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 50 = 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 50 = 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. © 2017
ScienceDirect Link
Recommended Citation
Mirzaei, M.; Mirdamadi, S.; Ehsani, M.R.; and Aminlari, M.
(2018)
"Production of antioxidant and ACE-inhibitory peptides from Kluyveromyces marxianus protein hydrolysates: Purification and molecular docking,"
Journal of Food and Drug Analysis: Vol. 26
:
Iss.
2
, Article 42.
Available at: https://doi.org/10.1016/j.jfda.2017.07.008
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Fulltext URL
https://www.sciencedirect.com/science/article/pii/S102194981730145X/pdfft?md5=fae148ad2414a76a5d48f882642b49a6&pid=1-s2.0-S102194981730145X-main.pdf
Included in
Food Science Commons, Medicinal Chemistry and Pharmaceutics Commons, Pharmacology Commons, Toxicology Commons
Abstract Image