A novel antioxidant and ACE inhibitory peptide from rice bran protein: Biochemical characterization and molecular docking study. (January 2017)

• Record Type: Journal Article
• Authors: Wang, Xiuming; Chen, Haixia; Fu, Xuegang; Li, Shuqin; Wei, Jing
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 75(2017)
• Page Start: 93
• Page End: 99
• Publication Date: 2017-01
• Subjects: Rice bran -- Antioxidant activities -- ACE inhibitory activity -- Peptide -- Molecular docking; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2016.08.047
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: Rice bran protein was hydrolyzed using trypsin. The hydrolysate (RBPH) was then further separated by membrane bioreactor system, gel filtration and reversed phase high-performance liquid chromatography (RP-HPLC). A novel antioxidant and angiotensin I-converting enzyme (ACE) inhibitory peptide named as F2-a, which exhibited high DPPH free radicals scavenging activity, reducing power and ACE inhibitory activity (IC50 of 76 μM) was isolated. The amino acid sequence, Tyr-Ser-Lys (Mw: 395.0 Da), was identified by Quardrupole Time-of-flight Mass Spectrometer (Q-TOF-MS) with an electro-spray ionization (ESI) source. The molecular docking study revealed that the ACE inhibition of Tyr-Ser-Lys was mainly attributed to forming very strong hydrogen bonds with the active pockets of human ACE. These results indicate that rice bran is a potential source of bioactive peptides possessing antioxidant and ACE inhibitory activities. Highlights: Rice bran protein was hydrolyzed using trypsin and the hydrolysates were isolated and purified. A novel antioxidant and antihypertension peptide was obtained. The amino acid sequences, Tyr-Ser-Lys was identified by Q-TOF-MS. Molecular docking studies were firstly used to reveal the ACE inhibition of the peptide.