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Biosynthetic production of acyl amino acids

An amino acid, a technology for producing acyl glycinate, applied in the directions of microorganism-based methods, microorganisms, acyltransferases, etc., can solve problems such as non-technical feasibility, achieve high-efficiency biotechnology approaches, and improve yield and purity.

Inactive Publication Date: 2017-08-18
EVONIK DEGUSSA GMBH
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Since the mixtures contain compounds that are highly related in chemical structure, it is often not technically feasible to purify or at least enrich a single component in an efficient and straightforward manner

Method used

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  • Biosynthetic production of acyl amino acids
  • Biosynthetic production of acyl amino acids
  • Biosynthetic production of acyl amino acids

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0162] California Umbrella Gene wxya Preparation of the expression vector

[0163] In order to prepare the california laurel encoding californoyl-CoA-thioesterase wxya The expression vector of the gene (SEQ ID NO: 1), which is codon-optimized for expression in Escherichia coli. The gene and tac The promoter (SEQ ID NO: 2) was synthesized together, and at the same time, a cleavage site was introduced upstream of the promoter and a cleavage site downstream of the terminator. The synthetic DNA fragment P tac -synUcTE with restriction endonuclease Bam H I and not I digested and ligated into correspondingly cut vector pJ294 (DNA2.0 Inc., Menlo Park, CA, USA). The completed E. coli expression vector was named pJ294[Ptac-synUcTE] (SEQ ID NO:3).

Embodiment 2

[0165] Escherichia coli fadD Preparation of co-expression vectors with Homo sapiens genes hGLYAT3 and hGLYAT2

[0166] In order to prepare the Homo sapiens gene hGLYAT2 (SEQ ID NO:4) or hGYLAT3 (SEQ ID NO:5) encoding human glycine-N-acyltransferase and Escherichia coli encoding Escherichia coli acyl-CoA synthetase fadD (SEQ ID NO: 6) co-expression vector, codon-optimized and synthesized genes hGLYAT2 and hGLYAT3 for expression in Escherichia coli. Synthetic DNA fragments were treated with restriction endonucleases Sac II and Eco 47III digested and ligated into the correspondingly cleaved removed aftA 1 gene in pCDF[atfA1_Ab(co_Ec)-fadD_Ec] (SEQ ID NO:7). Sequence segments that would otherwise be removed during this process are co-synthesized during gene synthesis. This vector is a pCDF derivative that already contains a synthetic tac promoter (SEQ ID NO:2) and E. coli fadD Gene. The resulting expression vectors were named pCDF{Ptac}[hGLYAT2(co_Ec)-fadD_Ec] (SEQ I...

Embodiment 3

[0168] Homo sapiens hGLYAT2, Escherichia coli fadD and Pseudomonas putida ( Pseudomonas putida ) Preparation of co-expression vector of alkL gene

[0169] To prepare a co-expression vector of the hGLYAT2 gene and the modified Pseudomonas putida alkL gene encoding AlkL, an outer membrane protein that facilitates the import of hydrophobic substrates into the cell, with the aid of sequence-specific oligonucleotides acid, the alkL gene (SEQ ID NO: 10) was amplified from plasmid pCDF[alkLmod1] (SEQ ID NO: 12) together with the lacuv5 promoter (SEQ ID NO: 11). restriction endonuclease Bam HI and Nsi I cut and ligated into the correspondingly cut vector pCDF{Ptac}[hGLYAT2(co_Ec)-fadD_Ec] (SEQ ID NO:8). The correct insertion of the target gene is checked by restriction analysis and the authenticity of the introduced gene is verified by DNA sequencing. The resulting expression vector was named pCDF{Ptac}[hGLYAT2(co_Ec)-fadD_Ec]{Placuv5}[alkLmod1] (SEQ ID NO: 13).

[0170] The f...

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Abstract

The present invention relates to a cell for producing acyl glycinateswherein the cell is genetically modified to comprise -at least a first genetic mutation that increases the expression relative to the wild type cell of an amino acid-N-acyl-transferase, -at least a second genetic mutation that increases the expression relative to the wild type cell of an acyl-CoA synthetase, and -at least a third genetic mutation that decreases the expression relative to the wild type cell of at least one enzyme selected from the group consisting of an enzyme of the glycine cleavage system, glycine hydroxymethyltransferase (GlyA) and threoninealdolase (LtaE).

Description

technical field [0001] The present invention relates to biotechnological methods and cells for the production of at least one acylamino acid. In particular, the acyl amino acid is an acyl glycinate from at least one fatty acid. Background technique [0002] Acyl amino acids are a class of surfactants that have a variety of uses such as detergents for washing purposes, emulsifiers in food products, and as various personal care products such as shampoos, soaps, moisturizers, etc. Basic ingredients. In addition to having a hydrophobic region and a hydrophilic region (a prerequisite for use as a surfactant), the compounds are made from naturally occurring molecules (more specifically, amino acids and fatty acids) that are not only harmless but environmentally friendly acceptable, but can be readily produced on a large scale using inexpensive biological feedstocks. Acylamino acids are used as neuromodulators and probes for new drug targets in pharmacological research. [0003...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12N1/21C12N9/00C12N9/10C12N9/88C12P13/04C12R1/19
CPCC12N9/1014C12N9/1029C12N9/88C12N9/93C12P13/04C12Y203/01012C12Y203/01016C12Y203/01194C12Y602/01003C12Y602/0101C12Y602/01015C12Y602/0102C12P13/02C12Y201/02001C12Y602/01C12Y203/01065C12Y401/02005C12Y602/01001C12P13/005
Inventor L.赖内克S.沙费尔K.格拉曼M.奥尔费尔特N.德克N.阿尔托H-G.亨内曼
Owner EVONIK DEGUSSA GMBH
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