Food Additives Benzoic Acid and its Methyl and Propyl Parahydroxy Derivatives Aggregate Proteins

Ramesh, Halavath; Sahari, Noorul Huda; Hossain, Mujahid; Bhuyan, Abani K.

doi:10.1021/acsfoodscitech.1c00347

Cited by 7 publications

(5 citation statements)

References 21 publications

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“…However, there is evidence indicating that proteins can bind benzoate and then the benzoate-bound proteins enter the aggregation pathway to produce amorphous and fibrillar structures. It is important that the concentration of benzoates needed to induce protein aggregation is much lower than the microbicidal and inhibitory concentrations prescribed by the FAO [ 38 ].…”

Section: Discussionmentioning

confidence: 99%

Alternative Enzyme Inhibition Assay for Safety Evaluation of Food Preservatives

Esimbekova

Асанова

Kratasyuk

2023

Life

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While food additives are widely used in the modern food industry and generally are important in maintaining the ability to provide food for the increasing world population, the progress occurring in this field is much ahead of the evaluation of their possible consequences for human health. The present study suggests a set of single- and multi-enzyme assay systems for revealing toxic effects of the most widely spread food preservatives, such as sorbic acid (E200), potassium sorbate (E202), and sodium benzoate (E211) at the primary molecular level of their interaction with enzymes. The assay is based on the inhibition of enzyme activity by toxic substances proportional to the amount of the toxicants in the sample. The single-enzyme assay system based on NAD(P)H:FMN oxidoreductase (Red) proved to be most sensitive to the impact of food additives, with the IC50 values being 29, 14, and 0.02 mg/L for sodium benzoate, potassium sorbate, and sorbic acid, respectively, which is considerably lower than their acceptable daily intake (ADI). No reliable change in the degree of inhibition of the enzyme assay systems by food preservatives was observed upon elongating the series of coupled redox reactions. However, the inhibition of activity of the multi-enzyme systems by 50% was found at a preservative concentration below the maximum permissible level for food. The inhibition effect of food preservatives on the activity of butyrylcholinesterase (BChE), lactate dehydrogenase (LDH), and alcohol dehydrogenase (ADH) was either absent or found in the presence of food preservatives at concentrations significantly exceeding their ADI. Among the preservatives under study, sodium benzoate is considered to be the safest in terms of the inhibiting effect on the enzyme activity. The results show that the negative effect of the food preservatives at the molecular level of organization of living things is highly pronounced, while at the organismal level it may not be obvious.

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Section: Discussionmentioning

confidence: 99%

Alternative Enzyme Inhibition Assay for Safety Evaluation of Food Preservatives

Esimbekova

Асанова

Kratasyuk

2023

Life

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“…While studying aspects of food preservative binding to globular proteins, we found in 2021 that the benzoate class of food additives perturbs the native states of lysozyme, cytochrome c, and myoglobin and transforms the protein population to a mixture of amorphous and amyloid fibrillar aggregates, presumably via denatured or quasi-native states . A study soon after showed that benzoates induce amyloid fibrillation of an intrinsically disordered protein (IDP) as well, raising concerns about the safety and use of synthetic food additives.…”

Section: Introductionmentioning

confidence: 99%

Food Colorants Acid Yellow 23, Azorubine, and Acid Red 18 Cause Aggregation and Fibrillation of Proteins

Ramesh,

Bhuyan

2024

ACS Food Sci. Technol.

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Acid Yellow 23 (AY23), Azorubine (AR), and Acid Red 18 (AR18) are three of a string of approved synthetic food colorants, each of whose maximal daily intake is set to about 100 mg kg–1 day–1. This study deploys spectroscopy, electron microscopy, and X-ray diffraction (XRD) to examine the effect of dye binding to lysozyme, cytochrome c, myoglobin, and bovine serum albumin (BSA) under acidic and neutral pH conditions. The c 1/2 value for binding of food dyes to globular proteins in vitro is lowest for AR18 (∼50 μM) but increases with AY23 (∼140 μM) and AR (∼190 μM). Dye binding reversibly transforms native proteins to quasi-native states, which enter the aggregation pathway to yield an initial amorphous mesopaque that reconfigures at longer times to produce crystalline fibrillar forms. In vivo protein aggregation is, however, unlikely because of a substantial negative gradient from intestinal to systemic concentrations of the dyes.

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“…In this article, we have reported the thermodynamic based study of aqueous solvation and dissociation of benzoic acid at Kelvin temperature range in between of 288 K to 318 K. In series of aromatic acids the benzoic acid (C 6 H 5 COOH) is a colorless crystalline solid (M.P. 395 K) substance having a very poor solubility into cold water with pleasant smell and used in food additives [10,11]. In derivatives of benzoic acid the ortho-hydroxybenzoic acid (salicylic acid) have solubility in respective solvents with greater importancy for medicinal purposes as antibacterial, anti-inflammatory and in skin diseases well [12].…”

Section: …………………………………………………………………………………………………… Introduction:-mentioning

confidence: 99%

Thermodynamic Based Aqueous Solvation and Dissociation of Benzoic Acid

Mishra¹,

Singh²

2023

IJAR

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In article, we have reported a thermodynamic based study of aqueous solvation of benzoic acid (C6H5COOH) at 288 to 318 Kelvin temperature. At this temperature range the dissociation constant (Ka) of benzoic acid into aqueous solvent has been determined by applying of titration method against standard basic solution of NaOH at different ionic strength of NaCl. Although, in observation, the value of Ka is being inversely proportional in respect of temperature in between 289 K to 303 K, and at higher temperature in between 303 K to 314 K, it being directly proportional. This reports that, there are no regular correlation in between temperature and Ka of that acid. Graphically, the plot has shown the value of Ka of benzoic acid is being 4.176 at 298 K temperature. In finding of precious results for benzoic acid solvation and its dissociation into water the applying Vant Hoff equation with Gibbs free energy change relationship (âˆ†G = âˆ†H - Tâˆ†S) for reaction (endothermic or exothermic) process at standard condition of thermodynamic parameters as in terms of enthalpy (H) and entropy (S). Where, the thermodynamic parameters value (in kJ.mol-1) are being as âˆ†G = 12.507, âˆ†H = 3.823 and âˆ†S = -29.14, but, at 298 K it is show that, the acid dissociation into aqueous is an endothermic process and non-spontaneous.

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Food Additives Benzoic Acid and its Methyl and Propyl Parahydroxy Derivatives Aggregate Proteins

Cited by 7 publications

References 21 publications

Alternative Enzyme Inhibition Assay for Safety Evaluation of Food Preservatives

Alternative Enzyme Inhibition Assay for Safety Evaluation of Food Preservatives

Food Colorants Acid Yellow 23, Azorubine, and Acid Red 18 Cause Aggregation and Fibrillation of Proteins

Thermodynamic Based Aqueous Solvation and Dissociation of Benzoic Acid

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