Some indazoles as alternative inhibitors for potato polyphenol oxidase

Öztürk, Cansu; Bayrak, Songül; Demir, Yeliz; Aksoy, Mine; Alım, Zuhal; Özdemir, Haşan; Küfrevioğlu, Ömer İrfan

doi:10.1002/bab.2283

Cited by 10 publications

(7 citation statements)

References 55 publications

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“…The affinity chromatography technique is highly preferred, because it enables the enzyme purification process to be completed quickly, and separates numerous biological materials that cannot be separated in a single step. 40 In our previous research, hydrazine was synthesized based on the methyl benzoate form. 37,39 However, the synthesis of hydroxamates was not performed.…”

Section: Synthesis Of Affinity Gels and Ft-ir Resultsmentioning

confidence: 99%

Development of a new affinity chromatography method for purification of horseradish peroxidase enzyme

Gerni,

Özdemir

2023

Biotech and App Biochem

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In this study, benzohydroxamic acid molecules were synthesized from methyl 4‐amino‐2‐methoxy, methyl 4‐amino‐3‐nitro, methyl 4‐amino‐3‐methyl, and methyl 4‐amino‐3‐chloro benzoate molecules, and the horseradish peroxidase (HRP) enzyme was purified in one step using the affinity chromatography technique for the first time. The IC50 and Ki values for the 4‐amino 3‐methyl benzohydroxamic acid molecule were 0.136 and 0.132 ± 0.054 μM, respectively, while the IC50 and Ki values for the 4‐amino‐3‐nitro benzohydroxamic acid molecule were 56.00 and 51.90 ± 9.90 μM, respectively. It was found that the IC50 and Ki values for the 4‐amino‐3‐chloro benzohydroxamic acid molecule were 218.33 and 175.67 ± 43.78 μM, respectively, whereas the IC50 and Ki values for the 4‐amino‐2‐methoxy benzohydroxamic acid molecule were 306.00 and 218.00 ± 68.80 μM, respectively. The HRP enzyme was synthesized from 4‐amino‐2‐methoxy hydroxamic acid column with a 35.97% yield 601.13 times, 4‐amino‐3‐nitro hydroxamic acid column, with a 14.00% yield 404.11 times, 4‐amino‐3‐methyl hydroxamic acid column with an 8.70% yield 394.88 times, and 4‐amino‐3‐chloro hydroxamic acid column with a 4.48% yield 284.85 times. Thus, the HRP enzyme was purified in a single step with hydroxamic acids, and its molecular weight was found to be 44 kDa. The optimum pH was 8.0, the optimum temperature was 15°C, and the optimum ionic strength was 0.4 M for the purified HRP enzyme.

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Section: Synthesis Of Affinity Gels and Ft-ir Resultsmentioning

confidence: 99%

Development of a new affinity chromatography method for purification of horseradish peroxidase enzyme

Gerni,

Özdemir

2023

Biotech and App Biochem

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“…Due to the negative side effects of synthetic drugs, the importance of medicinal plants is increasing day by day. Plant-derived inhibitors are being studied because of the significant enzyme inhibition potential of compounds isolated from plants (Bayrak et al, 2020;Öztürk et al, 2022). The activity of enzymes related to Alzheimer's Anticholinesterase activities of G. tuberosum extracts were calculated by their inhibitory capacity on AChE and BChE enzymes as mentioned.…”

Section: Resultsmentioning

confidence: 99%

Geranium tuberosum Metanol Ekstraktının Enzim İnhibitör Özellikleri ve Antimikrobiyal Aktivitesi

ALMAZ

2023

Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi

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Geranium tuberosum roots are consumed fresh in some areas of the countryside of Turkey. This study was conducted to scientifically validate the traditional use of the species. The enzyme inhibition effect and antimicrobial activity of the root and leaf parts of Geranium tuberosum were investigated using a methanol extract. The leaf extract had higher acetylcholinesterase and butyrylcholinesterase activity than the root extract, while the root extract showed a stronger inhibitory effect on xanthine oxidase enzyme.. Also, the antifungal and antibacterial activities of the extracts were investigated using the hollow agar technique. It was observed that both extracts gave high antimicrobial activity on different bacterial strains. These results confirmed that Geranium tuberosum is a natural antibacterial, and has enzyme inhibitory potential.

