scholarly journals The Physical Adsorption of Gelatinized Starch with Tannic Acid Decreases the Inhibitory Activity of the Polyphenol against α-Amylase

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1233
Author(s):  
Yueyi Wang ◽  
Shuangshuang Li ◽  
Fangting Bai ◽  
Junwei Cao ◽  
Lijun Sun
Keyword(s):  
Enzyme Inhibition ◽  
Tannic Acid ◽  
Inhibitory Activity ◽  
Adsorption Property ◽  
Physical Adsorption ◽  
Enzyme Active Site ◽  
Opposite Trend ◽  
Gelatinized Starch ◽  
The Difference

The effects of mixing orders of tannic acid (TA), starch, and α-amylase on the enzyme inhibition of TA were studied, including mixing TA with α-amylase before starch addition (order 1), mixing TA with pre-gelatinized starch before α-amylase addition (order 2) and co-gelatinizing TA with starch before α-amylase addition (order 3). It was found that the enzyme inhibition was always highest for order 1 because TA could bind with the enzyme active site thoroughly before digestion occurred. Both order 2 and 3 reduced α-amylase inhibition through decreasing binding of TA with the enzyme, which resulted from the non-covalent physical adsorption of TA with gelatinized starch. Interestingly, at low TA concentration, α-amylase inhibition for order 2 was higher than order 3, while at high TA concentration, the inhibition was shown with the opposite trend, which arose from the difference in the adsorption property between the pre-gelatinized and co-gelatinized starch at the corresponding TA concentrations. Moreover, both the crystalline structures and apparent morphology of starch were not significantly altered by TA addition for order 2 and 3. Conclusively, although a polyphenol has an acceptable inhibitory activity in vitro, the actual effect may not reach the expected one when taking processing procedures into account.

scholarly journals The Physical Adsorption of Gelatinized Starch With Tannic Acid Decreases the Inhibitory Activity of the Polyphenol Against α-Amylase

2021 ◽  
Author(s):  
Yueyi Wang ◽  
Fangting Bai ◽  
Junwei Cao ◽  
Lijun Sun
Keyword(s):  
Enzyme Inhibition ◽  
Tannic Acid ◽  
Inhibitory Activity ◽  
Adsorption Property ◽  
Physical Adsorption ◽  
Alpha Amylase ◽  
Enzyme Active Site ◽  
Gelatinized Starch ◽  
The Difference

The effects of mixing orders of tannic acid (TA), starch and α-amylase on the enzyme inhibition of TA were studied, including mixing TA with α-amylase before starch addition (order 1), mixing TA with pre-gelatinized starch before α-amylase addition (order 2) and co-gelatinizing TA with starch before α-amylase addition (order 3). It was found that the enzyme inhibition was always highest for order 1 because TA could bind with the enzyme active site thoroughly before digestion occurred. Both order 2 and 3 reduced α-amylase inhibition through decreasing binding of TA with the enzyme, which resulted from the non-covalent physical adsorption of TA with gelatinized starch. Interestingly, at low TA concentration, α-amylase inhibition for order 2 was higher than order 3, while at high TA concentration, the inhibition was shown with opposite trend, which arose from the difference in the adsorption property between the pre-gelatinized and co-gelatinized starch at the corresponding TA concentrations. Besides, both the crystalline structures and apparent morphology of starch were not significantly altered by TA addition for order 2 and 3. Conclusively, although a polyphenol may have an acceptable inhibitory activity in vitro, the actual effect may not reach the expected one when taking processing procedures into account.

