• Journal of the Korean Society of Food Culture
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• v.20 no.5
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• pp.603-607
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• 2005

Fourteen phenolic compounds(benzoic acid, p-hydroxybenzoic acid, protocatechuic acid, vanillic acid, syringic acid, gallic acid, caffeic acid, ferulic acid, (+)-catechin, quercetin, rutin, catechol, chlorogenic acid and L-ascorbic acid) were examined for their effects on the anticarigenic activity. Among tested samples, catechol was significantly inhibited the S. mutans, exhibiting an clear zone 18.5-19.5mm by 10 mg/disc level. The minimal inhibition concentration(MIC) of the phenolic compounds for Streptococcus mutans, M1 and M2 strain were determined as 2,000 ppm, whereas catechol was 1,000 ppm. The activity of glucosyltransferase(GTase) was significantly inhibited by catechol, at 10 ppm(58.7%), 50 ppm(60.7%) and 100 ppm(88.4%) and 500 ppm(89.6%), respectively. Among them, catechol showed most significant anticariogenic activity as well as inhibition of GTase activity.

• Journal of Adhesion and Interface
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• v.24 no.4
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• pp.113-119
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• 2023

Since it was reported that the unusual amino acid DOPA in synergy with lysine and histidine residues found in mussel adhesive proteins plays a pivotal role in mussel adhesion in underwater environments, there has been a burgeoning development of various catecholamines-based adhesives for biomedical applications. Among these, catechol-conjugated chitosan, containing catecholamine, featuring multiple catechol groups within its aminerich chitosan backbone, has found versatile utility in fields, such as tissue adhesion, wound dressing, tissue healing, hemostats, drug delivery systems, and tissue engineering scaffolds. Significantly, chitosan-catechol is a mussel-inspired material approved by both US Food and Drug Administration (FDA) and KR Ministry of Food and Drug Safety (MFDS) for its effectiveness in hemostasis. This review focuses on 1) general aspects of catechol-conjugated chitosan, highlighting catechol group integration into chitosan backbones, 2) examination of proposed mechanisms of hemostasis, and 3) exploration of diverse physical forms, including solution, hydrogels, patches, and thin films with practical applications inapplicable to hemostasis.

• KSBB Journal
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• v.18 no.3
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• pp.174-179
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• 2003

The bacterium NFQ-1 capable of utilizing quinoline (2,3-benzopyridine) as the sole source of carbon, nitrogen and energy was enriched and isolated from soil samples of dead coal pit areas. Strain NFQ-1 was identified as Pseudomonas nitroreducens NFQ-1 by BIOLOG system, and assigned to Pseudomonas sp. NFO-1. Pseudomonas sp. NFQ-1 was used with the concentration range of 1 to 10 mM quinoline. Strain NFQ-1 could degrade 2.5 mM quinoline within 9 hours of incubation. Initial pH 8.0 in the culture was reduced to 6.8, and eventually 7.0 as the incubation was proceeding. 2-Hydroxyquinoline, the first intermediate of the degradative pathway, accumulated transiently in the growth medium. The highest concentration of quinoline (15 mM) in this work inhibited cell growth and quinoline degradation. Pseudomonas sp. NFQ-1 was able to utilize various quinoline derivatives and aromatic compounds including 2-hydroxyquinoline, p-comaric acid, benzoic acid, p-cresol, p-hydroxybenzoate, protocatechuic acid, and catechol. The specific activity of catechol oxygenases was determined to approximately 184.7 unit/㎎ for catechol 1.2-dioxygenase and 33.19 unit/㎎ for catechol 2,3-dioxygenase, respectively. As the result, it showed that strain NFQ-1 degraded quinoline via mainly orthp-cleavage pathway, and in partial meta-cleavage pathway.

• Journal of Environmental Health Sciences
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• v.26 no.3
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• pp.86-91
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• 2000

The purpose of this was to investigate the degradation efficiency of phenol compounds(catechol, ferulic acid, protocatechuic acid, syringic acid, vanillic acid) by Streptomyces halstedii scabies SAI-36, Streptomyces avendulas SA2-14, and Strptomyces badius(ATCC 39117, control group). The results were as follows: Catechol showed the degradation efficiency that is lower than 50% in three strains. Ferulic acid and vanillic acid showed high degradation efficiency of 98.8% and 94.5% respectively by Streptomyces lavendulas SA2-14. protocatechuic acid and syringicacid showed high degradation efficiency of 89.6% and 77.9%. The degradation efficiency of catechol by Streptomyces halstedii scabies SAI-36, Streptomyces lavendulas SA2-14 and Streptomyces badius(ATCC 39117) was low as 49.2%, 40.2% and 20.2% respectively. But the degradation of other phenolic compoumds except catechol by Streptomyces laven-dulas SA2-36 and Streptomyces badius(ATCC 39117). The results demonstrated that two experimental strains are superior ability to control group in degradation of phenol compounds and Streptomyces lavendulas SA2-14 was superior of two experimental strain. This results were consistent with previous research results that Streptomyces lavendulas SA2-14 was the best strain in degradation ability for lignin, decoloration abilities for variousdyes, and various enzyme production abilities. Therefore, it is suggested that lignin can be used as a indicator when selecting Actinomycetes for degradation of non-degradable materials such as phenol compounds.

