scholarly journals Comparative assessment of physicochemical and antioxidative properties of mung bean protein hydrolysates

RSC Advances ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 2634-2645
Author(s):  
Zhaojun Zheng ◽  
Man Wang ◽  
Jiaxin Li ◽  
Jinwei Li ◽  
Yuanfa Liu
Keyword(s):  
Mung Bean ◽  
Protein Hydrolysates ◽  
Comparative Assessment ◽  
Antioxidative Properties ◽  
Commercial Plant ◽  
Plant Proteases ◽  
Bean Protein

Two commercial plant proteases namely ficin and bromelain, were acquired to hydrolyze mung bean protein over 300 min hydrolysis, and the physicochemical and antioxidative properties of the obtained hydrolysates were investigated.

scholarly journals Mung Bean Protein Hydrolysates Protect Mouse Liver Cell Line Nctc-1469 Cell from Hydrogen Peroxide-Induced Cell Injury

Foods ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 14 ◽  
Author(s):  
Jianhua Xie ◽  
Hedan Ye ◽  
Mengxia Du ◽  
Qiang Yu ◽  
Yi Chen ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Mung Bean ◽  
Cell Injury ◽  
Aromatic Amino Acids ◽  
Medical Application ◽  
Protein Hydrolysates ◽  
Dependent Relationship ◽  
Mouse Liver Cell ◽  
Bean Protein

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.

Isolation and characterization of zinc-binding peptides from mung bean protein hydrolysates

2019 ◽  
Vol 246 (1) ◽  
pp. 113-124 ◽  
Author(s):  
Tianxin Fu ◽  
Shu Zhang ◽  
Yanan Sheng ◽  
Yuchao Feng ◽  
Yingjun Jiang ◽  
...  
Keyword(s):  
Mung Bean ◽  
Protein Hydrolysates ◽  
Zinc Binding ◽  
Isolation And Characterization ◽  
Binding Peptides ◽  
Bean Protein

Mung-bean Protein Hydrolysates Obtained with Alcalase Exhibit Angiotensin I-converting Enzyme Inhibitory Activity

2005 ◽  
Vol 11 (4) ◽  
pp. 281-287 ◽  
Author(s):  
Guan Hong Li ◽  
Guo Wei Le ◽  
Huan Liu ◽  
Yong Hui Shi
Keyword(s):  
Inhibitory Activity ◽  
Mung Bean ◽  
Protein Hydrolysates ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory ◽  
Bean Protein

Mung-bean protein isolates were hydrolysed by two proteases alcalase and neutrase commercially available for food industry use, and the angiotensin I-converting enzyme (ACE) inhibitory activities of the enzymatic hydrolysates were measured at different hydrolysis times. The non-hydrolysed protein showed no inhibitory activity. Hydrolysates generated with neutrase displayed very low ACE inhibitory activity, while those obtained with alcalase exhibited high inhibitory activity. The highest ACE inhibitory activity with the IC50 value of 0.64 mg protein/mL was found in the hydrolysate obtained with alcalase at 2h of hydrolysis time. These results indicated that mung-bean protein is a good protein source of ACE inhibitory peptides when hydrolysed with the protease alcalase. The mung-bean protein hydrolysates prepared with alcalase might be utilised for physiologically functional foods with antihypertensive activity.

Extraction, physicochemical characteristics and functional properties of Mung bean protein

2018 ◽  
Vol 76 ◽  
pp. 131-140 ◽  
Author(s):  
Mengxia Du ◽  
Jianhua Xie ◽  
Bin Gong ◽  
Xin Xu ◽  
Wei Tang ◽  
...  
Keyword(s):  
Functional Properties ◽  
Mung Bean ◽  
Physicochemical Characteristics ◽  
Bean Protein

Effect of Trypsin on Antioxidant Activity and Gel-Rheology of Flaxseed Protein

2017 ◽  
Vol 13 (3) ◽  
Author(s):  
Yuan-yuan Chang ◽  
Chong-hao Bi ◽  
Li-jun Wang ◽  
Dong Li ◽  
Benu Adhikari ◽  
...  
Keyword(s):  
Gel Strength ◽  
Protein Hydrolysates ◽  
Hydrodynamic Diameter ◽  
Considerable Decrease ◽  
Antioxidative Properties ◽  
Trypsin Hydrolysis ◽  
Gelling Property ◽  
High Degree ◽  
Hydrolysis Of ◽  
Antioxidative Property

Abstract Enzymatic hydrolysis of flaxseed protein (FP) was carried out using trypsin in order to obtain flaxseed protein hydrolysates possessing better antioxidative property and modified rheological properties. The antioxidative properties of hydrolysates were much higher than the unhydrolyzed flaxseed protein. The hydrolysis also significantly reduced the hydrodynamic diameter of the magnitude of zeta potential of the dispersions. The gelling point of the hydrolysates occurred earlier than the unhydrolyzed sample while the duration of hydrolysis (30–120 min) did not affect gelling point of the hydrolysates. Considerable decrease in the gel strength and the frequency dependence of gel strength were observed in gels produced using hydrolyzed flaxseed protein. The above findings indicate that hydrolysates possessing high degree of antioxidative properties. The gels produces from these hydrolysates will have fast gelling property and will produce gels with reasonable strength. Thus, flaxseed protein hydrolysates obtained from trypsin hydrolysis can be used in applications that require proteins with higher antioxidative properties but softer texture.

