Isolation and characterization, antioxidant, and antihypertensive activity of novel bioactive peptides derived from hydrolysis of King Boletus mushroom
Journal article
Authors/Editors
Strategic Research Themes
Publication Details
Author list: Kaprasob, Ratchadaporn; Khongdetch, Jindaporn; Laohakunjit, Natta; Selamassakul, Orrapun; Kaisangsri, Nattapon
Publisher: Elsevier
Publication year: 2022
Journal: LWT - Food Science and Technology (0023-6438)
Volume number: 160
ISSN: 0023-6438
Languages: English-Great Britain (EN-GB)
View in Web of Science | View on publisher site | View citing articles in Web of Science
Abstract
King Boletus mushroom protein hydrolysate (KBMPH) was prepared using bromelain and isolated by membrane ultrafiltration into four molecular size fractions (>10, 3–10, 1–3, and <1 kDa). All fractions were assessed for their characteristics, antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. KBMPHF4 (<1 kDa) showed the highest surface hydrophobicity (S0), and high levels of hydrophobic amino acid (HAA). KBMPHF4 at 1 mg/mL exhibited antioxidative against DPPH• and ABTS•+ and linoleic acid oxidation, and ACE inhibitory activity (IC50 = 0.12 mg/mL). Peptide fraction-51 from ion-exchange-chromatography (IEC) showed high protein content, and biological properties. Three novel peptides (SETGGGHTTSCETDLGEFL, AAPLPGP, and GTDPTGEMLT) from F1 fraction had the highest antioxidant capacity and moderate ACE inhibitory activity. Six novel peptides (DLDLLEKGIRKT, NGGNAPI, VSWNVLQEP, DTGRGLGASH, IDDNLDNLIIKL, and LIYAQGFSK) from F4 fraction had moderate antioxidant capacity and the highest ACE inhibitory activity. LIYAQGFSK peptide had the greatest ACE-binding energy (−9.2 kcal/mol) through hydrogen bonds. Overall, novel peptides from KBMPHF4 could be potential use as natural antioxidants and antihypertensives in functional food and nutraceutical. © 2022
Keywords
ACE inhibitory Activity, King boletus mushroom peptides
ติดต่อสอบถามเพิ่มเติมได้ที่