• Bulletin of the Korean Chemical Society
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• v.35 no.6
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• pp.1769-1776
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• 2014

Binding modes of a series of catechol derivatives such as protein tyrosine phosphatase 1B (PTP1B) inhibitors were identified by molecular modeling techniques. Docking, molecular dynamics simulations and free energy calculations were employed to determine the modes of these new inhibitors. Binding free energies were calculated by involving different energy components using the Molecular Mechanics-Poisson-Boltzmann Surface Area and Generalized Born Surface Area methods. Relatively larger binding energies were obtained for the catechol derivatives compared to one of the PTP1B inhibitors already in use. The Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) free energy decomposition analysis indicated that the hydroxyl functional groups and biphenyl ring system had favorable interactions with Met258, Tyr46, Gln262 and Phe182 residues of PTP1B. The results of hydrogen bound analysis indicated that catechol derivatives, in addition to hydrogen bonding interactions, Val49, Ile219, Gln266, Asp181 and amino acid residues of PTP1B are responsible for governing the inhibitor potency of the compounds. The information generated from the present study should be useful for the design of more potent PTP1B inhibitors as anti-diabetic agents.

• Microbiology and Biotechnology Letters
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• v.23 no.3
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• pp.255-262
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• 1995

Intact cells of Acinetobacter sp. T5-7 completely degraded trichloroethylene (TCE) following growth with phenol. This strain could grow on at least eleven aromatic compounds, e.g., benzaldehyde, benzene, benzoate, benzylalochol, catechol, caffeic acid, 2.4-D, p-hydroxybenzoate, phenol, protocatechuate and salicylate, and did grow on alkane, such as octane. But except phenol, other aromatic compounds did not induced TCE degradation. Phenol biotransformation products, catechol was identified in the culture media. However, catechol-induced cells did not degrade TCE. So we assumed that phenol hydroxylase was responsible for the degradation of TCE. The isolate T5-7 showed growth in MM2 medium containing sodium lactate and catechol rather than phenol, but did not display phenol hydroxyalse activity, suggesting induction of enzyme synthesis by phenol. Phenol hydroxylase activity was independent of added NADH and flavin adenine dinucleotide but was dependent on NADPH addition. Degradation of phenol produced catechols which are then cleaved by meta-fission. We identified catechol-2.3-dioxygenase by active staining of polyacrylamide gel.

• Journal of Microbiology and Biotechnology
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• v.9 no.3
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• pp.249-254
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• 1999

A catechol 2,3-dioxygenase (C23O) was purified to apparent homogeneity from Pseudomonas putida SU10 through several purification steps consisting of ammonium sulfate precipitation and chromatographies on DEAE 5PW, Superdex S-200, and Resource-Q. Gel filtration indicated a molecular mass under nondenaturing conditions of about 130 kDa. The enzyme has a subunit of 34 kDa as was determined by SDS-PAGE. These results suggest that the native enzyme is composed of four identical subunits. The N-terminal amino acid sequence (30 residues) of the enzyme has been determined and exhibits high identity with other extradiol dioxygenases. The reactivity of this enzyme towards catechol and methyl-substituted catechols is somewhat different from that seen for other catechol 2,3-dioxygenases, with 4-methylcatechol cleaved at a higher rate than catechol or 3-methylcatechol. $K_m$ values of the enzyme for these substrates are between 3.5 and 5.7 M.

• Korean Journal of Microbiology
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• v.36 no.1
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• pp.58-63
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• 2000

A bacterial isolate capable of degrading benzoate was selected from wastewater of Yocheon industrial complex and examined its biochemical characteristics and fatty acid composition. The isolate was identified as Klebsiella oxytoca strain C302. The strain C3O2 degraded catechol, protocatechuate, and 4-hydroxybenzoate as well as benzoate. The strain grew on and degraded 0.5 to 1.0 mM catechol most actively in MM2 medium at pH 7.0 and $30^{\circ}C$.

• KSBB Journal
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• v.9 no.5
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• pp.525-531
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• 1994

Tyrosinase has two types of enzymatic activities, cresolase catalyzing the hydroxylation of monophenol and catecholase catalyzing the oxidation of o-phenol. Gradual inactivation of the enzyme during the reaction is a barrier to be overcome for the commercial application of the enzyme. Tyrosinase was stabilized by modifying the lysine residue of the enzyme using glutaraldehyde. In addition to that, tyrosinase was also stabilized by adapting the continuous reactor system. In packed bed reactor quinone could be easily removed, so the stability of tyrosinase increased. Borate buffer retarded the reaction rate of catechol to quinone and consequently decreased the tyroslnase inactivation. Tyrosinase immobilizer on controlled pore glass showed significantly enhanced stability in a packed-bed reactor.

• Journal of the Korean Electrochemical Society
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• v.7 no.1
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• pp.9-15
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• 2004

Cyclic voltammetry and chronocoulometry have been used for characterization of catechol violet (CV) at the hanging mercury drop electrode in acetic acid-sodium acetate buffer solution. At pH 2.94 a nearly symmetric cyclic voltammetric wave due to an irreversible weak adsorption of CV on mercury was obtained at concentration of $0.53{\mu}mol\;dm ^{-3}$. Under these conditions, CV adsorbes in a monolayer. Upon increasing the concentration, the symmetry of the wave decreases; it can be attributed to a mixed diffusion adsorption process. The amount of the adsorbed catechol violet on the HMDE expressed as surface concentration as well as the surface areaf occupied by one molecule$(\sigma)$ were calculated. It was found that the values obtained for f and o utilizing cyclic voltammetric and chrono-coulometry are almost identical. A 1:1 and 1:2 Th (IV)-CV complexes are formed on addition of thorium (IV) to catechol violet. These complexes are adsorbed and reduced on the HMDE at more negative potentials than the peak potential of free CV, Using the square-wave (SW) technique, the adsorptive cathodic stripping voltammetry, ACSV, of these complexes was studied. It was found that the SW-ACSV of Th(IV)-CV can be applied to the determination of thorium at the nanomole level. Optimum conditions and the analytical method of determination were presented and discussed.