Gallotannins and Tannic Acid: First Chemical Syntheses and In Vitro Inhibitory Activity on Alzheimer’s Amyloid β-Peptide Aggregation

2015 ◽  
Vol 54 (28) ◽  
pp. 8217-8221 ◽  
Author(s):  
Tahiri Sylla ◽  
Laurent Pouységu ◽  
Grégory Da Costa ◽  
Denis Deffieux ◽  
Jean-Pierre Monti ◽  
...  
Keyword(s):  
Tannic Acid ◽  
Inhibitory Activity ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation

Synthesis, Molecular Docking and α-Glucosidase Inhibitory Activity Study of 2,4,6-triaryl Pyrimidine Derivatives

2020 ◽  
Vol 17 (10) ◽  
pp. 1216-1226
Author(s):  
Mohammed Hussen Bule ◽  
Roghaieh Esfandyari ◽  
Tadesse Bekele Tafesse ◽  
Mohsen Amini ◽  
Mohammad Ali Faramarzi ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Docking ◽  
Inhibitory Activity ◽  
Abdominal Distension ◽  
Spectroscopic Techniques ◽  
Pyrimidine Derivatives ◽  
Molecular Docking Study ◽  
Enzyme Active Site ◽  
Glucosidase Inhibitors

Background: α-Glucosidase inhibitors hinder the carbohydrate digestion and play an important role in the treatment of diabetes mellitus. α-glucosidase inhibitors available on the market are acarbose, miglitol, and voglibose. However, the use of acarbose is diminishing due to related side effects like diarrhea, bloating and abdominal distension. Objectives: This study aimed to synthesize 2,4,6-triaryl pyrimidines derivatives, screen their α- glucosidase inhibitory activity, perform kinetic and molecular docking studies. Methods: A series of 2,4,6-triaryl pyrimidine derivatives were synthesized and their α-glucosidase inhibitory activity was screened in vitro. Pyrimidine derivatives 4a-m were synthesized via a twostep reaction with a yield between 49 and 93%. The structure of the synthesized compounds was confirmed by different spectroscopic techniques (IR, NMR and MS). The in vitro α-glucosidase inhibition activities of the synthesized compounds 4a-m was also evaluated against Saccharomyces cerevisiae α-glucosidase. Results and Discussion: The majority of synthesized compounds had α-glucosidase inhibitory activity. Particularly compounds 4b and 4g were the most active compounds with an IC50 value of 125.2± 7.2 and 139.8 ± 8.1 μM respectively. The kinetic study performed for the most active compound 4b revealed that the compound was a competitive inhibitor of Saccharomyces cerevisiae α-glucosidase with Ki of 122 μM. The molecular docking study also revealed that the two compounds have important binding interactions with the enzyme active site. Conclusion: 2,4,6-triarylpyrimidine derivative 4a-m were synthesized and screened for α- glucosidase inhibitory activity. Most of the synthesized compounds possess α-glucosidase inhibitory activity, and compound 4b demonstrated the most significant inhibitory action as compared to acarbose.

ENZYME INHIBITION BY DERIVATIVES OF PHENOTHIAZINE AND OF SULPHANILAMIDE

1940 ◽  
Vol 18b (11) ◽  
pp. 345-350 ◽  
Author(s):  
H. B. Collier
Keyword(s):  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Enzyme Inhibition ◽  
Ascaris Lumbricoides ◽  
Inhibitory Activity ◽  
Spectroscopic Observation ◽  
Hydroxyl Group ◽  
Bactericidal Action ◽  
Derivatives Of

Mammalian catalase and cytochrome oxidase are strongly inhibited by the hydroxy derivatives of phenothiazine and by p-hydroxylaminobenzenesulphonamide. Phenothiazine, sulphanilamide, and sulphapyridine have little or no effect. Cytochrome-c is irreversibly reduced by the hydroxy-sulphanilamide, as indicated by spectroscopic observation. The inhibitory activity apparently depends on the presence of the hydroxyl group. The relation of these findings to the vermicidal and bactericidal action of the compounds is discussed.Phenothiazine and thionol have no effect on Ascaris lumbricoides in vitro.

