The present invention relates to a novel human epidermal growth factor (hEGF)-trigger factor (TF) fusion protein and a use thereof. More particularly, the human epidermal growth factor (hEGF)-trigger factor (TF) fusion protein of the present invention has fused therein: a signal peptide of a Bacillus subtilis-derived xylanase; a human epidermal growth factor (hEGF); and an Escherichia coli-derived trigger factor (TF). Therefore, the present invention not only enhances the water solubility and expression rate of a target protein, but also notably enhances useful effects such as the effects of increasing skin cell growth and healing a wound, and thus may be widely used in various industries as an active ingredient for a functional cosmetic composition and a pharmaceutical composition.

A fusion protein, an amino acid sequence thereof, a coding nucleotide sequence thereof, a preparation method thereof and a use thereof are in the technical field of agricultural biotechnology. The fusion protein contains or consists of at least three, four, five, six, seven, or eight same and/or different PAMP (Pathogen-Associated Molecular Pattern) polypeptides. Optionally, there is at least one linker or no linker between two adjacent PAMP polypeptides. A plurality of PAMP polypeptides are assembled into the fusion protein having multiple immune epitopes. The fusion protein may induce defense immune responses of plants, weaken infestation ability of pathogenic microorganisms and substantially improve the disease resistance of plants. The method for preparing the fusion protein combines technologies of PTI (PAMP-Triggered Immunity) mechanism and gene engineering to obtain the fusion protein having multiple immune epitopes can be used in preparation of plant immune PAMP polypeptides.

Described herein are engineered metabolic pathways in recombinant microorganism host cells which result in the production of 2-phenylethanol or 2-phenylacetic acid. Also described herein are methods of using the recombinant microorganisms for the production of 2-phenylethanol or 2-phenylacetic acid.

Provided in this disclosure, in some embodiments, are methods and compositions for treating maple syrup urine disease (MSUD) and other conditions characterized by excessive branched-chain amino acids.

Described herein are non-natural variants of prenyltronsfcrases having at least one amino acid substitution as compared to its corresponding natural or unmodified prenyltransferascs. The variants are capable of an increased rate of formation of prenylated aromatic compounds, such as cannabinoids, as compared to a wild type control The prcnyltransferase variants can be expressed in an engineered microbe having a pathway to such cannabinoids, and optionally can include one or more other pathway transgencs to promote formation of substrate(s) for the prcnyltransferases. Therapeutically useful cannabinoids can be purified from engineered cells and cell cultures.

The amino acid sequence of the present IL-15 analog includes the amino acid sequence of IL-15 and an amino acid sequence including at least one positively charged amino acid added to the C-terminal of the amino acid sequence of IL-15. The present IL-15 analog is highly expressed in Escherichia Coli, wherein the expression level is about 20-fold higher than that of the wild-type IL-15, and there is no significant difference in cell activity in vitro. In addition, a conjugate of the IL-15 analog improves the half-life and the long-term efficacy of the IL-15 analog by coupling with the fatty acid chain. These improvements lay a foundation for the industrialization of IL-15 protein drugs.

Related are a recombinant microorganism for producing L-valine, a construction method and an application thereof. Through transferring an amino acid dehydrogenase gene and/or activating activity of a transhydrogenase and/or a NAD kinase, reducing power of NADPH in cell is increased, the titer and yield of L-valine generated by Escherichia coli are improved, and the production of L-valine by one-step anaerobic fermentation is achieved.

Related are a recombinant microorganism for producing L-valine, a construction method and an application thereof. Through enhancing amino acid dehydrogenase activity of L-valine fermentation strain, and/or activating an Entner-Doudoroff (ED) metabolic pathway, a problem in L-valine fermentation process that reducing power is unbalanced is solved, thereby the titer and yield of L-valine produced by Escherichia coli are improved, and L-valine was produced by one-step anaerobic fermentation.

Improved production of threonine from E. coli by fermentation is accomplished by attenuation but not elimination of the expression of either or both of the yafV gene encoding omega-amidase (a.k.a. 2-oxoglutaramate amidase). In certain embodiments the strain also has attenuated expression of the ilvA gene encoding threonine dehydratase (a.k.a threonine deaminase) in cases where there is attenuated express of the ilvA gene there is no need to express an exogenous cimA gene. In examples of both cases, attenuation is accomplished by engineering these genes to contain a weaker ribosome site. Further improvements in threonine production are made by expression of a heterologous pyruvate carboxylase gene exemplified by expression of the Corynebacterium glutamicum pyc gene under control of an E. coli promoter, to provide expression of pyruvate carboxylase that is not naturally expressed in E. coli. Still further improvement is accomplished by overexpression of the rhtC gene encoding the E. coli threonine transporter protein, exemplified by inserting a stronger ribosome binding site upstream of the open reading frame for the rhtC gene.

Provided is an amino acid dehydrogenase mutant. The amino acid sequence of the mutant is obtained by mutating the amino acid sequence shown in SEQ ID NO:1. The mutation includes at least one of the following mutation sites: 64th, 94th, 133rd, 137th, 148th, 168th, 173rd, 183 rd, 191st, 207th, 229th, 248th, 255th and 282nd sites; or the amino acid sequence of the amino acid dehydrogenase mutant is an amino acid sequence having the mutation sites in the mutated amino acid sequence and having a 80% or more homology with the mutated amino acid sequence. The mutant enzyme activity is more than 50 times higher than that of wild amino acid dehydrogenase, and the enzyme specificity is also correspondingly improved.