The present disclosure relates to an L-threonine export protein variant, a microorganism including same, and a method for production of L-threonine using same.

A method for producing ectoine by fermenting recombinant Corynebacterium glutamicum. The recombinant Corynebacterium glutamicum is obtained by overexpressing, in Corynebacterium glutamicum, an aspartokinase gene lysC of which feedback inhibition is relieved, then replacing the promoter of the dihydrodipicolinate synthase in the recombinant bacterium to attenuate the activity of the dihydropyrimidine dicarboxylic acid synthase, and then transforming the recombinant bacterium with the ectoine synthetic path related gene ectABC. The recombinant Corynebacterium glutamicum can be fermented using different cheap raw materials under a low salt condition to produce ectoine, and use cheap corn slurry instead of expensive yeast powder as a nutritional component, so as to further reduce the costs of the raw materials. In addition, the recombinant Corynebacterium glutamicum solves the biosafety problem, simplifies the post-extraction process, and has a good market application prospect.

The invention provides microorganisms genetically modified to overexpress biofilm dispersal related polypeptides to enhance the production of lysine and lysine derivatives by the microorganism, method of generating such microorganism, and methods of producing lysine and lysine derivatives using the genetically modified microorganisms.

The invention relates to a plasmid, a DNA assembly method and its application recombinant strain. The plasmid has single adjacent Type IIP and Type IIS RE recognition sites. The plasmid combines the properties of Type IIP and Type IIS REs to achieve recursive cycling, SCAR-free and repeat sequence assembly.

The present disclosure relates to the field of genetic engineering, especially relates to a xylose-induced genetically engineered bacteria used for producing ectoine as well as a construction method and use thereof The genetically engineered bacteria is constructed by heterologously expressing the ectABC gene cluster from Halomonas elongata on the E. coli chromosome, using the promoter of xylose transporter coding gene xylF to control the RNA polymerase from T7 bacteriophage, reconstructing a synthesis pathway of ectoine and constructing a plasmid-free system, and enhancing the expression of target genes by a strong promoter T7; the yiled of ectoine reached 12-16 g/L after 20-28 h fermentation in shake flask, and reached 35-50 g/L after 24-40 h fermentation in a 5 L fermentor.

Provided are Corynebacterium glutamicum that produces L-lysine, a method for constructing the L-lysine producing strain, and a method for producing L-lysine from the strain. The lysine yield and glucose conversion of the L-lysine producing strain are improved, thereby reducing the production cost.

The present disclosure relates to various different types of mutations in the thrA gene in E. coli leading to enhanced lysine production for, e.g., supplements and nutraceuticals.

The present invention relates to the field of bio-production of ectoine. There is a need in the art for ectoine production methods allowing its highly efficient synthesis and secretion. The solution proposed in the present invention is the use of a genetically modified yeast comprising many modifications as described in the present text.

Provided microorganisms genetically modified to overexpress an imine/enamine deaminase to enhance the production of lysine and lysine derivatives by the microorganism. Also provided a method of generating such microorganism, and methods of producing lysine and lysine derivatives using the genetically modified microorganisms.

Provided are a polypeptide with aspartate kinase activity and the use thereof in the production of an amino acid. Specifically, provided are a novel polypeptide with aspartate kinase activity, a recombinant polypeptide, a polynucleotide, a nucleic acid construct, a recombinant expression vector, a recombinant host cell, and a method for producing an amino acid. The polypeptide with aspartate kinase activity is a mutant mutated at one or more positions corresponding to positions 293, 294 and 307 of the amino acid sequence as shown in SEQ ID NO: 1. Compared with a polypeptide having the sequence as shown in SEQ ID NO: 1, the mutant polypeptide removes the feedback inhibition of lysine on aspartate kinase, has high aspartate kinase activity, and can be used for the stable and efficient production of lysine and derivatives thereof.