An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration

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Standard

An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration. / Gauer, Sabrina; Wang, Zhijie; Otten, Harm; Etienne, Mathieu; Bjerrum, Morten Jannik; Lo Leggio, Leila; Walcarius, Alain; Giffhorn, Friedrich; Kohring, Gert-Wieland.

I: Applied Microbiology and Biotechnology, Bind 98, Nr. 7, 2014, s. 3023-3032.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Gauer, S, Wang, Z, Otten, H, Etienne, M, Bjerrum, MJ, Lo Leggio, L, Walcarius, A, Giffhorn, F & Kohring, G-W 2014, 'An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration', Applied Microbiology and Biotechnology, bind 98, nr. 7, s. 3023-3032. https://doi.org/10.1007/s00253-013-5180-7

APA

Gauer, S., Wang, Z., Otten, H., Etienne, M., Bjerrum, M. J., Lo Leggio, L., Walcarius, A., Giffhorn, F., & Kohring, G-W. (2014). An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration. Applied Microbiology and Biotechnology, 98(7), 3023-3032. https://doi.org/10.1007/s00253-013-5180-7

Vancouver

Gauer S, Wang Z, Otten H, Etienne M, Bjerrum MJ, Lo Leggio L o.a. An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration. Applied Microbiology and Biotechnology. 2014;98(7):3023-3032. https://doi.org/10.1007/s00253-013-5180-7

Author

Gauer, Sabrina ; Wang, Zhijie ; Otten, Harm ; Etienne, Mathieu ; Bjerrum, Morten Jannik ; Lo Leggio, Leila ; Walcarius, Alain ; Giffhorn, Friedrich ; Kohring, Gert-Wieland. / An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration. I: Applied Microbiology and Biotechnology. 2014 ; Bind 98, Nr. 7. s. 3023-3032.

Bibtex

@article{f4be370029854ee79235a16a709fc564,
title = "An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration",
abstract = "A gene in Bradyrhizobium japonicum USDA 110, annotated as a ribitol dehydrogenase (RDH), had 87 % sequence identity (97 % positives) to the N-terminal 31 amino acids of an L-glucitol dehydrogenase from Stenotrophomonas maltophilia DSMZ 14322. The 729-bp long RDH gene coded for a protein consisting of 242 amino acids with a molecular mass of 26.1 kDa. The heterologously expressed protein not only exhibited the main enantio selective activity with D-glucitol oxidation to D-fructose but also converted L-glucitol to D-sorbose with enzymatic cofactor regeneration and a yield of 90 %. The temperature stability and the apparent K m value for L-glucitol oxidation let the enzyme appear as a promising subject for further improvement by enzyme evolution. We propose to rename the enzyme from the annotated RDH gene (locus tag bll6662) from B. japonicum USDA as a D-sorbitol dehydrogenase (EC 1.1.1.14).",
author = "Sabrina Gauer and Zhijie Wang and Harm Otten and Mathieu Etienne and Bjerrum, {Morten Jannik} and {Lo Leggio}, Leila and Alain Walcarius and Friedrich Giffhorn and Gert-Wieland Kohring",
year = "2014",
doi = "10.1007/s00253-013-5180-7",
language = "English",
volume = "98",
pages = "3023--3032",
journal = "Applied Microbiology and Biotechnology",
issn = "0175-7598",
publisher = "Springer",
number = "7",

}

RIS

TY - JOUR

T1 - An L-glucitol oxidizing dehydrogenase from Bradyrhizobium japonicum USDA 110 for production of D-sorbose with enzymatic or electrochemical cofactor regeneration

AU - Gauer, Sabrina

AU - Wang, Zhijie

AU - Otten, Harm

AU - Etienne, Mathieu

AU - Bjerrum, Morten Jannik

AU - Lo Leggio, Leila

AU - Walcarius, Alain

AU - Giffhorn, Friedrich

AU - Kohring, Gert-Wieland

PY - 2014

Y1 - 2014

N2 - A gene in Bradyrhizobium japonicum USDA 110, annotated as a ribitol dehydrogenase (RDH), had 87 % sequence identity (97 % positives) to the N-terminal 31 amino acids of an L-glucitol dehydrogenase from Stenotrophomonas maltophilia DSMZ 14322. The 729-bp long RDH gene coded for a protein consisting of 242 amino acids with a molecular mass of 26.1 kDa. The heterologously expressed protein not only exhibited the main enantio selective activity with D-glucitol oxidation to D-fructose but also converted L-glucitol to D-sorbose with enzymatic cofactor regeneration and a yield of 90 %. The temperature stability and the apparent K m value for L-glucitol oxidation let the enzyme appear as a promising subject for further improvement by enzyme evolution. We propose to rename the enzyme from the annotated RDH gene (locus tag bll6662) from B. japonicum USDA as a D-sorbitol dehydrogenase (EC 1.1.1.14).

AB - A gene in Bradyrhizobium japonicum USDA 110, annotated as a ribitol dehydrogenase (RDH), had 87 % sequence identity (97 % positives) to the N-terminal 31 amino acids of an L-glucitol dehydrogenase from Stenotrophomonas maltophilia DSMZ 14322. The 729-bp long RDH gene coded for a protein consisting of 242 amino acids with a molecular mass of 26.1 kDa. The heterologously expressed protein not only exhibited the main enantio selective activity with D-glucitol oxidation to D-fructose but also converted L-glucitol to D-sorbose with enzymatic cofactor regeneration and a yield of 90 %. The temperature stability and the apparent K m value for L-glucitol oxidation let the enzyme appear as a promising subject for further improvement by enzyme evolution. We propose to rename the enzyme from the annotated RDH gene (locus tag bll6662) from B. japonicum USDA as a D-sorbitol dehydrogenase (EC 1.1.1.14).

U2 - 10.1007/s00253-013-5180-7

DO - 10.1007/s00253-013-5180-7

M3 - Journal article

C2 - 24061413

VL - 98

SP - 3023

EP - 3032

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 7

ER -

ID: 99372402