Comparative studies on ACE inhibition, degree of hydrolysis, antioxidant property and phenolic acid composition of hydrolysates derived from simulated in vitro gastrointestinal proteolysis of three thermally treated legumes

2019 ◽  
Vol 281 ◽  
pp. 154-162 ◽  
Author(s):  
Yan Zhang ◽  
Sam K.C. Chang
Keyword(s):  
Acid Composition ◽  
Phenolic Acid ◽  
Comparative Studies ◽  
Ace Inhibition ◽  
Antioxidant Property ◽  
Degree Of Hydrolysis ◽  
Thermally Treated

scholarly journals Discovery of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Todarodes pacificus and Their Inhibitory Mechanism: In Silico and In Vitro Studies

2019 ◽  
Vol 20 (17) ◽  
pp. 4159 ◽  
Author(s):  
Dingyi Yu ◽  
Cong Wang ◽  
Yufeng Song ◽  
Junxiang Zhu ◽  
Xiaojun Zhang
Keyword(s):  
Angiotensin Converting Enzyme ◽  
In Silico ◽  
Ace Inhibition ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Todarodes Pacificus ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

In order to rapidly and efficiently excavate antihypertensive ingredients in Todarodes pacificus, its myosin heavy chain was hydrolyzed in silico and the angiotensin-converting enzyme (ACE) inhibitory peptides were predicted using integrated bioinformatics tools. The results showed the degree of hydrolysis (DH) theoretically achieved 56.8% when digested with papain, ficin, and prolyl endopeptidase (PREP), producing 126 ACE inhibitory peptides. By predicting the toxicity, allergenicity, gastrointestinal stability, and intestinal epithelial permeability, 30 peptides were finally screened, of which 21 had been reported and 9 were new. Moreover, the newly discovered peptides were synthesized to evaluate their in vitro ACE inhibition, showing Ile-Ile-Tyr and Asn-Pro-Pro-Lys had strong effects with a pIC50 of 4.58 and 4.41, respectively. Further, their interaction mechanisms and bonding configurations with ACE were explored by molecular simulation. The preferred conformation of Ile-Ile-Tyr and Asn-Pro-Pro-Lys located in ACE were successfully predicted using the appropriate docking parameters. The molecular dynamics (MD) result indicated that they bound tightly to the active site of ACE by means of coordination with Zn(II) and hydrogen bonding and hydrophobic interaction with the residues in the pockets of S1 and S2, resulting in stable complexes. In summary, this work proposed a strategy for screening and identifying antihypertensive peptides from Todarodes pacificus.

scholarly journals Blood Pressure Regulating and Antioxidant Potentials of Theobroma Cacao Pod Husk Protein Hydrolysates

2021 ◽  
Vol 9 (1) ◽  
pp. 26-36
Author(s):  
Rotimi Arise ◽  
Samuel Tobi Farohunbi ◽  
Halimat Olanike Ayilara
Keyword(s):  
Theobroma Cacao ◽  
Antioxidant Properties ◽  
Ace Inhibition ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Antioxidant Power ◽  
Significant Difference ◽  
Cocoa Pod Husk ◽  
Cocoa Pod Husks

Background: Agrowastes like Theobroma cacao (Cocoa) pod husk can be used to prepare bioactive peptides with various bio-functionalities. Objectives: This study aimed to investigate antioxidant and angiotensin converting enzyme I (ACE) inhibitory peptides contained in Theobroma cacao (cocoa) pod husks – an agro-waste. Methods: Protein isolated from cocoa pod husk was enzymatically digested with alcalase, pepsin, and trypsin. ACE inhibition, kinetics of ACE inhibition, and antioxidant properties of the cocoa pod husks hydrolysates were evaluated in vitro. Results: Trypsin and alcalase hydrolysates displayed higher peptide yields (63.1% and 61.2%) than pepsin hydrolysate (61.2%). However, no significant difference (P>0.05) was observed in the degree of hydrolysis (DH) of the three proteases on cocoa pod husk protein. Methionine, lysine, and cysteine were the amino acid residues presented in cocoa pod husk hydrolysates. A concentration-dependent ACE inhibition by cocoa pod husk hydrolysates was observed. The highest ACE inhibitions of 84.4%, 81.5%, and 73.5% were obtained at 2.0 mg/mL of pepsin, trypsin, and alcalase hydrolysates, respectively, with the minimum IC50 value of 0.36 mg/mL obtained for trypsin hydrolysate. An uncompetitive and mixed-type inhibition was obtained from double reciprocal plots of alcalase and pepsin as well as trypsin cocoa pod husk protein hydrolysates. The Ki values of ACE inhibition for pepsin, trypsin, and alcalase hydrolysates were 3.05, 2.19, and 3.57 mg/mL, respectively. A concentration-dependent increase in the scavenging of 2,2-diphenyl-1-picrylhydrazyl and superoxide radicals as well as ferric reducing antioxidant power were recorded for the cocoa pod husk hydrolysates. Conclusion: Trypsin and alcalase cocoa pod husk protein hydrolysates could be an effective source of a natural ACE inhibitor and antioxidant.

