Topic
Benzoic acid
About: Benzoic acid is a research topic. Over the lifetime, 11832 publications have been published within this topic receiving 167127 citations. The topic is also known as: Retardex & E210.
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TL;DR: In this paper, the authors present a Web of Science Record created on 2006-02-21, modified on 2017-05-12 for a paper entitled "Reference LPI-ARTICLE-2000-019:
Abstract: Reference LPI-ARTICLE-2000-019View record in Web of Science Record created on 2006-02-21, modified on 2017-05-12
214 citations
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TL;DR: The solubilization of rapamycin, a poorly water soluble investigational immunosuppressive drug, by facilitated hydrotropy is presented and yielded a dramatic (>1000-fold) increase in the aqueous solubility of Rapamycin.
213 citations
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TL;DR: It is proposed that sorbic acid acts as a membrane‐active substance rather than as a weak‐acid preservative, and shows similar inhibition to other six‐carbon acids, alcohols and aldehydes.
Abstract: Weak-acid preservatives are widely used to maintain microbial stability in foods and beverages. Classical weak-acid theory proposes that undissociated acid molecules pass through the plasma membrane, dissociate in the neutral pH of the cytoplasm, release protons and inhibit growth through acidification of the cytoplasm. Inhibitory concentrations of sorbic acid are shown to liberate fewer protons than other weak-acid preservatives. Sorbic acid shows similar inhibition to other six-carbon acids, alcohols and aldehydes, the latter being unable to act as weak acids. A survey of 22 yeasts showed high correlation between sorbate resistance and ethanol tolerance. Inhibition by short-chain acids or alcohols showed strong correlation with lipophilicity. It is proposed that sorbic acid acts as a membrane-active substance rather than as a weak-acid preservative.
211 citations
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TL;DR: Streptomyces olivochromogenes FAE showed activity against methyl ferulate, methyl sinapinate and methyl p-coumarate, but at a level 420-fold less than the A. niger esterase, which shows the necessity for C-3 on the phenol ring to be methoxylated and the aliphatic region of the substrate to be unsaturated.
Abstract: An inducible ferulic acid esterase (FAE-III) has been isolated, purified and partially characterized from Aspergillus niger after growth on oat spelt xylan. The purification procedure utilized ammonium sulphate precipitation, hydrophobic interaction and anion-exchange chromatography. The purified enzyme appeared almost pure by SDS-PAGE, with an apparent M
r of 36000. A single band, corresponding to a pl of 3·3 was observed on isoelectric focusing. With methyl ferulate as substrate, the enzyme had a specific activity of 67 IU (mg protein)-1, pH and temperature optima of 5 and 55–60 °C, respectively, and a Km of 2·08 mM and a V
max of 175 μmol min-1 (mg protein)-1. The enzyme was also active upon methyl sinapinate, methyl-3,4-dimethoxy cinnamate and methyl p-coumarate, but not benzoic acid methyl esters or methyl caffeate. Similarly, Streptomyces olivochromogenes FAE showed activity against methyl ferulate, methyl sinapinate and methyl p-coumarate, but at a level 420-fold less (on methyl ferulate) than the A. niger esterase. No activity was detected against the benzoate methyl esters. For both enzymes, this shows the necessity for C-3 on the phenol ring to be methoxylated and the aliphatic region of the substrate to be unsaturated. The specific activity of FAE-III on destarched wheat bran was 31 U (mg protein)-1 in the presence of Trichoderma viride xylanase and 3 U (mg protein)-1 in the absence. Apparent pH dependent binding of A. niger FAE-III to microcrystalline cellulose was also demonstrated.
210 citations
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TL;DR: The microbial model system yielded patterns of phenolic metabolites similar to those reported with cytochrome P 450 monooxygenases of hepatic microsomes and/or in vivo mammalian systems.
210 citations