2019
DOI: 10.3389/fphar.2018.01579
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Three Novel ACE Inhibitory Peptides Isolated From Ginkgo biloba Seeds: Purification, Inhibitory Kinetic and Mechanism

Abstract: Alcalase, dispase, trypsin, and flavourzyme were used to hydrolyze the extracted Ginkgo biloba seeds protein isolate (GPI). The Ginkgo protein hydrolyzates (GPHs) with the maximum degree of hydrolysis (DH) and ACE inhibitory activity were selected, and ultra-filtered to obtain components with different molecular weights (MW) (<1 kDa, 1–3, 3–5, and 5–10 kDa). The components with MW of <1 kDa showed better ACE inhibition (IC50:0.2227 mg/mL). Purification and identification by Sephadex G-15 gel chromatography and… Show more

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Cited by 73 publications
(47 citation statements)
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“…Since the inhibition pattern of the ACE inhibitory peptides is related to their inhibitory structures, we hypothesize that these peptides may have similar structures to the substrate; hence, they might compete with the substrate for binding to the same interaction site on the enzyme. Most of the ACE inhibitory peptides show competitive inhibition patterns 31 , as is also seen in this study. By using secondary plots (Fig.…”
Section: Resultssupporting
confidence: 86%
See 1 more Smart Citation
“…Since the inhibition pattern of the ACE inhibitory peptides is related to their inhibitory structures, we hypothesize that these peptides may have similar structures to the substrate; hence, they might compete with the substrate for binding to the same interaction site on the enzyme. Most of the ACE inhibitory peptides show competitive inhibition patterns 31 , as is also seen in this study. By using secondary plots (Fig.…”
Section: Resultssupporting
confidence: 86%
“…1B,C). Accordingly, these small peptides seemed to have higher inhibitory activity towards ACE than some other peptides described in literature as ACE inhibitors including TNLDWY (IC 50 = 1.932 mM), RADFY (IC 50 = 1.35 mM), and RVFDGAV (IC 50 = 1.00 mM) purified from Ginkgo biloba seeds 31 , while they are less active than some other peptides such as KAQYPYV (IC 50 = 0.0370 mM), KIIIYN (IC 50 = 0.058 mM), and KILIYG (IC 50 = 0.053 mM) purified from coconut cake albumin hydrolysates 32 . The IC 50 value of captopril was calculated to be 2.2 ng/ml which is lower than those of F2 and F4 peptides.…”
Section: Resultsmentioning
confidence: 78%
“…These pockets harbor residues that interacts with potential inhibitors [6,50]. Ala354, Glu384, and Tyr523 constitute the S1 subsite; Gln281, His353, Lys511, His513, and Tyr520 constitute the S2 subsite, and Glu162 forms part of the S1′ subsite [51].…”
Section: Discussionmentioning
confidence: 99%
“…The binding stability of peptides at the binding site of the ACE enzyme depends upon hydrogen bonding [86]. Additionally, the involvement of His353, Ala354, Ser355, Glu384, His513, and Pro519 residues are significant for the stability of peptide and enzyme complex while numerous effective peptides have been reported for their interactions at the specified binding sites [87,88].…”
Section: Derived Peptidesmentioning
confidence: 99%