pro-Pro-Lys showed the highest antioxidant and ACE inhibitory properties (IC = 15.20 μM, 5568 μM TE/mg protein). The molecular docking studies revealed that the ACE inhibitory activities of VL-9 is due to interaction with the S2 (His513, His353, Glu281) and S'1 (Glu162) pockets of ACE and LL-9 can fit perfectly into the S1 (Thr345) and S2 (Tyr520, Lys511, Gln281) pockets of ACE.

Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

“…It also would be supposed that the peptide sequences were buried deeper in the original protein structures from which they come or the sequences were embedded in the structured parts in which they were forced to be in the conformations that could not fit the active site of ACE. These results were also similar to that of other reports [20][21][22][23].…”

Novel ACE inhibitors derived from soybean proteins using in silico and in vitro studies

“…Moreover, YASGR was docked into the active pockets of ACE with the residues Ala354 and His353, and GNGSGYVSR‐ACE complex were stabilized by binding with the residues Glu384 and Tyr523 (Guo et al, ). Simultaneously, VL‐9 (VLESFPPK) interaction with S 2 pocket (His513, His353, Glu281) and S 1 ’ pocket (Glu162) of ACE, moreover, LL‐9 (LPESVHLDK) (Mirzaei, Mirdamadi, Ehsani, & Aminlari, ) could be docked into S 2 (Gln281, Lys511, Tyr520) of ACE. Thus, according to the docking result and others research consequences, it is a speculation that EGW, DMG, and DTW have the potential to reduce blood pressure.…”

Bifunctional peptides with antioxidant and angiotensin‐converting enzyme inhibitory activity in vitro from egg white hydrolysates

“…Whereas, lysine was often at the C‐terminus (Lee & Hur, 2017). For example, the peptide LPESVHLDK was determined to be potent ACE inhibitory peptides (Mirzaei, Mirdamadi, Ehsani, & Aminlari, 2018). In our results, it could be demonstrated by the strong ACE‐inhibitory activity of the peptide LAPYK.…”