Changes in ACE inhibitory and antioxidant activities in alcalase treated idli batter and idli after fermentation

The present study investigated angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities of barbel muscle protein hydrolysate prepared with Alcalase. The barbel muscle protein hydrolysate displayed a high ACE inhibitory activity (CI50=0.92 mg/mL). The antioxidant activities of protein hydrolysate at different concentrations were evaluated using variousin vitroantioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method and reducing power assay. The barbel muscle protein hydrolysate exhibited an important radical scavenging effect and reducing power. These results obtained byin vitrosystems obviously established the antioxidant potency of barbel hydrolysate to donate electron or hydrogen atom to reduce the free radical. Furthermore, these bioactive substances can be exploited into functional foods or used as source of nutraceuticals.

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ACE-Inhibitory and Antioxidant Activities of Hydrolysates from the By-Products of Hybrid Grouper (Epinephelus Lanceolatus × Epinephelus Fuscoguttatus)

Sains Malaysiana ◽

10.17576/jsm-2020-4902-04 ◽

2020 ◽

Vol 49 (2) ◽

pp. 261-270

Author(s):

Pei-Teng Chan ◽

Patricia Matanjun ◽

Cahyo Budiman ◽

Rossita Shapawi ◽

Jau-Shya Lee

Keyword(s):

Antioxidant Activities ◽

Hybrid Grouper ◽

Epinephelus Fuscoguttatus ◽

By Products ◽

Ace Inhibitory

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Phenolic Profile, Antioxidant Capacities and Enzymatic Inhibitory Activities of Propolis from Different Geographical Areas: Needs for Analytical Harmonization

Antioxidants ◽

10.3390/antiox9010075 ◽

2020 ◽

Vol 9 (1) ◽

pp. 75 ◽

Cited By ~ 14

Author(s):

Sandra M. Osés ◽

Patricia Marcos ◽

Patricia Azofra ◽

Ana de Pablo ◽

Miguel Ángel Fernández-Muíño ◽

...

Keyword(s):

Ferulic Acid ◽

High Performance ◽

Antioxidant Activities ◽

Radical Scavenging ◽

Trolox Equivalent Antioxidant Capacity ◽

Coumaric Acid ◽

Antioxidant Capacities ◽

Functional Product ◽

Inhibitory Activities ◽

Ace Inhibitory

Propolis is a resinous vegetal exudate modified by bees, and is interesting as a preservative and potentially functional product. This work dealt with studying the common phenolic profiles and antioxidant capacities of 13 bee propolis from different geographical areas. Both hyaluronidase and angiotensin converting enzyme (ACE) inhibitory activities were also assessed and related when possible with particular phenolic compounds. High performance liquid chromatography-ultraviolet detection (HPLC-UV) analysis showed that every propolis contained p-coumaric acid (1.2–12.2 mg/g) and ferulic acid (0.3–11.0 mg/g). Pinocembrin, catechin, and caffeic acid phenethyl ester (CAPE) plus galangin were the main flavonoids. Antioxidant activities were higher than 280 µmol trolox/g for trolox equivalent antioxidant capacity (TEAC), 0.099 mmol uric acid/g for radical-scavenging effect on hydroxyl radicals, and 0.19 mg/mL for half maximal inhibitory concentration (IC50) of antioxidant activity against superoxide anion radical. Working with solutions of 10 mg/mL propolis, hyaluronidase inhibitory activity ranged between 0% and 68.20%, being correlated to ferulic acid content. ACE inhibitory effect determined by HPLC was higher than 78%, being correlated with catechin and p-coumaric acid. Therefore, propolis could be useful for food, pharmaceutical, and cosmetic companies, also helping to reduce risk factors for diseases related to oxidative damage, inflammatory processes, and hypertension. This research also highlights the necessity for harmonized analysis methods and the expression of results for propolis.

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ACE Inhibitory and Antioxidant Activities of Collagen Hydrolysates from the Ribbon Jellyfish (Chrysaora sp.)

Food Technology and Biotechnology ◽

10.17113/ftb.52.04.14.3641 ◽

2014 ◽

Vol 52 (4) ◽

pp. 495-504 ◽

Cited By ~ 18

Author(s):

Zoha Barzideh ◽

◽

Aishah Abd Latif ◽

Chee-Yuen Gan ◽

Md. Zainul Abedin ◽

...

Keyword(s):

Antioxidant Activities ◽

Collagen Hydrolysates ◽

Ace Inhibitory

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

Applied Mechanics and Materials ◽

10.4028/www.scientific.net/amm.145.179 ◽

2011 ◽

Vol 145 ◽

pp. 179-183 ◽

Cited By ~ 3

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.

