TY  - JOUR
AU  - Brooks, Sarah J.
AU  - Nikodinović-Runić, Jasmina
AU  - Martin, Leona
AU  - Doyle, Evelyn M.
AU  - O'Sullivan, Timothy
AU  - Guiry, Patrick J.
AU  - Coulombel, Lydie
AU  - Li, Zhi
AU  - O'Connor, Kevin E.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1352
AB  - 1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.
PB  - Springer, Dordrecht
T2  - Biotechnology Letters
T1  - Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase
VL  - 35
IS  - 5
SP  - 779
EP  - 783
DO  - 10.1007/s10529-013-1148-z
ER  - 

@article{
author = "Brooks, Sarah J. and Nikodinović-Runić, Jasmina and Martin, Leona and Doyle, Evelyn M. and O'Sullivan, Timothy and Guiry, Patrick J. and Coulombel, Lydie and Li, Zhi and O'Connor, Kevin E.",
year = "2013",
abstract = "1-(3,4-Dihydroxyphenyl) ethanol was produced biocatalytically for the first time using mushroom tyrosinase. 4-Ethylphenol at 1 mM was consumed over 12 min giving 0.23 mM 4-ethylcatechol and 0.36 mM (R/S)-1-(3,4-dihydroxyphenyl) ethanol (ee 0.5 %). Mushroom tyrosinase consumed 4-ethylphenol at 6.7 mu mol min(-1) mg protein(-1) while the rates of formation of 4-ethylcatechol and 1-(3,4-dihydroxyphenyl) ethanol were 1.1 and 1.9 mu mol min(-1) mg protein(-1). Addition of the ascorbic acid, as a reducing agent to biotransformation reactions, increased 4-ethylcatechol formation by 340 %. However, accumulation of 1-(3,4-dihydroxyphenyl) ethanol was not observed in the presence of ascorbic acid. While the 1-(3,4-dihydroxyphenyl) ethanol was racemic, it is the first chiral product produced by tyrosinase starting from a non-chiral substrate.",
publisher = "Springer, Dordrecht",
journal = "Biotechnology Letters",
title = "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase",
volume = "35",
number = "5",
pages = "779-783",
doi = "10.1007/s10529-013-1148-z"
}

Brooks, S. J., Nikodinović-Runić, J., Martin, L., Doyle, E. M., O'Sullivan, T., Guiry, P. J., Coulombel, L., Li, Z.,& O'Connor, K. E.. (2013). Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters
Springer, Dordrecht., 35(5), 779-783.
https://doi.org/10.1007/s10529-013-1148-z

Brooks SJ, Nikodinović-Runić J, Martin L, Doyle EM, O'Sullivan T, Guiry PJ, Coulombel L, Li Z, O'Connor KE. Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase. in Biotechnology Letters. 2013;35(5):779-783.
doi:10.1007/s10529-013-1148-z .

Brooks, Sarah J., Nikodinović-Runić, Jasmina, Martin, Leona, Doyle, Evelyn M., O'Sullivan, Timothy, Guiry, Patrick J., Coulombel, Lydie, Li, Zhi, O'Connor, Kevin E., "Production of a chiral alcohol, 1-(3,4-dihydroxyphenyl) ethanol, by mushroom tyrosinase" in Biotechnology Letters, 35, no. 5 (2013):779-783,
https://doi.org/10.1007/s10529-013-1148-z . .