Gallotannins and Tannic Acid: First Chemical Syntheses and In Vitro Inhibitory Activity on Alzheimer’s Amyloid β-Peptide Aggregation

2015 ◽  
Vol 127 (28) ◽  
pp. 8335-8339 ◽  
Author(s):  
Tahiri Sylla ◽  
Laurent Pouységu ◽  
Grégory Da Costa ◽  
Denis Deffieux ◽  
Jean-Pierre Monti ◽  
...  
Keyword(s):  
Tannic Acid ◽  
Inhibitory Activity ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Peptide Aggregation

scholarly journals Studies on the inhibition of ferrochelatase by N-alkylated dicarboxylic porphyrins. Steric factors involved and evidence that the inhibition is reversible

1985 ◽  
Vol 226 (2) ◽  
pp. 537-544 ◽  
Author(s):  
F De Matteis ◽  
A H Gibbs ◽  
C Harvey
Keyword(s):  
Enzyme Inhibition ◽  
Active Site ◽  
Inhibitory Activity ◽  
Alkyl Group ◽  
Structural Requirements ◽  
Prolonged Incubation ◽  
Enzyme Active Site ◽  
Steric Factors ◽  
Haem Oxygenase ◽  
Pyrrole Nitrogen

The structural requirements for the inhibition of ferrochelatase by N-alkylated porphyrins were investigated and experiments carried out to explore the mechanism of enzyme inhibition. Three dicarboxylic porphyrins, all substrates of the enzyme, are strongly inhibitory when N-alkylated; in contrast, uroporphyrin and coproporphyrin (which are not substrates) do not inhibit after N-alkylation. Free carboxylic acid functions are required for inhibition, as the methyl ester derivatives are not themselves inhibitory. Porphyrins bearing the alkyl group on the pyrrole nitrogen of rings C and D are less effective inhibitors, particularly when zinc is chelated in the centre of the tetrapyrrole or the N-alkyl group is relatively large in size. The substituents at the 2- and 4-positions of the porphyrin system may also affect the inhibitory activity, particularly for the isomers with ring C and D alkylated. The zinc chelates of several N-alkylprotoporphyrins are inhibitory towards haem oxygenase, another haem-binding enzyme, and also in this case increasing the size of the alkyl group decreased the inhibitory activity, particularly for isomers with ring C or D alkylated. The inhibition could be reversed by prolonged incubation with excess porphyrin substrate, but dealkylation of the N-alkylporphyrin during enzyme inhibition could not be demonstrated. It is concluded (a) that N-alkylated dicarboxylic porphyrins compete reversibly with the porphyrin substrate for the enzyme active site and (b) that the structural and steric factors discussed above affect the inhibitory activity by modifying the affinity of the N-alkylporphyrin inhibitor for the enzyme.

Strategies for the isolation and identification of trypanocidal compounds from the Rutales

2001 ◽  
Vol 73 (3) ◽  
pp. 617-622 ◽  
Author(s):  
Paulo C. Vieira ◽  
Jair Mafezoli ◽  
Mônica T. Pupo ◽  
João B. Fernandes ◽  
M. Fátima das G. F. da Silva ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
3D Structure ◽  
Glycolytic Enzyme ◽  
Significant Activity ◽  
Isolation And Identification ◽  
X Ray ◽  
Enzyme Active Site ◽  
X Ray Crystallography ◽  
Trypomastigote Form

Crude extracts of Rutales species were tested in vitro against the trypomastigote form of Trypanosoma cruzi at 4 mg/mL, and 20% of them showed significant activity (80%). Their inhibitory activity against the glycolytic enzyme GAPDH from T. cruzi has also been evaluated at the concentrations of 100 and 200 mg/mL. Additionally, the inhibitory activity of 13 purified coumarins were also assayed against T. cruzi-GAPDH. Chalepin was the most active substance with IC50 = 64 mM. The 3D structure of the complex chalepin-enzyme was elucidated by X-ray crystallography, revealing the architecture of the interactions between the inhibitor and the enzyme active site.

Enzyme inhibitory assessment of the isolated constituents from Plantago holosteum Scop.

