Modeling the enzymatic transformation of 3,5-dimethoxy,4-hydroxy cinnamic acid by polyphenoloxidase from the white-rot fungusTrametes versicolor

Lacki, K.

doi:10.1002/(sici)1097-0290(19960805)51:3<249::aid-bit1>3.0.co;2-d

Cited by 14 publications

(5 citation statements)

References 22 publications

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“…If the product of DAD thermolysis was also transformed by the same mechanism (i.e., the reaction took place at the same active site), then during phase A of the overall transformation of SA there would be at least three substrates that could compete for the enzyme active site. This hypothesis was successfully applied in modeling the dynamics of SA oxidation using the model based on the Theorrel-Chance Bi-Bi mechanism with three alternate substrates (Lacki and Duvnjak, 1996b). The fact that in the present study the two phases were so distinct could be related to the difference in the pH optima for the enzymatic transformations of SA (Lacki and Duvnjak, 1996a) and of DAD, which are 3.7 and 4.5 (Fig.…”

Section: Discussionmentioning

confidence: 67%

Transformation of 3,5‐dimethoxy,4‐hydroxy cinnamic acid by polyphenol oxidase from the fungus Trametes versicolor: Product elucidation studies

Lacki

1998

Biotechnol. Bioeng.

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Sinapic acid (SA), 3,5-dimethoxy,4-hydroxy cinnamic acid, was incubated with a crude polyphenol oxidase from the fungus Trametes versicolor. Some products of this transformation were isolated and their structures identified using mass spectrometry, nuclear magnetic resonance and Fourier transform infrared spectroscopy, and X-ray crystallography. It was found that the enzymatic oxidation of SA includes two distinct phases. In the initial phase SA is enzymatically transformed to r-1H-2c,6c-bis-(4'-hydroxy-3', 5'-dimethoxyphenyl)-3,7-dioxabicyclo-[3,3,0]-octane-4,8-dione, dehydrodisinapic acid dilactone. The mechanism of this reaction may involve coupling of two phenoxy radicals by the beta-beta mode and subsequent intramolecular nucleophilic attack. In the second phase dehydrodisinapic acid dilactone is transformed by polyphenol oxidase into several intermediate products, including 4-(4-(3, 5-dimethoxy-4-oxo-2,5-cyclohexadienyliden)-1, 4-dihydroxy-(E)-2-butenylidene)-2,6-dimethoxy-2, 5-cyclohexadien-1-one. The final product of the overall transformation of SA is 2,6-dimethoxy-p-benzoquinone. The obtained results were used to propose a part of the transformation pathway for the enzymatic oxidation of SA by polyphenol oxidase.

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Section: Discussionmentioning

confidence: 67%

Transformation of 3,5‐dimethoxy,4‐hydroxy cinnamic acid by polyphenol oxidase from the fungus Trametes versicolor: Product elucidation studies

Lacki

1998

Biotechnol. Bioeng.

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“…The kinetic was monitored at various interval times by withdrawing samples (0.1 ml) from the reaction mixture of the aqueous and of the hydro-organic media (in emulsion) and from each phase of the hydro-organic biphasic medium (aqueous and organic phase). The enzymatic reaction was stopped by the addition of methanol (0.9 ml) containing 0.03% (v/v) of TFA (Lacki & Duvnjak, 1996;Maurizo et al, 1983).…”

Section: Oxidation Of Phenolsmentioning

confidence: 99%

Phenolic colorants obtained by enzymatic synthesis using a fungal laccase in a hydro-organic biphasic system

Mustafa¹,

Muniglia²,

Rovel³

et al. 2005

Food Research International

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“…Sinapic acid (3,5-dimethoxy-4-hydroxycinnamic acid, 1 , Figure ), which is also a widespread cinnamic acid derivative () with anti-inflammation and antioxidation capabilities ( , ), exists in many foods and fruits, such as the fruit of Citrus limon , Vitis vinifera , and the root of Allium cepa ( − ). Sinapic acid is a good substrate for many oxidoreductases such as polyphenol oxidase from the white-rot fungus Trametes versicolor ( − ), cell wall-bound peroxidases (), and horseradish peroxidase (). Some dehydrodimers obtained both in vitro and in vivo by oxidoreductases have already been characterizied ( − ).…”

Section: Introductionmentioning

confidence: 99%

Biotransformation of Sinapic Acid Catalyzed by Momordica charantia Peroxidase

Liu

Wan

Huang

et al. 2007

J. Agric. Food Chem.

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Biotransformation of sinapic acid (1) with H2O2/Momordica charantia peroxidase, which exists in the widely used food M. charantia, at pH 5.0, 43 degrees C, in the presence of acetone resulted in six compounds, including four new compounds. Compound 2 was the first isolation of a new unique sinapic acid tetrameric derivate, which is formed by peroxidase catalysis in vitro. Besides 2, three other new sinapic acid dimers, 3-5 have also been isolated. Their structures were established on the basis of spectroscopic data. Compound 5 showed a stronger antioxidative activity than the parent sinapic acid (1). Compounds 4 and 5 significantly inhibited the growth of HL-60 cell at the concentration of 10-5 microl/L.

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Modeling the enzymatic transformation of 3,5-dimethoxy,4-hydroxy cinnamic acid by polyphenoloxidase from the white-rot fungusTrametes versicolor

Cited by 14 publications

References 22 publications

Transformation of 3,5‐dimethoxy,4‐hydroxy cinnamic acid by polyphenol oxidase from the fungus Trametes versicolor: Product elucidation studies

Transformation of 3,5‐dimethoxy,4‐hydroxy cinnamic acid by polyphenol oxidase from the fungus Trametes versicolor: Product elucidation studies

Phenolic colorants obtained by enzymatic synthesis using a fungal laccase in a hydro-organic biphasic system

Biotransformation of Sinapic Acid Catalyzed by Momordica charantia Peroxidase

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