Microorganisms for n-propanol production

A technology of n-propanol and recombinant host cells, applied in fermentation, bacteria, etc.

Inactive Publication Date: 2014-05-14
NOVOZYMES AS
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, unlike polyethylene, the generation of polyethylene s

Method used

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  • Microorganisms for n-propanol production
  • Microorganisms for n-propanol production
  • Microorganisms for n-propanol production

Examples

Experimental program
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Effect test

Embodiment 1

[0436] Example 1: Cloning of Clostridium acetobutylicum Thiolase Gene and Construction of Vector pTRGU51

[0437] The 1176 bp coding sequence (CDS) of the thiolase gene identified in Clostridium acetobutylicum was optimized for expression in E. coli and synthetically constructed into pTRGU51. A DNA fragment containing a codon-optimized CDS was designed to have a ribosome binding site (RBS, sequence 5'-GAAGGAGATATACC-3') immediately before the start codon. The resulting sequence was then submitted to and synthesized by Geneart AG (Regenburg, Germany) and delivered into a pMA backbone vector containing the β-lactamase encoding gene blaTEM-1. When synthesized, the CDS and RBS fragments are flanked by restriction sites to facilitate subsequent cloning steps. The entire synthetic fragment cloned into the pMA vector was EcoRI-RBS-CDS-STOP-BamHI-XbaI resulting in pTRGU51.

[0438] The wild-type nucleotide sequence (WT) and deduced amino acid sequence of the Clostridium acetobutylic...

Embodiment 2

[0439] Embodiment 2: Bacillus subtilis succinyl CoA: the cloning of acetoacetate transferase gene and the construction of vector pTRGU58 and pTRGU59

[0440] The 699bp coding sequence (CDS) of the scoA subunit of the subtilis succinyl CoA: acetoacetate transferase gene and the 648bp coding sequence of the scoB subunit of the subtilis succinyl CoA: acetoacetate transferase gene are optimized for use in the large intestine Bacteria and were synthetically constructed into pTRGU58 and pTRGU59, respectively. Each DNA fragment containing a codon-optimized CDS was designed with a ribosome binding site and synthesized by Geneart AG (Regenburg, Germany) as described in Example 1 with the modified restriction sites shown below point. The entire synthetic fragment containing scoA cloned into the pMA vector was EcoRI-BamHI-RBS-scoA-STOP-NotI-XbaI resulting in pTRGU58. The entire synthetic fragment containing scoB cloned into the pMA vector was EcoRI–NotI–RBS–scoB–STOP–HindIII–XbaI, and ...

Embodiment 4

[0448] Example 4: Cloning of Clostridium beijerinckii acetoacetate decarboxylase gene and construction of vector pTRGU62

[0449] The 738 bp coding sequence (CDS) of the acetoacetate decarboxylase gene of C. beijerinckii was optimized for expression in E. coli and synthetically constructed into pTRGU62. A DNA fragment containing a codon-optimized CDS was designed with a ribosome binding site and synthesized by Geneart AG as described in Example 1 with the modified restriction sites shown below. The entire synthetic fragment cloned into the pMA vector was EcoRI-HindIII-RBS-CDS-STOP-AscI-XbaI resulting in pTRGU62.

[0450] The wild-type nucleotide sequence (WT) and deduced amino acid sequence of C. beijerinckii acetoacetate decarboxylase correspond to SEQ ID NO: 47 and 48, respectively. The coding sequence is 741 bp, including the stop codon, and the encoded predicted protein is 246 amino acids. No signal peptide was predicted in this sequence using the SignalP program (Nielse...

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Abstract

Described herein are host cells comprising lactate dehydrogenase activity, lactaldehyde dehydrogenase activity, lactaldehyde reductase activity, propanediol dehydratase activity, and/or n-propanol dehydrogenase activity, wherein the cells are capable of producing n-propanol. Also described are methods of producing n-propanol comprising (a) cultivating the host cells having lactate dehydrogenase activity, lactaldehyde dehydrogenase activity, lactaldehyde reductase activity, propanediol dehydratase activity, and/or n-propanol dehydrogenase activity in a medium under suitable conditions to produce n-propanol; and (b) recovering the n-propanol. Methods of producing polypropylene from the recombinant n-propanol are also provided.

Description

[0001] Cross References to Related Applications [0002] This application claims the benefit of priority to US Provisional Application No. 61 / 490,989, filed May 27, 2011, and US Provisional Application No. 61 / 490,995, filed May 27, 2011. The entire contents of these applications are incorporated herein by reference. [0003] Sequence listing involved [0004] This application contains a Sequence Listing in computer readable form, which is hereby incorporated by reference. Background of the invention [0005] Concerns about future oil supplies have spurred research in the field of renewable energy and other renewable sources of raw materials. Biofuels, such as ethanol, and bioplastics, such as polylactic acid in particular, are examples of products that can be produced directly from agricultural sources using microorganisms. Other desired products can then be obtained using non-enzymatic chemical transformations, such as the dehydration of ethanol to ethylene. [0006] Poly...

Claims

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Application Information

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IPC IPC(8): C12N1/20
CPCC12N1/20C12P5/026C12P7/04
Inventor P.奥尔森L.克里斯坦森S.乔尔根森T.雷圭拉B.克里斯坦森B.柯布曼T.格罗特克耶尔
Owner NOVOZYMES AS
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