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

Sabrina Gauer; Zhijie Wang; Harm Otten; Mathieu Etienne; Morten Jannik Bjerrum; Leila Lo Leggio; Alain Walcarius; Friedrich Giffhorn; Gert-Wieland Kohring

doi:10.1007/s00253-013-5180-7

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

Sabrina Gauer, Zhijie Wang, Harm Otten, Mathieu Etienne, Morten Jannik Bjerrum, Leila Lo Leggio, Alain Walcarius, Friedrich Giffhorn, Gert-Wieland Kohring

Kemisk Institut

7 Citationer (Scopus)

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).

Originalsprog	Engelsk
Tidsskrift	Applied Microbiology and Biotechnology
Vol/bind	98
Udgave nummer	7
Sider (fra-til)	3023-3032
Antal sider	10
ISSN	0175-7598
DOI	https://doi.org/10.1007/s00253-013-5180-7
Status	Udgivet - apr. 2014

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10.1007/s00253-013-5180-7

Citationsformater

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

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 et al.
I: Applied Microbiology and Biotechnology, Bind 98, Nr. 7, 04.2014, s. 3023-3032.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

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

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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",

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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 - 2014/4

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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

SN - 0175-7598

VL - 98

SP - 3023

EP - 3032

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

IS - 7

ER -

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

Abstract

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