Abstract: Provided is a recombinant expression vector containing a hybrid signal sequence and a method for secretory production of a human insulin-like growth factor-1 using the same. A heterologous signal sequence that significantly improves secretory expression of the human insulin-like growth factor-1 (hIGF1) is introduced into Komagataella phaffii, which is a unicellular eukaryotic cell, used as a host, such that various types of available signal sequences may be secured, and significantly improved secretion productivity may be achieved.

Abstract: Provided is a method of preparing a circular permutation (CP)-based functional recombinant human-derived fibroblast growth factor 7 and a use thereof. The fibroblast growth factor 7 to which a circular permutation is applied (CP-hFGF7115-114) is independently expressed in a host cell, such that soluble overexpression of the fibroblast growth factor 7 may be induced without causing problems according to the related art, such as lower expression level and stability compared to those of a wild-type hFGF7 protein and amino acid changes in a process of removing a fusion tag.

Abstract: An NADPH-regeneration system based on monomeric isocitrate dehydrogenase (IDH) and a use thereof. Specifically, the present invention relates to a recombinant vector including a polynucleotide encoding an isocitrate dehydrogenase recombinant protein derived from Corynebacterium glutamicum (CgIDH) and an isocitrate dehydrogenase recombinant protein derived from Azotobacter vinelandii (AvIDH), a method for producing the recombinant protein, and an NADPH-regeneration system using the recombinant protein produced by the method. The enzyme in a monomeric form that may be efficiently used in the NADPH-regeneration system in the transformant into which the recombinant vector was introduced, was found, and the NADPH-regeneration system using the enzyme in a monomeric form has a very high utility value as biological parts and biocatalyst materials that provides NADPH to the NADPH-dependent enzyme.

Abstract: A method of expressing hydrophobin in a soluble form and a method of purifying hydrophobin, and more particularly, to a method of expressing a recombinant fusion protein including hydrophobin in a soluble form in a host cell and then purifying the expressed recombinant fusion protein are provided.

Abstract: A recombinant vector according to an embodiment of the present invention may produce fibroblast growth factor 19 (FGF19) having enhanced solubility. The synonymous codon substitution variant fibroblast growth factor 19 (scvhFGF19) and chaperone ?ssDsbC may be simultaneously and independently expressed in a host cell into which the recombinant vector is introduced, thereby it is possible to overexpress the fibroblast growth factor 19 in a soluble state.

Abstract: The present invention relates to an NADPH-regeneration system based on monomeric isocitrate dehydrogenase (IDH) and a use thereof. Specifically, the present invention relates to a recombinant vector including a polynucleotide encoding an isocitrate dehydrogenase recombinant protein derived from Corynebacterium glutamicum (CgIDH) and an isocitrate dehydrogenase recombinant protein derived from Azotobacter vinelandii (AvIDH), a method for producing the recombinant protein, and an NADPH-regeneration system using the recombinant protein produced by the method. In the present invention, the enzyme in a monomeric form that may be efficiently used in the NADPH-regeneration system in the transformant into which the recombinant vector was introduced, was found, and the NADPH-regeneration system using the enzyme in a monomeric form has a very high utility value as biological parts and biocatalyst materials that provides NADPH to the NADPH-dependent enzyme.

Abstract: A recombinant vector according to an embodiment of the present invention may be used for producing a reconstituted cytochrome P450 oxygenase-reductase fusion protein. Oxygenase and reductase may be independently expressed in a host cell into which the recombinant vector is introduced, and then may be fused with a split intein so that it is possible to increase the heme content contained in the active site of the oxygenase and improve enzyme activity and stability.

Abstract: A method of expressing hydrophobin in a soluble form and a method of purifying hydrophobin, and more particularly, to a method of expressing a recombinant fusion protein including hydrophobin in a soluble form in a host cell and then purifying the expressed recombinant fusion protein are provided.

Abstract: A recombinant vector according to an embodiment of the present invention may produce fibroblast growth factor 19 (FGF19) having enhanced solubility. The synonymous codon substitution variant fibroblast growth factor 19 (scvhFGF19) and chaperone ?ssDsbC may be simultaneously and independently expressed in a host cell into which the recombinant vector is introduced, thereby it is possible to overexpress the fibroblast growth factor 19 in a soluble state, due to when not utilizing tags such as an existing fusion partner there is no change in the amino acid, which is a problem generated in the removal process.

Abstract: A recombinant vector according to an embodiment of the present invention may be used for producing a reconstituted cytochrome P450 oxygenase-reductase fusion protein. Oxygenase and reductase may be independently expressed in a host cell into which the recombinant vector is introduced, and then may be fused with a split intein so that it is possible to increase the heme content contained in the active site of the oxygenase and improve enzyme activity and stability.

Abstract: Provided is a real-time imaging method of NAPDH-dependent metabolic activity in a cell and a use thereof, and more particularly, an imaging method capable of measuring concentration gradient and change in an intracellular coenzyme using a mutant of metagenome-derived blue fluorescent protein (mBFP) in real-time and an application method thereof. In particular, the method of imaging and quantifying the coenzyme contained in various biological samples may be performed by improving fluorescence in a short time even under anaerobic conditions, without adding a substrate required for coenzyme measurement or conversion without destroying cells, and without consuming the time required for formation of a special structure (fluorophore) for generating fluorescence unlike the existing quantitative systems.