scholarly journals In Silico Analysis and In Vitro Characterization of the Bioactive Profile of Three Novel Peptides Identified from 19 kDa α-Zein Sequences of Maize

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5405
Author(s):  
Jorge L. Díaz-Gómez ◽  
Ines Neundorf ◽  
Laura-Margarita López-Castillo ◽  
Fabiola Castorena-Torres ◽  
Sergio O. Serna-Saldívar ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Structural Model ◽  
Solid Phase ◽  
Antioxidant Activities ◽  
Ace Inhibitory Activity ◽  
Helical Structures ◽  
In Vitro Characterization ◽  
Ace Inhibitory

In this study, we characterized three novel peptides derived from the 19 kDa α-zein, and determined their bioactive profile in vitro and developed a structural model in silico. The peptides, 19ZP1, 19ZP2 and 19ZP3, formed α-helical structures and had positive and negative electrostatic potential surfaces (range of −1 to +1). According to the in silico algorithms, the peptides displayed low probabilities for cytotoxicity (≤0.05%), cell penetration (10–33%) and antioxidant activities (9–12.5%). Instead, they displayed a 40% probability for angiotensin-converting enzyme (ACE) inhibitory activity. For in vitro characterization, peptides were synthesized by solid phase synthesis and tested accordingly. We assumed α-helical structures for 19ZP1 and 19ZP2 under hydrophobic conditions. The peptides displayed antioxidant activity and ACE-inhibitory activity, with 19ZP1 being the most active. Our results highlight that the 19 kDa α-zein sequences could be explored as a source of bioactive peptides, and indicate that in silico approaches are useful to predict peptide bioactivities, but more structural analysis is necessary to obtain more accurate data.

ACE Inhibitory, Antitumor and Antioxidant Activities of Submerged Culture Materials of Three Medicinal Mushrooms

2011 ◽  
Vol 145 ◽  
pp. 179-183 ◽  
Author(s):  
Xiu Jun Gao ◽  
Pei Sheng Yan ◽  
Jian Bing Wang ◽  
Jia Jia Yu
Keyword(s):  
Inhibitory Activity ◽  
Natural Compound ◽  
Antioxidant Activities ◽  
Inhibitory Effect ◽  
Ace Inhibitory Activity ◽  
Medicinal Mushrooms ◽  
Proliferative Effect ◽  
Ace Inhibitory ◽  
Lyophyllum Decastes

Mushrooms have been highly valued as tonic foods and herb remedies since ancient times, and have been increasingly concerned because of their biological and pharmacological activities recognized through recent scientific research. Antitumor, antioxidant and ACE inhibitory activities in vitro of liquid fermentation materials from Ramaria botrytoides, Lyophyllum decastes and Mycoleptodonoides aitchisonii were investigated in this study. Water extracts from fermented mycelia and supernatant materials were used to measure their antitumor effect by MTT assay, antioxidant capacity by kit, and ACE inhibitory activity by RP-HPLC. Results showed that mycelia extracts from Ramaria botrytoides has significantly higher anti-proliferative effect on human HCC cell line SMMC7721 (IC50=0.284±0.005mg/ml, p<0.001). Total antioxidant activity of mycelia extracts of Ramaria botrytoides (0.711±0.053U/mg), inhibitory effect of mycelia extracts of Mycoleptodonoidesaitchisonii on hydroxyl radical (86.153±1.763U/mg) and superoxide anion radical (7.363±0.280 U/g) were higher than others significantly (p<0.001). ACE inhibitory activity of mycelia extracts of Lyophyllum decastes (IC50=1.637±0.057mg/ml) was significantly higher than others (p<0.001). Results demonstrated that liquid fermented mycelium of Ramaria botrytoides was potent source of natural compound with antitumor and antioxidant potential. Mycelium of Lyophyllum decastes was potent source of natural compound with ACE inhibitory activity.

scholarly journals Simulated Gastrointestinal Digestion of Cocoa: Detection of Resistant Peptides and In Silico/In Vitro Prediction of Their Ace Inhibitory Activity

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 985 ◽  
Author(s):  
Angela Marseglia ◽  
Luca Dellafiora ◽  
Barbara Prandi ◽  
Veronica Lolli ◽  
Stefano Sforza ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Internal Standard ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Cocoa Beans ◽  
Vitro Assay ◽  
Simulated Gastrointestinal Digestion ◽  
Ace Inhibitory

In this study we investigated the oligopeptide pattern in fermented cocoa beans and derived products after simulated gastrointestinal digestion. Peptides in digested cocoa samples were identified based on the mass fragmentation and on the software analysis of vicilin and 21 KDa cocoa seed protein sequences, the most abundant cocoa proteins. Quantification was carried out by liquid chromatography/electrospray ionisation mass spectrometry (LC/ESI-MS) using an internal standard. Sixty five peptides were identified in the digested samples, including three pyroglutamyl derivatives. The in vitro angiotensin-converting enzyme (ACE)-inhibitory activity of cocoa digests were tested, demonstrating a high inhibition activity, especially for digestates of cocoa beans. The peptides identified were screened for their potential ACE inhibitory activity through an in silico approach, and about 20 di-, three- and tetra-peptides actually present in our samples were predicted as active. Two of the potentially active peptides were chemically synthesized and then assessed for their inhibitory activity by using the ACE in vitro assay. These peptides demonstrated an ACE inhibitory activity, however, that was too weak to explain alone the high activity of cocoa digestates, suggesting a synergic effect of all cocoa peptides. As a whole, results showed that an average chocolate portion (30 g) ensures an amount of peptides after digestion that, assuming complete absorption, could reach almost a complete inhibition of ACE.