TY  - JOUR
AU  - Coulombel, Lydie
AU  - Nolan, Louise C.
AU  - Nikodinović-Runić, Jasmina
AU  - Doyle, Evelyn M.
AU  - O'Connor, Kevin E.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1161
AB  - Escherichia coli cells, expressing 4-hydroxyphenylacetate 3-hydroxylase, fully transformed 4-halogenated phenols to their equivalent catechols as single products in shaken flasks. 4-Fluorophenol was transformed at a rate 1.6, 1.8, and 3.4-fold higher than the biotransformation of 4-chloro-, 4-bromo-, and 4-iodo- phenol, respectively. A scale-up from shaken flask to a 5 L stirred tank bioreactor was undertaken to develop a bioprocess for the production of 4-substituted halocatechols at higher concentrations and scale. In a stirred tank reactor, the optimized conditions for induction of 4-HPA hydroxylase expression were at 37 C for 3 h. The rate of biotransformation of 4-fluorophenol to 4-fluorocatechol by stirred tank bioreactor grown cells was the same at 1 and 4.8 mM (5.13 mu mol/min/g CDW) once the ratio of biocatalyst (E. coli CDW) to substrate concentration (mM) was maintained at 2:1. At 10.8 mM 4-fluorophenol, the rate of 4-fluorocatechol formation decreased by 4.7-fold. However, the complete transformation of 1.3 g of 4-fluorophenol (10.8 mM) to 4-fluorocatechol was achieved within 7 h in a 1 L reaction volume. Similar to 4-fluorophenol, other 4-substituted halophenols were completely transformed to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM resulted in a 2.5-20-fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography resulted in the production of purified products with a final yield of between 33% and 38%.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase
VL  - 89
IS  - 6
SP  - 1867
EP  - 1875
DO  - 10.1007/s00253-010-2969-5
ER  - 

@article{
author = "Coulombel, Lydie and Nolan, Louise C. and Nikodinović-Runić, Jasmina and Doyle, Evelyn M. and O'Connor, Kevin E.",
year = "2011",
abstract = "Escherichia coli cells, expressing 4-hydroxyphenylacetate 3-hydroxylase, fully transformed 4-halogenated phenols to their equivalent catechols as single products in shaken flasks. 4-Fluorophenol was transformed at a rate 1.6, 1.8, and 3.4-fold higher than the biotransformation of 4-chloro-, 4-bromo-, and 4-iodo- phenol, respectively. A scale-up from shaken flask to a 5 L stirred tank bioreactor was undertaken to develop a bioprocess for the production of 4-substituted halocatechols at higher concentrations and scale. In a stirred tank reactor, the optimized conditions for induction of 4-HPA hydroxylase expression were at 37 C for 3 h. The rate of biotransformation of 4-fluorophenol to 4-fluorocatechol by stirred tank bioreactor grown cells was the same at 1 and 4.8 mM (5.13 mu mol/min/g CDW) once the ratio of biocatalyst (E. coli CDW) to substrate concentration (mM) was maintained at 2:1. At 10.8 mM 4-fluorophenol, the rate of 4-fluorocatechol formation decreased by 4.7-fold. However, the complete transformation of 1.3 g of 4-fluorophenol (10.8 mM) to 4-fluorocatechol was achieved within 7 h in a 1 L reaction volume. Similar to 4-fluorophenol, other 4-substituted halophenols were completely transformed to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM resulted in a 2.5-20-fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography resulted in the production of purified products with a final yield of between 33% and 38%.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase",
volume = "89",
number = "6",
pages = "1867-1875",
doi = "10.1007/s00253-010-2969-5"
}

Coulombel, L., Nolan, L. C., Nikodinović-Runić, J., Doyle, E. M.,& O'Connor, K. E.. (2011). Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. in Applied Microbiology and Biotechnology
Springer, New York., 89(6), 1867-1875.
https://doi.org/10.1007/s00253-010-2969-5

Coulombel L, Nolan LC, Nikodinović-Runić J, Doyle EM, O'Connor KE. Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. in Applied Microbiology and Biotechnology. 2011;89(6):1867-1875.
doi:10.1007/s00253-010-2969-5 .

Coulombel, Lydie, Nolan, Louise C., Nikodinović-Runić, Jasmina, Doyle, Evelyn M., O'Connor, Kevin E., "Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase" in Applied Microbiology and Biotechnology, 89, no. 6 (2011):1867-1875,
https://doi.org/10.1007/s00253-010-2969-5 . .