COMPARATIVE STUDIES OF THE POTENTIATION OF CORTICOTROPHIN ACTIVITY BY SEVERAL INACTIVE DERIVATIVES

1963 ◽  
Vol 42 (2) ◽  
pp. 209-213 ◽  
Author(s):  
Arthur I. Cohen ◽  
Edward H. Frieden
Keyword(s):  
Biological Activity ◽  
Comparative Studies ◽  
Free Amino ◽  
Hormonal Activity ◽  
Amino Groups

ABSTRACT A number of corticotrophin analogues have been prepared, some of which potentiate the biological activity of the untreated hormone in vitro. The free amino groups of corticotrophin appear to be essential not only for hormonal activity, but also for the interaction of the analogues with the tissue corticotrophin inactivating system which is assumed to account for the potentiating effect.

COMPARATIVE STUDIES OF MICRO-ULTRASTRUCTURE AND FATTY ACID COMPOSITION OF NORMAL AND ALBINO HEPATOPANCREAS OF CHINESE MITTEN

2009 ◽  
Vol 32 (5) ◽  
pp. 687-693 ◽  
Author(s):  
Guo-Liang CHANG ◽  
Yong-Xu CHENG ◽  
Xu-Gan WU ◽  
Xiao-Zhen YANG ◽  
Zong-Kai WANG ◽  
...  
Keyword(s):  
Fatty Acid Composition ◽  
Fatty Acid ◽  
Acid Composition ◽  
Comparative Studies

Extraction, Chemical Composition, Antioxidant Property and In vitro Anticancer Activity of Silymarin from Silybum Marianum On Kb and A549 Cell Lines

2020 ◽  
Vol 17 ◽  
Author(s):  
Mojgan Azadpour ◽  
Mohammad Mehdi Farajollahi ◽  
Ali Mohammad Varzi ◽  
Pejman Hashemzadeh ◽  
Hossein Mahmoudvand ◽  
...  
Keyword(s):  
Anticancer Activity ◽  
Cell Lines ◽  
A549 Cell ◽  
Hplc Analysis ◽  
Antioxidant Properties ◽  
Radical Scavenging ◽  
Antioxidant Property ◽  
Silybum Marianum ◽  
Stable Free Radical

Introduction: This study aimed to evaluate the antioxidant property of silymarin (SM) extracted from the seed of Silybum marianum and its anticancer activity on KB and A549 cell lines following 24, 48, and 72 h of treatment. Methods: Ten grams of powdered S. marianum seeds were defatted using n-hexane for 6 hours and then extracted by methanol. The silymarin extracted of extraction components The extracted components of silymarin were measured by spectrophotometric assay and HPLC analysis. 2, 2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging, phenol content, total flavonoid content, and total antioxidant capacity were measured to detect the antioxidant properties of SM. The anticancer activity of the SM on cell lines evaluated by MTT. Results: In HPLC analysis, more than 50% of the peaks were related to silibin A and B. SM was reducedDPPH (the stable free radical) with a 50% inhibitory concentration (IC50) of 6.56 μg/ ml in comparison with butylated hydroxyl toluene (BHT), which indicated an IC50 of ~3.9 μg/ ml.The cytotoxicity effect of SM on the cell lines was studied by MTT assay. The cytotoxicity effect of the extracted silymarin on KB and A549 cell lines was observed up to 80 and 70% at 156 and 78 µg/ml, respectively. The IC50 value of the extracted SM on KB and A549 cell lines after 24 hours of treatment was seen at 555 and 511 µg/ml, respectively. Conclusion: Due to the good antioxidant and anticancer properties of the isolated silymarin, its use as an anticancer drug is suggested.

