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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.
Abstract:
Mung bean is nutritious and rich in protein (19.5%-33.1%). However, there are few studies on mung bean protein active peptides so the mung bean protein hydrolysates (MBPHs) were investigated for evaluating their ability to clear intracellular reactive oxygen species (ROS) and regulating the ability of antioxidant enzymes on NCTC-1469 cells. Results showed that MBPHs, MBPHs-I (molecular weight < 3 kDa), MBPHs-II (molecular weight between 3 and 10 kDa), and MBPHs-III (molecular weight > 10 kDa) could all improve the survival rate of cells compared with the model group. MBPHs, MBPHs-I, and MBPHs-II could significantly decrease the content of lactate dehydrogenase (LDH) and reduce the generation of malonaldehyde (MDA) at a concentration of 0.4 mg/mL. Regarding the intracellular ROS, the result showed that MBPHs-I significantly reduced the production of ROS (from 58.3% to 26.6%) and had a dose-dependent relationship. In addition, the amino acid analysis showed that MBPHs-I had a balanced amino acid composition. MBPHs-I is rich in lysine but was deficient in cereals. Therefore, the hydrophobic and aromatic amino acids in MBPHs-I were high, which could improve its antioxidant activity. According to the results, MBPHs-I was the best and most potent natural antioxidant and it can contribute to drug development and medical application.
Insights
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.
