A recombinant human type XVII collagen consists of an amino acid sequence shown in (A).sub.n or includes the amino acid sequence shown in (A).sub.n, where A is a sequence set forth in SEQ ID NO: 2, a sequence undergoing an amino acid modification to a predetermined extent based on SEQ ID NO: 2, or a sequence that has more than 80% homology with SEQ ID NO: 2; n is an integer greater than or equal to 1; and A represents a basic unit, and when there are two or more basic units, the two or more basic units are identical or different and are directly connected in tandem through a peptide bond. In the present disclosure, it is confirmed that the recombinant human type XVII collagen can undergo efficient secretory and soluble expression in eukaryotic host cells such as Pichia pastoris (P. pastoris).

Provided herein are recombinant nucleic acid molecules, nucleic acid constructs, fusion enzymes, transformed host cells, and methods for making aroma compounds alpha-ionone or beta-ionone.

The present invention relates to the fields of life sciences, genetics and regulation of gene expression. Specifically, the invention relates to a non-viral transcription activation domain for a eukaryotic host. Also, the present invention relates to a polypeptide or artificial transcription factor comprising the transcription activation domain of the present invention. And furthermore, the present invention relates to a polynucleotide, an expression cassette, expression system, and/or a eukaryotic host. Still, the present invention relates to a method for producing a desired protein product in the eukaryotic host of the present invention or to a method of preparing a non-viral transcription activation domain of the present invention or a polynucleotide encoding said non-viral transcription activation domain. And still further, the present invention relates to use of the transcription activation domain, polypeptide, artificial transcription factor, polynucleotide, expression cassette, expression system or eukaryotic host of the present invention for metabolic engineering and/or production of a desired protein product.

The present invention relates to a composition comprising a 3D printed hydrogel, wherein at least two different populations of cells are embedded in the 3D printed hydrogel. The different populations of cells can produce one or more products. The 3D printed hydrogel can be lyophilized and rehydrated, and the cells can continue to produce the product. Also disclosed are methods of producing a product, and methods of producing a 3D printed hydrogel comprising different populations of cells.

The disclosure relates cells or cellular systems that express both a membrane protein and a binding domain directed to the membrane protein. Also, methods are provided that use such cells or cellular systems to produce higher amounts of the membrane proteins. Further, the cells or cellular systems can be used as tools for the structural and functional characterization of membrane proteins, as well as for screening and drug discovery efforts targeting membrane proteins.

The present disclosure describes the engineering of microbial cells for fermentative production of cystathionine and provides novel engineered microbial cells and cultures, as well as related cystathionine production methods. An engineered microbial cell that expresses a heterologous cystathionine beta-synthase or a heterologous cystathionine gamma-synthase, wherein the engineered microbial cell produces cystathionine.

The current invention relates to recombinant vectors for high protein expression. More particularly, it relates to recombinant vector having promoter sequence and terminator sequence for constitutive expression of homologous and heterologous proteins wherein the promoter sequence is selected from the group consisting of SEQ ID NO: 1 and SEQ ID NO: 2 and terminator sequence having sequence selected from the group consisting of SEQ ID NO: 3 and SEQ ID NO: 4.

A protein capable of converting chlorogenic acid into isochlorogenic acid. The protein includes or is an amino acid sequence SEQ ID No. 1, a sequence having at least 80% identity with this sequence or a fragment of this sequence. Also, a process for producing isochlorogenic acid from chlorogenic acid, which includes producing the protein and bringing it into contact with chlorogenic acid.

The disclosure discloses a genetically engineered strain for producing porcine myoglobin and fermentation and purification thereof, and belongs to the technical field of genetic engineering. The disclosure realizes efficient secretion and expression of porcine myoglobin by integrating the gene of porcine myoglobin in P. pastoris. On this basis, optimization of the medium and culture conditions of recombinant P. pastoris can significantly increase the titer of porcine myoglobin, so that the titer can reach 285.42 mg/L under fermenter conditions. In addition, by creatively adding different concentrations of ammonium sulfate to fermentation broth step by step, the purity of myoglobin obtained by final concentration is up to 88.0%, and the purification rate is up to 66.1%. The disclosure realizes efficient expression and high purification of porcine myoglobin from various steps such as synthesis, fermentation and purification of porcine myoglobin, and provides broad prospects for industrial production of porcine myoglobin.

The invention relates to the ADH3 promoter; polynucleotide sequences, vectors and expression cassettes including DNA regions responsible for the regulation of the ADH3 promoter; the host cells, including these vectors and expression cassettes, and, the recombinant proteins performed with the developed cells. In the scope of the invention, deletion analyzes in the ADH3 promoter were performed to identify regions that affect promoter strength and significant data was obtained in the formation of mutant ADH3 promoters. Deletion of the nucleotides between 539 and 638 (−361 to −262) in SEQ ID NO: 1 resulted in a 63% increase in ADH3 promoter activity. Five different synthetic promoters were created using positive regulatory regions identified and approximately 165% to 200% promoter activities were achieved with these promoters.