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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).
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https://hal.univ-lorraine.fr/hal-01497266
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Submitted on : Tuesday, March 28, 2017 - 2:46:14 PM
Last modification on : Friday, February 26, 2021 - 2:42:01 PM

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Sabrina Gauer, Zhijie Wang, Harm Otten, Mathieu Etienne, Morten Jannik Bjerrum, et al.. 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, Springer Verlag, 2014, 98 (7), pp.3023 - 3032. ⟨10.1007/s00253-013-5180-7⟩. ⟨hal-01497266⟩

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