C12R1/15

RamA transcription factor mutant for promoting production of N-acetylglucosamine and use thereof

The present invention discloses a RamA transcription factor mutant for promoting the production of N-acetylglucosamine and use thereof. The mutant is obtained by mutating lysine at position 90 to asparagine and serine at position 92 to lysine in a parent having an amino acid sequence as shown in SEQ ID NO: 2. The present invention provides a genetically engineered strain that overexpresses the RamA transcription factor mutant and increases the production of N-acetylglucosamine. By overexpressing the transcription factor RamA that is involved in the regulation of carbon metabolism, the extracellular accumulation of N-acetylglucosamine is increased, with a maximum concentration reaching 31.5 g/L, which lays a foundation for further metabolic engineering of Corynebacterium glutamicum to produce glucosamine. The method for constructing recombinant Corynebacterium glutamicum of the invention is simple, and convenient in use, and thus has good application prospects.

Method for preparing immobilized arginine deiminase (ADI) and producing [.SUP.14/15.N]-L-citrulline

Arginine deiminase (ADI)-containing genetically engineered Corynebacterium glutamicum (C. glutamicum), a fusion protein cipA-arc, use thereof, and a method for preparing [.sup.14/15N]-L-citrulline through enzymatic catalysis are provided. The ADI-containing genetically engineered Corynebacterium glutamicum (C. glutamicum) has a deposit number of CGMCC No. 19404, which expresses a fusion protein cipA-arc. Both the genetically engineered strain and the fusion protein cipA-arc can be used to convert [.sup.14/15N]-L-arginine into [.sup.14/15N]-L-citrulline.

Method for increasing the production of small molecules in submerged <i>Corynebacterium </i>culture

Described are methods for increasing the production of small molecules in a submerged Corynebacterium culture by supplementing Corynebacterium growth medium with the non-enzymatic fraction of spent Trichoderma fermentation broth.

Microorganism of <i>Corynebacterium </i>genus having enhanced L-arginine or L-citrulline productivity and a method for producing L-arginine or L-citrulline using the same

The present disclosure relates to a Corynebacterium sp. mutant strain having increased L-arginine or L-citrulline productivity and a method of producing L-arginine or L-citrulline using the same. The Corynebacterium sp. mutant strain has enhanced activity of acetylornithine aminotransferase involved in the L-arginine biosynthesis pathway, and thus is capable of producing L-arginine or L-citrulline productivity in an increased yield compared to a parent strain.

BLUE PIGMENT AND BIOSYNTHESIS METHOD THEREOF
20250354185 · 2025-11-20 ·

The present application relates to the technical field of biocatalysis and biosynthesis, and specifically discloses a blue pigment and a biosynthesis method thereof. In the present application, an indigoidine synthetase and a 4-phosphopantetheinyl transferase are expressed by a metabolically engineered strain to catalyze the biosynthesis of the blue pigment N-acetyl-indigoidine from glutamine and N-acetylglutamine, and a molecular structure of the blue pigment is inferred by mass spectrometry, nuclear magnetic resonance spectroscopy, etc. The present application achieves the catalytic synthesis of N-acetyl-indigoidine from glutamine and N-acetylglutamine in Escherichia coli (E. coli), Corynebacterium glutamicum (C. glutamicum), Saccharomyces cerevisiae (S. cerevisiae), and Streptomyces. Compared with indigoidine, N-acetyl-indigoidine has a maximum absorption wavelength of 584 nm, and a stable color having high brightness that is not easy to fade. Thus, the blue pigment shows an extensive application range and a promising industrial production prospect.

Modified polypeptide with attenuated activity of citrate synthase and method for producing L-amino acid using the same

The present disclosure relates to a modified polypeptide with attenuated activity of citrate synthase, a microorganism producing leucine comprising the modified polypeptide, and a method for producing an L-amino acid using the microorganism.

Isopropylmalate synthase variant and a method of producing L-leucine using the same

The present disclosure relates to an isopropylmalate synthase variant and a method of producing L-leucine using the same.

Microorganism of <i>Corynebacterium </i>genus having enhanced L-arginine or L-citrulline productivity and a method for producing L-arginine or L-citrulline using the same

The present disclosure relates to a Corynebacterium sp. mutant strain having increased L-arginine or L-citrulline productivity and a method of producing L-arginine or L-citrulline using the same. The Corynebacterium sp. mutant strain has enhanced activity of acetylglutamate kinase involved in the L-arginine biosynthesis pathway, and thus is capable of producing L-arginine or L-citrulline in an increased yield compared to a parent strain.

Mutant of <i>Corynebacterium glutamicum </i>with enhanced l-glutamic acid productivity and method for preparing l-glutamic acid using the same

The present invention relates to a Corynebacterium glutamicum mutant strain having increased L-glutamic acid productivity, a method for constructing the same, and a method of producing L-glutamic acid using the same. The Corynebacterium glutamicum mutant strain is a strain into which a mechanosensitive ion channel gene derived from a Corynebacterium sp. strain has been introduced, and thus it can produce L-glutamic acid in an improved yield due to enhancement of glutamic acid release. Therefore, when the mutant strain is used, it is possible to more effectively produce L-glutamic acid.

Genetically modified microorganism for production of aspartic acid and downstream metabolites from aspartic acid as target substance, and method for producing target substance using same
12600991 · 2026-04-14 · ·

The present disclosure relates to a genetically modified microorganism satisfying some of predetermined conditions. The predetermined conditions include: (I) succinate dehydrogenase activity or fumarate reductase activity being reduced or inactivated relative to a wild-type microorganism; (II) lactate dehydrogenase activity being reduced or inactivated relative to the wild-type microorganism; (III) the genetically modified microorganism having modified phosphoenolpyruvate carboxylase activity showing resistance to feedback inhibition by aspartic acid in wild-type phosphoenolpyruvate carboxylase activity, or exogenous phosphoenolpyruvate carboxylase activity having higher resistance to feedback inhibition by aspartic acid than that of the wild-type phosphoenolpyruvate carboxylase activity shown by the wild-type microorganism; and (IV) pyruvate:quinone oxidoreductase being reduced or inactivated relative to the wild-type microorganism.