Metabolic aspects of antioxidants and preservatives

Jw, Daniel

doi:10.3109/00498258609038984

Cited by 69 publications

(33 citation statements)

References 18 publications

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“…According to the US Food and Drug Administration list, PG is also used to preserve and stabilize medicinal preparations [4]. It is an allowed additive in the European Union and in many others countries.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

Bouaziz¹,

Horchani²,

Salem³

et al. 2010

Journal of Molecular Catalysis B: Enzymatic

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a b s t r a c tThe ability of a non-commercial immobilized Staphylococcus xylosus lipase to catalyze the esterification of propanol with gallic acid was investigated and the antioxidant as well as the antimicrobial activities of the ester formed were evaluated. The response surface methodology, based on a three variables Box-Behnken design (reaction temperature, enzyme amount and 1-propanol/gallic acid molar ratio), was used to optimize the experimental conditions of propylgallate synthesis. The maximum conversion yield (90% ±3.5) was obtained by using 400 IU of immobilized lipase and a propanol/gallic acid at a molar ratio of 160 at 52 • C. The obtained ester was characterized by spectroscopic methods, NMR and FTIR. The antioxidant activity of propyl gallate was evaluated and compared to the synthetic classical antioxidants, BHA and ascorbic acid, taken as references. In addition, the antimicrobial activity of the propyl gallate was tested against S. xylosus, Escherchia coli and Staphylococcus aureus using disc diffusion and macrodilution methods. Our results show that the synthesized propyl gallate ester presents a higher antioxidant and antimicrobial power than the parent gallic acid as well as the synthetic classical antioxidants.

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Section: Introductionmentioning

confidence: 99%

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

Bouaziz¹,

Horchani²,

Salem³

et al. 2010

Journal of Molecular Catalysis B: Enzymatic

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show abstract

“…PG is also used to preserve and stabilize medicinal preparations on the US Food and Drug Administration list (1). Because of its prevalent usage, the potential toxicity of PG has been investigated in vivo (2,3) and in vitro, to assess various toxicological properties, i.e., mutagenicity (4) and cytogenetic effects (5).…”

Section: Introductionmentioning

confidence: 99%

Propyl gallate inhibits the growth of HeLa cells via caspase-dependent apoptosis as well as a G1 phase arrest of the cell cycle

Han

Moon²,

You³

et al. 2010

Oncol Rep

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Abstract. Propyl gallate (PG) as a synthetic antioxidant exerts a variety of effects on tissue and cell functions. Here, we evaluated the effects of PG on the growth of HeLa cells in relation to apoptosis and the cell cycle. PG dosedependently inhibited the growth of HeLa cells with an IC 50 of approximately 800 μM at 24 h. DNA flow cytometric analysis indicated that PG significantly induced a G1 phase arrest of the cell cycle along with an increase in the cyclindependent kinase inhibitor (CDKI) p27. In addition, PG induced apoptosis, which was accompanied by the loss of mitochondrial membrane potential (MMP; Δae m ), activation of caspase-3 and caspase-8 and PARP cleavage. All the tested caspase inhibitors (pan-caspase, caspase-3, -8 or -9 inhibitor) significantly rescued HeLa cells from PG-induced cell death. However, none of the caspase inhibitors prevented the loss of MMP (Δae m ) induced by PG. In conclusion, PG inhibited the growth of HeLa cells via caspase-dependent apoptosis as well as a G1 phase arrest of the cell cycle.

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“…PG is also used to preserve and stabilize medicinal preparations on the US Food and Drug Administration list (2). Because of its prevalent usage, the potential toxicity of PG has been investigated in vivo (3,4) and in vitro, to assess various toxicological properties, i.e., mutagenicity (5) and cytogenetic effects (6).…”

Section: Introductionmentioning

confidence: 99%

Propyl gallate inhibits the growth of endothelial cells, especially calf pulmonary arterial endothelial cells via caspase-independent apoptosis

Han

Moon²,

You³

et al. 2010

Int J Mol Med

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Abstract. Propyl gallate (PG) as a synthetic antioxidant exerting a variety of effects on tissue and cell functions. We evaluated the effects of PG on the growth of endothelial cells, especially calf pulmonary artery endothelial cells (CPAEC) in relation to apoptosis. PG dose-dependently inhibited the growth of CPAEC and human umbilical vein endothelial cells (HUVEC) at 24 h. The susceptibility of CPAEC to PG was higher than that of HUVEC. PG induced apoptosis in CPAEC, which was accompanied by the loss of mitochondrial membrane potential (MMP; ΔΨ m ). The tested caspase inhibitors (pan-caspase, caspase-3, -8 or -9 inhibitor) did not rescue CPAEC from PG-induced cell death but instead slightly enhanced the cell death. PG increased reactive oxygen species (ROS) level in CPAEC. The caspase inhibitors did not significantly change the ROS level. Furthermore, PG increased the GSH depleted cell number and decreased GSH level in CPAEC. The tested caspase inhibitors did not significantly change the number in PG-treated CPAEC. Each caspase inhibitor differently alters GSH levels in CPAEC. In conclusion, PG inhibited the growth of endothelial cells, especially CPAEC via caspase-independent apoptosis. PGinduced CPAEC death was accompanied by ROS increase and GSH depletion.

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Metabolic aspects of antioxidants and preservatives

Cited by 69 publications

References 18 publications

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

Enzymatic propyl gallate synthesis in solvent-free system: Optimization by response surface methodology

Propyl gallate inhibits the growth of HeLa cells via caspase-dependent apoptosis as well as a G1 phase arrest of the cell cycle

Propyl gallate inhibits the growth of endothelial cells, especially calf pulmonary arterial endothelial cells via caspase-independent apoptosis

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