Methods for increasing carbon-based chemical product yield in an organism by genetically modifying one or more genes involved in a stringent response and/or in a regulatory network, nonnaturally occurring organisms having increased carbon-based chemical product yield, and methods for use in production of carbon-based chemical products are provided.

Disclosed herein are methods for production of 2-phenylethanol by microbial fermentation of substrates comprising carbon monoxide and/or carbon dioxide and further disclosed are genetically modified microorganisms for use in such methods. Additionally, the processes disclosed herein are improved methods of 2-PE production that alleviate dependence on natural and petrochemical processes.

Provided are a polynucleotide having promoter activity and an application of the polynucleotide in producing an amino acid. Also disclosed are a transcription expression cassette, a recombinant expression vector, and a recombinant host cell which contain the polynucleotide, and a method for enhancing expression of a target gene, a method for preparing a protein, and a method for producing an amino acid. The polynucleotide having the promoter activity is a mutant of a polynucleotide having the sequence as shown in SEQ ID NO: 9. Compared with the polynucleotide having the sequence as shown in SEQ ID NO: 9, the promoter activity of the mutant is significantly enhanced, thereby promoting the stable and efficient expression of the target gene.

A novel method of producing high-purity hydroxy-L-pipecolic acids in an efficient and inexpensive manner while suppressing the production of hydroxy-L-proline is provided. The method includes allowing an L-pipecolic acid hydroxylase, a microorganism or cell having the ability to produce the enzyme, a processed product of the microorganism or cell, and/or a culture liquid comprising the enzyme and obtained by culturing the microorganism or cell, to act on L-pipecolic acid as a substrate in the presence of 2-oxoglutaric acid and ferrous ion, wherein the L-pipecolic acid hydroxylase has the properties: (1) the enzyme can act on L-pipecolic acid in the presence of 2-oxoglutaric acid and ferrous ion to add a hydroxy group to the carbon atom at positions 3, 4, and/or 5 of L-pipecolic acid; and (2) the enzyme has a catalytic efficiency (kcat/Km) with L-proline that is equal to or less than 7 times the catalytic efficiency (kcat/Km) with L-pipecolic acid.

Application of glutamate dehydrogenase GdhA of Peptostreptococcus asaccharolyticus in increasing the yield of poly-γ-glutamic acid from Bacillus licheniformis. The glutamate dehydrogenase GdhA of the Bacillus licheniformis WX-02 per se is replaced with the glutamate dehydrogenase derived from the Peptostreptococcus asaccharolyticus by means of homologous recombination, which significantly increases the level of synthesizing the poly-γ-glutamic acid for the Bacillus licheniformis, and the yield of the obtained poly-γ-glutamic acid from strains is increased at least by more than 20% compared with control strains.

The present invention relates to a secretagogue compound derived from oxalate degrading bacteria, for use in the treatment of an oxalate related disease and/or oxalate related imbalance in a subject, wherein the administration of the secretagogue results in a reduction of urinary oxalate and/or plasma oxalate in the subject. The invention further relates to a pharmaceutical composition comprising such a secretagogue compound, a method for treating a subject suffering from an oxalate related disease, and to a method for preparing a secretagogue.

An aqueous composition includes (i) glutamate dehydrogenase from a bacterium of the Clostridium genus, (ii) a stabilizing compound that is a carboxylic acid having a carbon-based chain of at least three carbon atoms and comprising at least two —COOH groups, or a salt thereof, and (iii) any of a monosaccharide polyol, disaccharide polyol, or polymeric macromolecule in addition to the glutamate dehydrogenase. A process for stabilizing the glutamate dehydrogenase in order to maintain antigenic properties of the glutamate dehydrogenase includes stabilizing the glutamate dehydrogenase in the aqueous composition and maintaining the antigenic properties of the glutamate dehydrogenase during storage of the aqueous composition.

An enzymatic electrochemical method for the quantification of analytes in isolated samples of biological fluids based on a dual biosensor strip electrochemical system. The sample is analyzed in parallel using first and second different biosensor test strips (blank and complete) and the results are obtained by subtracting a response obtained in the electrodes of the first biosensor test strip from a response obtained in the electrodes of the second biosensor test strip, thus eliminating the effect of interferences and isolating the signal corresponding only to the analyte determination.

A novel method of producing high-purity hydroxy-L-pipecolic acids in an efficient and inexpensive manner while suppressing the production of hydroxy-L-proline is provided. The method includes allowing an L-pipecolic acid hydroxylase, a microorganism or cell having the ability to produce the enzyme, a processed product of the microorganism or cell, and/or a culture liquid comprising the enzyme and obtained by culturing the microorganism or cell, to act on L-pipecolic acid as a substrate in the presence of 2-oxoglutaric acid and ferrous ion, wherein the L-pipecolic acid hydroxylase has the properties: (1) the enzyme can act on L-pipecolic acid in the presence of 2-oxoglutaric acid and ferrous ion to add a hydroxy group to the carbon atom at positions 3, 4, and/or 5 of L-pipecolic acid; and (2) the enzyme has a catalytic efficiency (kcat/Km) with L-proline that is equal to or less than 7 times the catalytic efficiency (kcat/Km) with L-pipecolic acid.

The present invention discloses an amino acid dehydrogenase mutant and application thereof in synthesizing L-glufosinate-ammonium, the amino acid dehydrogenase mutant is obtained by a single mutation or a multi-site mutation of the amino acid at position 95, 108, 172, 303 of the amino acid sequence shown in SEQ ID No.2. The amino acid dehydrogenase mutant DyGDH-F95I-A108T-R172P-R303H prepared by the present invention has a specific enzyme activity that is 33 times higher than that of the original Aldo-keto reductase, and the concentration of the largest substrate, 2-carbonyl-4-(hydroxymethylphosphinyl)-butyric acid reaches 500 mM, the amino acid dehydrogenase mutant has more industrial application prospects. Using the amino acid dehydrogenase mutant to produce L-glufosinate-ammonium, the reaction time is significantly shortened, the general process takes 20 hours, and the reaction time of the present invention only requires 120 minutes, which shows that the amino acid dehydrogenase mutant has a good industrial application prospect.