scholarly journals Whole Wheat Crackers Fortified with Mixed Shrimp Oil and Tea Seed Oil Microcapsules Prepared from Mung Bean Protein Isolate and Sodium Alginate

Foods ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 202
Author(s):  
Saqib Gulzar ◽  
Krisana Nilsuwan ◽  
Navaneethan Raju ◽  
Soottawat Benjakul
Keyword(s):  
Fatty Acids ◽  
Sodium Alginate ◽  
Mung Bean ◽  
Seed Oil ◽  
Protein Isolate ◽  
Tea Seed Oil ◽  
Whole Wheat ◽  
Wide Range ◽  
Shrimp Oil ◽  
Bean Protein

Shrimp oil (SO) rich in n-3 fatty acids and astaxanthin, mixed with antioxidant-rich tea seed oil (TSO), was microencapsulated using mung bean protein isolate and sodium alginate and fortified into whole wheat crackers. SO and TSO mixed in equal proportions were emulsified in a solution containing mung bean protein isolate (MBPI) and sodium alginate (SA) at varied ratios. The emulsions were spray-dried to entrap SO-TSO in MBPI-SA microcapsules. MBPI-SA microcapsules loaded with SO-TSO showed low to moderately high encapsulation efficiencies (EE) of 32.26–72.09% and had a fair flowability index. Two selected microcapsules with high EE possessed the particle sizes of 1.592 and 1.796 µm with moderate PDI of 0.372 and 0.403, respectively. Zeta potential values were −54.81 mV and −53.41 mV. Scanning electron microscopic (SEM) images indicated that microcapsules were spherical in shape with some shrinkage on the surface and aggregation took place to some extent. Fourier transform infrared (FTIR) and differential scanning calorimetry (DSC) analyses of samples empirically validated the presence of SO-TSO in the microcapsules. Encapsulated SO-TSO showed superior oxidative stability and retention of polyunsaturated fatty acids (PUFAs) to unencapsulated counterparts during storage of 6 weeks. When SO-TSO microcapsules were fortified in whole wheat crackers at varying levels (0–10%), the crackers showed sensorial acceptability with no perceivable fishy odor. Thus, microencapsulation of SO-TSO using MBPI-SA as wall materials could be used as an alternative carrier system, in which microcapsules loaded with PUFAs could be fortified in a wide range of foods.

scholarly journals The anti hypertensive nutraceuticals of Vigna sp bean protein hydrolized by alcalase and flavourzyme

2020 ◽  
Vol 2 (1) ◽  
pp. 63-73
Author(s):  
Tejasari ◽  
Sih Yuwanti ◽  
Mohammad Bazar Ahmadi ◽  
Yuna Luki Afsari
Keyword(s):  
Amino Acids ◽  
G Protein ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Small Molecular Weight ◽  
Hydrophobic Amino Acids ◽  
Prevention Of Hypertension ◽  
Hydrolysis Of ◽  
Bean Protein

Peptide with hydrophobic amino acids had been studied for their inhibitory activity against angiotensin-I converting enzyme (ACE-1) transformation into ACE-2 and prevention of hypertension. The active peptides may come from alcalase and flavourzyme hydrolysis of bean protein. This study aimed to measure ACE-1 inhibitory of protein hydrolysates from Vigna sp. bean (mung bean and cowpea) that grew in Indonesia, and its solubility. The bean protein (22.9 - 23.6 %) was extracted using isoelectric precipitation at pH 4-4.6. The extracts were hydrolyzed at pH 8 for alcalase and pH 7 for flavourzyme, followed with inactivation at 80-85 oC. ACE-1 inhibitory activity was calculated based on the amount of hippuric acid (HA) formed by the hydrolysis of Hippuryl-His-Leu (HHL), in spectrophotometry detection method (228 nm). Ultrachromatography evaluation showed that the protein hydrolysates of mungbean contained higher hydrophobic amino acids (382 mg/g protein) compared to those of cowpea (329 mg/g protein). Protein hydrolysates of both beans from alcalase hydrolysis have higher ACE-1 inhibitory activity rather than those from flavourzyme. Protein hydrolysate from Vigna spp bean protein hydrolysis by alcalase, contained small molecular weight peptides (3.9-4.63 kDa) and high ACE-1 inhibition ability (80-93 %), and therefore suggested as antihypertensive nutraceuticals. Highest solubility of protein hydrolysates resulted from alcalase hydrolysis of both beans were observed at pH 8, while those resulted from flavorzyme hydrolysis were at pH 7, respectively.

Structural and rheological properties of mung bean protein emulsion as a liquid egg substitute: The effect of pH shifting and calcium

2022 ◽  
pp. 107485
Author(s):  
Ying Wang ◽  
Jing Zhao ◽  
Shucheng Zhang ◽  
Xiangzhong Zhao ◽  
Yuanfa Liu ◽  
...  
Keyword(s):  
Rheological Properties ◽  
Mung Bean ◽  
Effect Of Ph ◽  
Ph Shifting ◽  
Bean Protein
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