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Mung Bean Protein Hydrolysates Protect Mouse Liver Cell Line Nctc-1469 Cell from Hydrogen Peroxide-Induced Cell
Jianhua Xie1, Hedan Ye1, Mengxia Du1
1State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China.
Foods (Basel, Switzerland)
|December 28, 2019
Summary
Mung bean protein hydrolysates (MBPHs), particularly MBPHs-I, demonstrate potent antioxidant activity by reducing reactive oxygen species (ROS) and enhancing cell survival. These findings highlight MBPHs-I as a promising natural antioxidant for medical applications.
Area of Science:
- Biochemistry
- Food Science
- Cell Biology
Background:
- Mung bean protein is a rich source of nutrients, yet its bioactive peptides remain understudied.
- Investigating mung bean protein hydrolysates (MBPHs) for antioxidant properties is crucial for potential health applications.
Purpose of the Study:
- To evaluate the antioxidant capacity of mung bean protein hydrolysates (MBPHs) in NCTC-1469 cells.
- To identify specific fractions of MBPHs with significant reactive oxygen species (ROS) scavenging and antioxidant enzyme regulating abilities.
Main Methods:
- Mung bean protein was hydrolyzed and fractionated into MBPHs-I (<3 kDa), MBPHs-II (3-10 kDa), and MBPHs-III (>10 kDa).
- Cell viability, lactate dehydrogenase (LDH), malonaldehyde (MDA), and intracellular ROS levels were assessed in NCTC-1469 cells exposed to MBPHs.
- Amino acid composition of the most active fraction was analyzed.
Main Results:
- All MBPH fractions improved cell survival. MBPHs, MBPHs-I, and MBPHs-II significantly reduced LDH and MDA levels at 0.4 mg/mL.
- MBPHs-I demonstrated a significant, dose-dependent reduction in intracellular ROS production (from 58.3% to 26.6%).
- MBPHs-I exhibited a balanced amino acid profile, rich in lysine, with high levels of hydrophobic and aromatic amino acids contributing to its antioxidant activity.
Conclusions:
- MBPHs-I is identified as the most potent natural antioxidant fraction derived from mung bean protein.
- MBPHs-I's ability to clear ROS and its favorable amino acid composition suggest significant potential for drug development and medical applications.