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ACE inhibitory and antioxidant activities of red scorpionfish (Scorpaena notata) protein hydrolysates

Journal of Food Science and Technology ◽

10.1007/s13197-015-1862-8 ◽

2015 ◽

Vol 52 (11) ◽

pp. 7092-7102 ◽

Cited By ~ 8

Author(s):

Neyssene Aissaoui ◽

Ferid Abidi ◽

M. Nejib Marzouki

Keyword(s):

Antioxidant Activities ◽

Protein Hydrolysates ◽

Scorpaena Notata ◽

Ace Inhibitory

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Angiotensin Converting Enzyme Inhibitory and Antioxidant Activities of Enzymatic Hydrolysates of Korean Native Cattle (Hanwoo) Myofibrillar Protein

BioMed Research International ◽

10.1155/2017/5274637 ◽

2017 ◽

Vol 2017 ◽

pp. 1-9 ◽

Cited By ~ 5

Author(s):

Seung Yun Lee ◽

Sun Jin Hur

Keyword(s):

Molecular Weight ◽

Angiotensin Converting Enzyme ◽

Antioxidant Activities ◽

Radical Scavenging ◽

Myofibrillar Protein ◽

Raw 264.7 Cells ◽

Converting Enzyme ◽

Molecular Weights ◽

Native Cattle ◽

Ace Inhibitory

The purpose of this study was to determine the angiotensin converting enzyme (ACE) inhibitory and antioxidant activities of myofibrillar protein hydrolysates (HMPHs) of different molecular weights (<3 and <10 kDa) derived from Korean native cattle (Hanwoo breed) using a commercially available and inexpensive enzyme (Alkaline-AK). HMPH of both tested molecular weights had ACE inhibitory activity. Among the antioxidant activities, iron chelation and nitrite scavenging activities were higher in low-molecular-weight peptide of HMPH (<3 kDa), whereas 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity was higher in high-molecular-weight peptide of HMPH (<10 kDa). HMPH did not induce cytotoxicity in RAW 264.7 cells at concentrations of 5–20 mg/mL. These results indicate that HMPH can be cheaply produced using Alkaline-AK and applied as a potential ACE inhibitor and antioxidant.

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Bioactivity of water soluble extracts and some characteristics of white cheese during the ripening period as effected by packaging type and probiotic adjunct cultures

Journal of Dairy Research ◽

10.1017/s0022029914000703 ◽

2015 ◽

Vol 82 (1) ◽

pp. 47-55 ◽

Cited By ~ 15

Author(s):

Tuba Erkaya ◽

Mustafa Şengul

Keyword(s):

Total Nitrogen ◽

Antioxidant Activities ◽

Bifidobacterium Bifidum ◽

Water Soluble ◽

Soluble Nitrogen ◽

Adjunct Cultures ◽

White Cheese ◽

Vacuum Package ◽

Ace Inhibitory

In this study, the chemical composition, proteolysis and in vitro angiotensin-converting enzyme-(ACE)-inhibitory and antioxidant activities of white cheeses made using probiotic adjunct cultures (Bifidobacterium bifidum DSMZ 20456 and Lactobacillus acidophilus DSMZ 20079) were investigated. The cheeses were ripened in a vacuum package or brine for 120 d at 4 °C. The cheese samples maintained the probiotic characteristics of the viable cells as >106 cfu/g even after ripening for 120 d. The proteolysis degrees in terms of water-soluble nitrogen/total nitrogen (WSN/TN), trichloroacetic acid-soluble nitrogen/total nitrogen (TCA-SN/TN) and phosphotungstic acid-soluble nitrogen/total nitrogen (PTA-SN/TN) values in the cheeses increased throughout the ripening. The highest levels of proteolysis were found in cheese made using Lb. acidophilus DSMZ 20079 and ripened in a vacuum package. ACE-inhibitory activity of the water soluble extracts (WSEs) of the cheeses increased significantly (P < 0·05) throughout the ripening (IC50 values 82·78–140·99 μg/ml). Use of Lb. acidophilus DSMZ 20079 and packaging under vacuum significantly increased the percentage of ACE inhibiting activity. WSEs had DPPH scavenging activity (the IC50 values were 2·41–5·39 mg/ml and the inhibition values were 5·10–10·38%), increasing up to 60 d ripening. In the present study, it was observed that Lb. acidophilus DSMZ 20079 was more effective than Bifido. bifidum DSMZ 20456 in terms of the cheese characteristics investigated.

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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 ◽

10.3390/molecules25225405 ◽

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.

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