Antityrosinase and antioxidant properties of mung bean seed proanthocyanidins: Novel insights into the inhibitory mechanism

• Published in: Food chemistry Vol. 260; pp. 27 - 36
• Main Authors: Chai, Wei-Ming, Ou-Yang, Chong, Huang, Qian, Lin, Mei-Zhen, Wang, Ying-Xia, Xu, Kai-Li, Huang, Wen-Yang, Pang, Dan-Dan
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 15.09.2018
• Subjects: Antioxidant; Antioxidants - chemistry; Antioxidants - pharmacology; Chromatography, High Pressure Liquid - methods; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - pharmacology; ESI-Full-MS; HPLC-ESI-MS; Kinetics; MALDI-TOF MS; Molecular Docking Simulation; Molecular Structure; Monophenol Monooxygenase - antagonists & inhibitors; Monophenol Monooxygenase - chemistry; Monophenol Monooxygenase - metabolism; Mung bean; Proanthocyanidins; Proanthocyanidins - chemistry; Proanthocyanidins - pharmacology; Seeds - chemistry; Seeds - metabolism; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tyrosinase inhibitor; Vigna - chemistry; MALDI-TOF MS; ESI-Full-MS; HPLC-ESI-MS; Tyrosinase inhibitor; Antioxidant; Mung bean; Proanthocyanidins
• DOI: 10.1016/j.foodchem.2018.04.001
• ISSN: 0308-8146

•Mung bean contained procyanidins, prodelphinidins, and their rhamnosides.•Mung bean proanthocyanidins were efficient tyrosine inhibitor.•Hydrogen bond, hydrophobic, and electrostatic interactions caused the inhibition.•Mung bean proanthocyanidins had powerful antioxidant activity. This study investigated the structure, antioxidant activity, antityrosinase activity and mechanism of proanthocyanidins from mung bean seed [Vigna radiata (L.) Wilczek]. The structural composition were characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), electrospray ionization-full-mass spectrometry (ESI-Full-MS), and high-pressure liquid chromatography-electrospray ionization-mass spectrometry (HPLC-ESI-MS) techniques. The mung bean seed proanthocyanidins were composed of procyanidins, prodelphinidins, and their rhamnosides. According to enzyme kinetic analysis, these compounds were potent, reversible, and mixed-type inhibitors of tyrosinase. They inhibited the enzyme activity by interacting with enzyme as well as substrates. The results of molecular docking showed that the interaction between mung bean seed proanthocyanidins and tyrosinase was driven by hydrogen bond, hydrophobic and electrostatic interactions. In addition, mung bean seed proanthocyanidins were demonstrated as powerful antioxidants. Therefore, this study confirmed a novel tyrosinase inhibitor and would lay a scientific foundation for their utilization in pharmaceutical and food industries.