scholarly journals ACE inhibitory peptides in standard and fermented deer velvet: an in silico and in vitro investigation

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Stephen R. Haines ◽  
Mark J. McCann ◽  
Anita J. Grosvenor ◽  
Ancy Thomas ◽  
Alasdair Noble ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Bioactive Peptides ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
In Vitro Investigation ◽  
Vitro Analysis ◽  
Ace Inhibitory ◽  
In Vitro Analysis

Abstract Background The use of deer velvet antler (DVA) as a potent traditional medicine ingredient goes back for over 2000 years in Asia. Increasingly, though, DVA is being included as a high protein functional food ingredient in convenient, ready to consume products in Korea and China. As such, it is a potential source of endogenous bioactive peptides and of ‘cryptides’, i.e. bioactive peptides enzymatically released by endogenous proteases, by processing and/or by gastrointestinal digestion. Fermentation is an example of a processing step known to release bioactive peptides from food proteins. In this study, we aimed to identify in silico bioactive peptides and cryptides in DVA, before and after fermentation, and subsequently to validate the major predicted bioactivity by in vitro analysis. Methods Peptides that were either free or located within proteins were identified in the DVA samples by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by database searching. Bioactive peptides and cryptides were identified in silico by sequence matching against a database of known bioactive peptides. Angiotensin-converting enzyme (ACE) inhibitory activity was measured by a colorimetric method. Results Three free bioactive peptides (LVVYPW, LVVYPWTQ and VVYPWTQ) were solely found in fermented DVA, the latter two of which are known ACE inhibitors. However matches to multiple ACE inhibitor cryptides were obtained within protein and peptide sequences of both unfermented and fermented DVA. In vitro analysis showed that the ACE inhibitory activity of DVA was more pronounced in the fermented sample, but both unfermented and fermented DVA had similar activity following release of cryptides by simulated gastrointestinal digestion. Conclusions DVA contains multiple ACE inhibitory peptide sequences that may be released by fermentation or following oral consumption, and which may provide a health benefit through positive effects on the cardiovascular system. The study illustrates the power of in silico combined with in vitro methods for analysis of the effects of processing on bioactive peptides in complex functional ingredients like DVA.

Changes in Some Quality Properties of Kefir during Storage and Inhibition Effect of Water Soluble Extracts on Angiotensin-I Converting Enzyme Purified by Human Plasma

2015 ◽  
Vol 11 (5) ◽  
pp. 659-665
Author(s):  
Tuba Erkaya ◽  
Aykut Öztekin ◽  
Hasan Özdemir ◽  
Mustafa Şengül
Keyword(s):  
Human Plasma ◽  
Inhibitory Activity ◽  
Specific Activity ◽  
Storage Period ◽  
Water Soluble ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Quality Properties ◽  
Ace Inhibitory

Abstract Angiotensin converting enzyme (ACE)-inhibitory activity in water soluble extracts (WSEs) of kefir was investigated. Kefir was produced traditionally using kefir grains and stored at refrigerated temperature for 20 days. During storage period (on 1, 5, 10, 15 and 20 days) in vitro ACE-inhibitory activity in WSEs was determined. ACE was purified from human plasma to determine kinetic parameters. Purified ACE had a specific activity of 20.75 EU.mg−1, a yield of 16.6% with a factor of 22100. The inhibition effects of kefir on ACE increased at 15 storage days than other storage days. Some microbiological and physicochemical characteristics of kefir were also studied. Counts of presumptive LAB on M-17 and presumptive LAB on MRS in the kefir were about 108 CFU.ml−1 throughout the storage period. Yeast counts were lower than lactic acid bacteria counts and the average of the counts was approximately 106 log CFU.ml−1. Storage period had a significant effect (P < 0.05) on titratable acidity and pH values. On the contrary, it had no significant effect (P > 0.05) on viscosity and serum separation values of kefir.

scholarly journals Milk Fermentation by Lacticaseibacillus rhamnosus GG and Streptococcus thermophilus SY-102: Proteolytic Profile and ACE-Inhibitory Activity

Fermentation ◽  
2021 ◽  
Vol 7 (4) ◽  
pp. 215
Author(s):  
Jessica Lizbeth Sebastián-Nicolas ◽  
Elizabeth Contreras-López ◽  
Juan Ramírez-Godínez ◽  
Alma Elizabeth Cruz-Guerrero ◽  
Gabriela Mariana Rodríguez-Serrano ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Ace Inhibition ◽  
Added Value ◽  
Low Molecular Weight ◽  
Ace Inhibitory Activity ◽  
Milk Fermentation ◽  
Sds Page ◽  
Ace Inhibitory

Health benefits of probiotics and production of inhibitors of angiotensin converting enzyme (ACE) released during milk fermentation are well known. That is why in this investigation the proteolytic profile and ACE inhibitory capacity of peptide fractions from protein hydrolysis of milk during fermentation processes was analyzed. Milk fermentation was carried out inoculating 106 CFU of L. rhamnosus GG, S. thermophilus SY-102 and with both bacteria. The proteolytic profile was determined using: TNBS, SDS-PAGE and SEC-HPLC techniques. In vitro ACE inhibition capacity was measured. The pH of 4.5 was reached at 56 h when the milk was fermented with L. rhamnosus, at 12 h with S. thermophillus and at 41 h in the co-culture. Production of free amino groups corresponded with the profile of low molecular weight peptides observed by SDS-PAGE and SEC-HPLC. Co-culture fermentation showed both the highest concentration of low molecular weight peptides and the ACE inhibitory activity (>80%). Results indicated that the combination of lactic cultures could be useful in manufacture of fermented milk with an added value that goes beyond basic nutrition, such as the production of ACE-inhibitory peptides.

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