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“…Non-competitive inhibition of tyrosinase by indazoles has been described ( Figure S10 ) [ 28 ]. The values described for

are always greater than the IC 50 , and a possible explanation for this could be that the activity measurements are made with catechol, which derives a very unstable o -quinone after its oxidation.…”

Section: Resultsmentioning

confidence: 99%

The Relationship between the IC50 Values and the Apparent Inhibition Constant in the Study of Inhibitors of Tyrosinase Diphenolase Activity Helps Confirm the Mechanism of Inhibition

et al. 2022

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Tyrosinase is the enzyme involved in melanization and is also responsible for the browning of fruits and vegetables. Control of its activity can be carried out using inhibitors, which is interesting in terms of quantitatively understanding the action of these regulators. In the study of the inhibition of the diphenolase activity of tyrosinase, it is intriguing to know the strength and type of inhibition. The strength is indicated by the value of the inhibition constant(s), and the type can be, in a first approximation: competitive, non-competitive, uncompetitive and mixed. In this work, it is proposed to calculate the degree of inhibition (iD), varying the concentration of inhibitor to a fixed concentration of substrate, L-dopa (D). The non-linear regression adjustment of iD with respect to the initial inhibitor concentration [I]0 allows for the calculation of the inhibitor concentration necessary to inhibit the activity by 50%, at a given substrate concentration (IC50), thus avoiding making interpolations between different values of iD. The analytical expression of the IC50, for the different types of inhibition, are related to the apparent inhibition constant (KIapp). Therefore, this parameter can be used: (a) To classify a series of inhibitors of an enzyme by their power. Determining these values at a fixed substrate concentration, the lower IC50, the more potent the inhibitor. (b) Checking an inhibitor for which the type and the inhibition constant have been determined (using the usual methods), must confirm the IC50 value according to the corresponding analytical expression. (c) The type and strength of an inhibitor can be analysed from the study of the variation in iD and IC50 with substrate concentration. The dependence of IC50 on the substrate concentration allows us to distinguish between non-competitive inhibition (iD does not depend on [D]0) and the rest. In the case of competitive inhibition, this dependence of iD on [D]0 leads to an ambiguity between competitive inhibition and type 1 mixed inhibition. This is solved by adjusting the data to the possible equations; in the case of a competitive inhibitor, the calculation of KI1app is carried out from the IC50 expression. The same occurs with uncompetitive inhibition and type 2 mixed inhibition. The representation of iD vs. n, with n=[D]0/KmD, allows us to distinguish between them. A hyperbolic iD vs. n representation that passes through the origin of coordinates is a characteristic of uncompetitive inhibition; the calculation of KI2app is immediate from the IC50 value. In the case of mixed inhibitors, the values of the apparent inhibition constant of meta-tyrosinase (Em) and oxy-tyrosinase (Eox), KI1app and the apparent inhibition constant of metatyrosinase/Dopa complexes (EmD) and oxytyrosinase/Dopa (EoxD), KI2app are obtained from the dependence of iD vs. n, and the results obtained must comply with the IC50 value.

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Some indazoles as alternative inhibitors for potato polyphenol oxidase

Cited by 10 publications

References 55 publications

Development of a new affinity chromatography method for purification of horseradish peroxidase enzyme

Development of a new affinity chromatography method for purification of horseradish peroxidase enzyme

Geranium tuberosum Metanol Ekstraktının Enzim İnhibitör Özellikleri ve Antimikrobiyal Aktivitesi

The Relationship between the IC50 Values and the Apparent Inhibition Constant in the Study of Inhibitors of Tyrosinase Diphenolase Activity Helps Confirm the Mechanism of Inhibition

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