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Title: Heat-stable, FE-dependent alcohol dehydrogenase for aldehyde detoxification

Abstract

The present invention relates to microorganisms and polypeptides for detoxifying aldehydes associated with industrial fermentations. In particular, a heat-stable, NADPH- and iron-dependent alcohol dehydrogenase was cloned from Thermoanaerobacter pseudethanolicus 39E and displayed activity against a number of aldehydes including inhibitory compounds that are produced during the dilute-acid pretreatment process of lignocellulosic biomass before fermentation to biofuels. Methods to use the microorganisms and polypeptides of the invention for improved conversion of bio mass to biofuel are provided as well as use of the enzyme in metabolic engineering strategies for producing longer-chain alcohols from sugars using thermophilic, fermentative microorganisms.

Inventors:
;
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1436517
Patent Number(s):
9,951,359
Application Number:
15/060,078
Assignee:
UT-BATTELLE, LLC (Oak Ridge, TN) ORNL
DOE Contract Number:
AC05-00OR22725
Resource Type:
Patent
Resource Relation:
Patent File Date: 2016 Mar 03
Country of Publication:
United States
Language:
English

Citation Formats

Elkins, James G., and Clarkson, Sonya. Heat-stable, FE-dependent alcohol dehydrogenase for aldehyde detoxification. United States: N. p., 2018. Web.
Elkins, James G., & Clarkson, Sonya. Heat-stable, FE-dependent alcohol dehydrogenase for aldehyde detoxification. United States.
Elkins, James G., and Clarkson, Sonya. Tue . "Heat-stable, FE-dependent alcohol dehydrogenase for aldehyde detoxification". United States. doi:. https://www.osti.gov/servlets/purl/1436517.
@article{osti_1436517,
title = {Heat-stable, FE-dependent alcohol dehydrogenase for aldehyde detoxification},
author = {Elkins, James G. and Clarkson, Sonya},
abstractNote = {The present invention relates to microorganisms and polypeptides for detoxifying aldehydes associated with industrial fermentations. In particular, a heat-stable, NADPH- and iron-dependent alcohol dehydrogenase was cloned from Thermoanaerobacter pseudethanolicus 39E and displayed activity against a number of aldehydes including inhibitory compounds that are produced during the dilute-acid pretreatment process of lignocellulosic biomass before fermentation to biofuels. Methods to use the microorganisms and polypeptides of the invention for improved conversion of bio mass to biofuel are provided as well as use of the enzyme in metabolic engineering strategies for producing longer-chain alcohols from sugars using thermophilic, fermentative microorganisms.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Tue Apr 24 00:00:00 EDT 2018},
month = {Tue Apr 24 00:00:00 EDT 2018}
}

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