scholarly journals Muscle Protein Hydrolysates and Amino Acid Composition in Fish

Marine Drugs ◽  
2021 ◽  
Vol 19 (7) ◽  
pp. 377
Author(s):  
Bomi Ryu ◽  
Kyung-Hoon Shin ◽  
Se-Kwon Kim
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Muscle Protein ◽  
Fish Muscle ◽  
Amino Acid Profile ◽  
Industrial Applications ◽  
Protein Hydrolysates ◽  
Added Value ◽  
Degree Of Hydrolysis

Fish muscle, which accounts for 15%–25% of the total protein in fish, is a desirable protein source. Their hydrolysate is in high demand nutritionally as a functional food and thus has high potential added value. The hydrolysate contains physiologically active amino acids and various essential nutrients, the contents of which depend on the source of protein, protease, hydrolysis method, hydrolysis conditions, and degree of hydrolysis. Therefore, it can be utilized for various industrial applications including use in nutraceuticals and pharmaceuticals to help improve the health of humans. This review discusses muscle protein hydrolysates generated from the muscles of various fish species, as well as their amino acid composition, and highlights their functional properties and bioactivity. In addition, the role of the amino acid profile in regulating the biological and physiological activities, nutrition, and bitter taste of hydrolysates is discussed.

Physicochemical characteristics, ATR-FTIR molecular interactions and in vitro starch and protein digestion of thermally-treated whole pulse flours

2018 ◽  
Vol 105 ◽  
pp. 371-383 ◽  
Author(s):  
Carolina Estefanía Chávez-Murillo ◽  
Jorge Ivan Veyna-Torres ◽  
Luisa María Cavazos-Tamez ◽  
Julián de la Rosa-Millán ◽  
Sergio Othon Serna-Saldívar
Keyword(s):  
Molecular Interactions ◽  
Physicochemical Characteristics ◽  
Protein Digestion ◽  
Thermally Treated

scholarly journals Bacterial Cellulose Membrane Containing Epilobium angustifolium L. Extract as a Promising Material for the Topical Delivery of Antioxidants to the Skin

2021 ◽  
Vol 22 (12) ◽  
pp. 6269
Author(s):  
Anna Nowak ◽  
Paula Ossowicz-Rupniewska ◽  
Rafał Rakoczy ◽  
Maciej Konopacki ◽  
Magdalena Perużyńska ◽  
...  
Keyword(s):  
Bacterial Cellulose ◽  
Topical Application ◽  
Phenolic Acid ◽  
Antioxidant Properties ◽  
Ethanolic Extract ◽  
Cellulose Membrane ◽  
Hydroxybenzoic Acid ◽  
Epilobium Angustifolium ◽  
Bacterial Cellulose Membrane

Bacterial cellulose membranes (BCs) are becoming useful as a drug delivery system to the skin. However, there are very few reports on their application of plant substances to the skin. Komagataeibacter xylinus was used for the production of bacterial cellulose (BC). The BC containing 5% and 10% ethanolic extract of Epilobium angustifolium (FEE) (BC-5%FEE and BC-10%FEE, respectively) were prepared. Their mechanical, structural, and antioxidant properties, as well as phenolic acid content, were evaluated. The bioavailability of BC-FESs using mouse L929 fibroblasts as model cells was tested. Moreover, in vitro penetration through the pigskin of the selected phenolic acids contained in FEE and their accumulation in the skin after topical application of BC-FEEs was examined. The BC-FEEs were characterized by antioxidant activity. The BC-5% FEE showed relatively low toxicity to healthy mouse fibroblasts. Gallic acid (GA), chlorogenic acid (ChA), 3,4-dihydroxybenzoic acid (3,4-DHB), 4-hydroxybenzoic acid (4-HB), 3-hydroxybenzoic acid (3-HB), and caffeic acid (CA) found in FEE were also identified in the membranes. After topical application of the membranes to the pigskin penetration of some phenolic acid and other antioxidants through the skin as well as their accumulation in the skin was observed. The bacterial cellulose membrane loaded by plant extract may be an interesting solution for topical antioxidant delivery to the skin.

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