2020 ◽  
Vol 75 (3-4) ◽  
pp. 121-128
Author(s):  
F. Tugce Guragac Dereli ◽  
Yasin Genc ◽  
Iclal Saracoglu ◽  
Esra Kupeli Akkol
Keyword(s):  
Experimental Data ◽  
Enzyme Inhibition ◽  
Aqueous Extract ◽  
Inhibitory Activity ◽  
Folk Medicine ◽  
Inhibition Test ◽  
Phenylethanoid Glycosides ◽  
First Report ◽  
Aerial Parts

AbstractPlants of the Plantago genus are widely used in Turkish folk medicine especially for the treatment of wound, abscess, and inflammation. The aqueous extract and five phenylethanoid glycosides acteoside (1), arenarioside (2), echinacoside (3), isoacteoside (4), and leucosceptoside A (5) isolated from the aerial parts and roots of Plantago holosteum Scop. (Plantaginaceae) were tested for their possible inhibitory activity against hyaluronidase, elastase, and collagenase, related to wound pathogenesis. Even though the aqueous extract prepared from the aerial parts (36.26%) and roots (47.01%) and the isolated compounds acteoside (29.13%), echinacoside (28.73%), and isoacteoside (31.69%) exerted a notable inhibition, arenarioside and leucosceptoside A were found inactive in the hyaluronidase enzyme inhibition test. Similar results were obtained from the collagenase enzyme inhibition test. The aqueous extract prepared from the aerial parts (31.09%) and roots (35.17%), echinacoside (25.13%), and isoacteoside (23.85%) exerted a notable inhibition in this test. However, none of the extracts and isolated compounds displayed elastase enzyme inhibitory activity. The experimental data demonstrated that P. holosteum displayed a remarkable enzyme inhibitory activity against hyaluronidase and collagenase. This paper is the first report regarding the in vitro enzyme inhibitory activity of P. holosteum.

Inhibitory effects of bioaccessible anthocyanins and procyanidins from apple, red grape, cinnamon on α-amylase, α-glucosidase and lipase

2020 ◽  
pp. 1-9
Author(s):  
Pınar Ercan ◽  
Sedef Nehir El
Keyword(s):  
Inhibitory Activity ◽  
Digestive Enzymes ◽  
Positive Control ◽  
Anthocyanin Content ◽  
Inhibitory Effects ◽  
Total Anthocyanin ◽  
Total Anthocyanin Content ◽  
Before And After ◽  
Red Grape

Abstract. The goals of this study were to determine and evaluate the bioaccessibility of total anthocyanin and procyanidin in apple (Amasya, Malus communis), red grape (Papazkarası, Vitis vinifera) and cinnamon (Cassia, Cinnamomum) using an in vitro static digestion system based on human gastrointestinal physiologically relevant conditions. Also, in vitro inhibitory effects of these foods on lipid (lipase) and carbohydrate digestive enzymes (α-amylase and α-glucosidase) were performed with before and after digested samples using acarbose and methylumbelliferyl oleate (4MUO) as the positive control. While the highest total anthocyanin content was found in red grape (164 ± 2.51 mg/100 g), the highest procyanidin content was found in cinnamon (6432 ± 177.31 mg/100 g) (p < 0.05). The anthocyanin bioaccessibilities were found as 10.2 ± 1%, 8.23 ± 0.64%, and 8.73 ± 0.70% in apple, red grape, and cinnamon, respectively. The procyanidin bioaccessibilities of apple, red grape, and cinnamon were found as 17.57 ± 0.71%, 14.08 ± 0.74% and 18.75 ± 1.49%, respectively. The analyzed apple, red grape and cinnamon showed the inhibitory activity against α-glucosidase (IC50 544 ± 21.94, 445 ± 15.67, 1592 ± 17.58 μg/mL, respectively), α-amylase (IC50 38.4 ± 7.26, 56.1 ± 3.60, 3.54 ± 0.86 μg/mL, respectively), and lipase (IC50 52.7 ± 2.05, 581 ± 54.14, 49.6 ± 2.72 μg/mL), respectively. According to our results apple, red grape and cinnamon have potential to inhibit of lipase, α-amylase and α-glucosidase digestive enzymes.

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