Eureka AIR delivers breakthrough ideas for toughest innovation challenges, trusted by R&D personnel around the world.
Process for the production of beta-lysine
What is Al technical title?
Al technical title is built by PatSnap Al team. It summarizes the technical point description of the patent document.
A lysine and aspartokinase technology, applied in the field of recombinant microorganisms, can solve the problems of time-consuming and expensive raw materials
Inactive Publication Date: 2009-04-01
BASF SE
View PDF6 Cites 7 Cited by
Summary
Abstract
Description
Claims
Application Information
AI Technical Summary
This helps you quickly interpret patents by identifying the three key elements:
Problems solved by technology
Method used
Benefits of technology
Problems solved by technology
However, the chemical synthesis of β-lysine is time-consuming, requires expensive starting materials, and produces a racemic mixture
Method used
the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more
Image
Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
Click on the blue label to locate the original text in one second.
Reading with bidirectional positioning of images and text.
Smart Image
Examples
Experimental program
Comparison scheme
Effect test
Embodiment
[0060] 1. Cloning of the proximal Clostridium lysine 2,3-aminomutase gene
[0061] According to the conserved regions upstream and downstream of the lysine 2,3-aminomutase genes of Fusobacterium nucleatum and Thermoanaerobacter tengcongensis, a set of oligonucleotide primers were designed for In the isolation of the proximal Clostridium lysine 2,3-aminomutase gene (kamA). Using PCR primers WKJ90 / WKJ65 and WKJ68 / WKJ93, and using the chromosome of Clostridium axeum as a template, the DNA fragments of the upstream and downstream regions, including the N-terminal and C-terminal sequences of the kamA gene, were amplified, respectively. After the sequence analysis of the amplified DNA fragment is completed, it is purified to obtain a product containing the start and end sequences of the kamA structural region. Based on the determined upstream and downstream sequences, PCR primers WKJ105 / WKJ106 were synthesized for isolating the full sequence of the Clostridium proximal kamA gene. ...
the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More
PUM
Login to View More
Abstract
Process for the production of -lysine by constructing a recombinant microorganism which has a deregulated lysine 2,3-aminomutase gene and at least one deregulated gene selected from the group (i) which consists of aspartokinase, aspartatesemialdehyde dehydrogenase, dihydrodipicolinate synthase, dihydrodipicolinate reductase, tetrahydrodipicolinate succinylase, succinyl-amino-ketopimelate transaminase, succinyl-diamino-pimelate desuccinylase, diaminopimelate epimerase, diaminopimelate dehydrogenase, arginyl-tRNA synthetase, diaminopimelate decarboxylase, pyruvate carboxylase, phosphoenolpyruvate carboxylase, glucose-6-phosphate dehydrogenase, transketolase, transaldolase, 6-phosphogluconolactonase, fructose 1,6-biphosphatase, homoserine dehydrogenase, phophoenolpyruvate carboxykinase, succinyl-CoA synthetase, methylmalonyl-CoA mutase, provided that if aspartokinase is deregulated as gene (i) at least a second gene (i) other than aspartokinase has to be deregulated, and cultivating said microorganism.
Description
technical field [0001] The present invention relates to a method for producing β-lysine. More specifically, the present invention relates to the use of recombinant microorganisms comprising deregulated forms of DNA molecules necessary for the production of β-lysine. Background technique [0002] Although β-amino acids are rare compared to the corresponding α-amino acids, they still occur in nature both in free form and in polypeptides. Cardillo and Tomasini, Chem. Soc. Rev. 25:77 (1996); Sewald, Amino Acids 11:397 (1996). Since β-amino acids are stronger bases and weaker acids than the corresponding α-amino acids, polypeptides containing β-amino acids instead of α-amino acids have different backbone atom patterns, leading to new properties. [0003] In the 1950s, L-β-lysine was identified in several strongly basic peptide antibiotics produced by Streptomyces. Antibiotics that produce L-β-lysine by hydrolysis include puromycin, aflatoxin A, violacein, rosethricin, and dext...
Claims
the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More
Application Information
Patent Timeline
Application Date:The date an application was filed.
Publication Date:The date a patent or application was officially published.
First Publication Date:The earliest publication date of a patent with the same application number.
Issue Date:Publication date of the patent grant document.
PCT Entry Date:The Entry date of PCT National Phase.
Estimated Expiry Date:The statutory expiry date of a patent right according to the Patent Law, and it is the longest term of protection that the patent right can achieve without the termination of the patent right due to other reasons(Term extension factor has been taken into account ).
Invalid Date:Actual expiry date is based on effective date or publication date of legal transaction data of invalid patent.