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 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.

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.

scholarly journals Angiotensin I-converting Enzyme (ACE) Inhibitory Activity and Chemical Composition of Alchemilla Viridiflora Rothm.

2021 ◽  
Author(s):  
Jelena Radović ◽  
Relja Suručić ◽  
Marjan Niketić ◽  
Tatjana Kundakovic-Vasovic
Keyword(s):  
Inhibitory Activity ◽  
Methanol Extract ◽  
Flavonoid Glycosides ◽  
Herbaceous Plant ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Abstract Alchemilla viridiflora Rothm., Rosaceae is a herbaceous plant widespread in central Greece, Bulgaria, North Macedonia and Serbia with Kosovo. LC-MS analysis leads to the identification of 20 compounds in methanol extract, mainly ellagitannins and flavonoid glycosides. Considering that different plant extracts were traditionally used for treatment of hypertension and that some of the analyzed methanol extract constituents possess beneficial cardiovascular effects, we hypothesized that some of these effects are achieved through inhibition of angiotensin I-converting enzyme (ACE). The dose-dependent activities ACE inhibitory activity of A. viridiflora and miquelianin were observed with an IC50 of 2.51 ± 0.00 µg/ml of A. viridiflora compared to IC50 of 2.59 ± 0.00 µg/mL for miquelianin. Contribution of the single compounds to the tested activity was further analyzed through the in silico experimental approach. Computational docking results showed that tiliroside, ellagic acid pentose and galloyl-HHDP-glucose exhibited even better binding affinity for ACE active site than miquelianin, which ACE activity was confirmed by an in vitro assay.

Angiotensin I Converting Enzyme–Inhibitory Activity of Bovine, Ovine, and Caprine κ-Casein Macropeptides and Their Tryptic Hydrolysates

2003 ◽  
Vol 66 (9) ◽  
pp. 1686-1692 ◽  
Author(s):  
M. A. MANSO ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Gastrointestinal Conditions ◽  
Tryptic Hydrolysate ◽  
Inhibitory Activities ◽  
Ace Inhibitory

This work evaluated the angiotensin-converting enzyme (ACE)–inhibitory activities of bovine, ovine, and caprine κ-casein macropeptides (CMPs) and their tryptic hydrolysates. The results obtained indicate that bovine, ovine, and caprine CMPs exhibited moderate in vitro ACE-inhibitory activities that increased considerably after digestion under simulated gastrointestinal conditions. Active peptides could also be produced from CMPs via proteolysis with trypsin, with tryptic hydrolysates exhibiting a more extensive ACE-inhibitory activity than intact CMPs during simulated gastrointestinal digestion. Two active fractions were chromatographically separated from the tryptic hydrolysate of the bovine CMP, but their complexity hampered the assignment of the ACE-inhibitory activity to specific peptide sequences. Evidence for the release of the strong ACE-inhibitory tripeptide IPP was found upon simulation of the gastrointestinal digestion of peptides released by trypsin from the CMP sequence. These findings might help to promote further exploitation of cheese whey in the preparation of nutraceuticals for inclusion in the composition of functional food products with high added values.

scholarly journals Effects of Various Drying Methods on Some Physico-Chemical Properties and the Antioxidant Profile and ACE Inhibition Activity of Oyster Mushrooms (Pleurotus Ostreatus)

Foods ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 160 ◽  
Author(s):  
Sergey Piskov ◽  
Lyudmila Timchenko ◽  
Wolf-Dieter Grimm ◽  
Igor Rzhepakovsky ◽  
Svetlana Avanesyan ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Pleurotus Ostreatus ◽  
Microwave Drying ◽  
Drying Methods ◽  
The Sun ◽  
Ace Inhibitory Activity ◽  
Peptide Profile ◽  
Hot Air ◽  
Ace Inhibitory

In food biotechnology, Pleurotus ostreatus is of great interest as a source of natural antioxidants and angiotensin-converting enzyme (ACE) inhibitors. However, research in this area has not yet been completed. The effect of various drying methods on the structural properties and the rehydration capacity of mushrooms was investigated in this paper. The content of secondary metabolites, the peptide profile, and the antioxidative effect and ACE inhibitory activity of dry mushrooms were investigated in vitro, simulating the process of gastrointestinal digestion. X-ray microtomography has confirmed that structure of lyophilic and sun-dried mushrooms is dominated by open pores, and in mushrooms dried with hot air and microwave, closed pores. Experiments have shown that the conditions of freeze drying and sun drying of Pleurotus ostreatus provide a higher rehydration capacity of dried mushrooms. The maximum activity of radical absorption of the oyster mushroom after microwave drying was observed. The iron restoring capacity of the mushrooms is maximally maintained with microwave drying and hot-air drying. The properties of the antioxidant product with an emphasis on the high activity of inhibiting lipid oxidation of the mushroom maximized after drying in the sun. Mushrooms dried lyophilically and in the sun showed the highest ACE inhibitory activity.

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