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Homologous overexpression of hydrogenase and glycerol dehydrogenase in Clostridium pasteurianum to enhance hydrogen production from crude glycerol.

08:00 EDT 16th March 2019 | BioPortfolio

Summary of "Homologous overexpression of hydrogenase and glycerol dehydrogenase in Clostridium pasteurianum to enhance hydrogen production from crude glycerol."

This study reports engineering of a hypertransformable variant of C. pasteurianum for bioconversion of glycerol into hydrogen (H). A functional glycerol-triggered hydrogen pathway was engineered based on two approaches: (1) increasing product yield by overexpression of immediate enzyme catalyzing H production, (2) increasing substrate uptake by overexpression of enzymes involved in glycerol utilization. The first strategy aimed at overexpression of hydA gene encoding hydrogenase, and the second one, through combination of overexpression of dhaD1 and dhaK genes encoding glycerol dehydrogenase and dihydroxyacetone kinase. These genetic manipulations resulted in two recombinant strains (hydA/dhaD1K) capable of producing 97% H (v/v), with yields of 1.1 mol H/mol glycerol in hydA overexpressed strain, and 0.93 mol H/mol glycerol in dhaD1K overexpressed strain, which was 1.5 fold higher than wild type. Among two strains, dhaD1K consumed more glycerol than hydA which proves that overexpression of glycerol enzymes has enhanced glycerol intake rate.

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This article was published in the following journal.

Name: Bioresource technology
ISSN: 1873-2976
Pages: 168-177

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Medical and Biotech [MESH] Definitions

A non-heme iron-sulfur protein isolated from Clostridium pasteurianum and other bacteria. It is a component of NITROGENASE along with molybdoferredoxin and is active in nitrogen fixation.

A non-heme iron-sulfur protein isolated from Clostridium pasteurianum and other bacteria. It is a component of NITROGENASE, which is active in nitrogen fixation, and consists of two subunits with molecular weights of 59.5 kDa and 50.7 kDa, respectively.

An NAD-dependent enzyme that catalyzes the oxidation of sn-glycerol 3-phosphate to glycerone phosphate.

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A species of gram-positive bacteria in the family Clostridiaceae. Its GLUTAMATE DEHYDROGENASE is commonly used in research.

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