Vicilin—A major storage protein of mungbean exhibits antioxidative potential, antiproliferative effects and ACE inhibitory activity

Xuanwei ham is especially rich in a large amount of peptides and free amino acids under the action of protein degradation. Some of these peptides can potentially exert bioactivities of interest for human health. Traditionally, Xuanwei ham should undergo Chinese household cooking treatments before eating. However, it has not been known how its bioactivity changes after cooking and gastrointestinal digestion. Herein, Xuanwei ham is analysed before and after cooking, as well as gastrointestinal digestion being simulated so as to evaluate and compare its effect on antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. The antioxidant activity is analysed using five different methods, and results demonstrate that cooking has some negative effects on antioxidative capacity when determined using different antioxidant methods except for a significant increment in 1,1'-diphenyl-2-picrylhydrazyl radical-scavenging activity, while ACE inhibitory activity increases significantly after cooking compared with control samples. After gastrointestinal digestion of samples, there is a significant increment of the antioxidant and ACE inhibitory activities in comparison with control and cooked samples. Particularly, after gastrointestinal digestion, free thiols content and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical-cation-scavenging activity of Xuanwei ham, respectively, increase about twice and fourfold, while ACE inhibitory activity increases about twice compared to cooked samples, reaching the value of 83.73%. Therefore, through cooking the antioxidant activity and ACE inhibitory activity of Xuanwei ham are not completely lost and a part of them is still maintained, while gastrointestinal digestion produces a significant enhancement in both bioactivities, highlighting a greater potential for a beneficial physiological effect on human health after eating it.

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Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽

10.3390/biom8040101 ◽

2018 ◽

Vol 8 (4) ◽

pp. 101 ◽

Cited By ~ 7

Author(s):

Guowei Shu ◽

Jie Huang ◽

Chunju Bao ◽

Jiangpeng Meng ◽

He Chen ◽

...

Keyword(s):

Inhibitory Activity ◽

Goat Milk ◽

Cow Milk ◽

Degree Of Hydrolysis ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

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Preparation of rapeseed protein hydrolysates with ACE inhibitory activity by optimization and molecular weight distribution of hydrolysates

Turkish Journal of Biochemistry ◽

10.1515/tjb-2017-0044 ◽

2017 ◽

Vol 42 (4) ◽

Author(s):

Asif Wali ◽

Haile Ma ◽

Muhammad Tayyab Rashid ◽

Qui Fang Liang

Keyword(s):

Molecular Weight ◽

Response Surface ◽

Molecular Weight Distribution ◽

Weight Distribution ◽

Inhibitory Activity ◽

Proteolytic Enzymes ◽

Ace Inhibitory Activity ◽

Rapeseed Protein Hydrolysates ◽

Hydrolysis Conditions ◽

Ace Inhibitory

AbstractObjective:The main purpose of this study was to screen effective proteolytic enzymes for producing hydrolysates from rapes protein, and to optimize hydrolysis conditions using response surface design to prepare hydrolysates with maximum ACE inhibitor activity.Methods:RSM design was successfully applied to the hydrolysis conditions on the basis of single factor experiments which further derived a statistical model for experimental validation. The molecular weight distribution of rapeseed protein hydrolysates with different degree of hydrolysis was also investigated.Results:All the proteolytic enzymes tested produced hydrolysates that possessed ACE inhibitory activity. Aiding RSM design the highest ACE inhibitory activity 56.3% was achieved under optimum hydrolysis conditions at the hydrolysis time, pH, hydrolysis temperature, and enzyme dosage were at 90.11 min, 8.88, 50°C and 3580.36 UgConclusion:Enzymatic hydrolysis and response surface methodology found good techniques in order to achieve hydrolysates with maximum ACE inhibitory activity. The findings of current research suggested that the hydrolysates obtained under optimized conditions could be utilized to formulate nutraceuticals and pharmaceuticals

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