A method for producing a recombinant protein of interest (POI) is provided, comprising the steps of (a) culturing cells in a cell culture medium to express said POI by adding a feed comprising at least one substrate to said cell culture, (b) applying a feeding strategy based on calculating, setting and optionally controlling the specific substrate uptake rate q.sub.s of the cells during the induction phase and/or production phase of the POI, wherein q.sub.s is set to be close to the maintenance rate of the cell culture; and (c) isolating said POI from the cell culture.

The present invention is within the field of industrial protein production. The invention provides a novel expression system using dehydroorotate dehydrogenase (DHODH) as a selection marker in combination with leflunomide or a metabolite thereof, notably for use in mammalian cell lines. Expression vectors encoding DHODH, cell lines comprising said vectors and methods of producing recombinant proteins are also provided.

Provided is a technique for highly expressing a target protein in a plant cell by using a glycosylation domain, a recombinant vector comprising a gene encoding a fusion protein of a glycosylation domain and a target protein, a recombinant cell, a transformed plant, and a method of producing a target protein using these.

A method is used for producing a modified non-ribosomal peptide, e.g. a modified microcystin and/or modified nodularin (together CA), including the steps of: a) growing a modified non-ribosomal peptide producing cyanobacteria strain in a culture media, h) adding one or more modified substrates, preferably modified amino acids to said culture, and c) inoculating the non-ribosomal peptide, producing strain the presence of said modified substrates. The thus modified non-ribosomal peptide may be used for the therapy of various diseases.

A bacteria referred to here as Bacillus subtilis 6A-1 is provided, compositions thereof and processes for use of the bacteria, spores, cells, extracts and enzymes. The compositions which comprise the bacteria, spores, cells, extracts and/or enzymes are capable of degrading polysaccharides. Such compositions are capable of degrading cellulose, including plant-produced cellulose, microcrystalline cellulose and carboxymethyl cellulose. The bacteria produces at least two cellulose-degrading protein fractions. Cellulose degrading activity continues across pH2 to pH13.

Provided is a technique for highly expressing a target protein in a plant cell by using a glycosylation domain, a recombinant vector comprising a gene encoding a fusion protein of a glycosylation domain and a target protein, a recombinant cell, a transformed plant, and a method of producing a target protein using these.

The present disclosure relates to tagatose-6-phosphate phosphatase consisting of an amino acid sequence of SEQ ID NO: 1, a nucleic acid encoding the tagatose-6-phosphate phosphatase, and a transformant comprising the nucleic acid. Additionally, the present disclosure relates to a composition for producing tagatose, which comprises the tagatose-6-phosphate phosphatase of the present disclosure, and a method for producing tagatose using the tagatose-6-phosphate phosphatase of the present disclosure.

The present disclosure provides a system to produce soluble, folded, and post-translationally modified proteins. The system includes a fusion protein comprising a catalytic domain of an enzyme involved in post-translational protein modification and a targeting domain, and a substrate protein comprising a protein of interest and a sequence that interacts with the targeting domain. The present disclosure also provides polynucleotide sequences encoding fusion proteins and substrate proteins, vectors for expressing polynucleotide sequences, vectors comprising the polynucleotide sequences, and isolated cells comprising said vectors.

The invention belongs to the technical field of polypeptide preparation methods, and in particular relates to a preparation method of a liraglutide intermediate polypeptide GLP-1 (7-37). In the preparation method, main steps include constructing recombinant liraglutide engineered bacteria via E. coli to induce expression of a liraglutide intermediate fusion protein in the form of inclusion bodies, and performing denaturation, renaturation, enzyme digestion, separation and purification to obtain the liraglutide intermediate polypeptide GLP-1 (7-37). The invention alters expression pattern into the expression of the intracellular insoluble inclusion bodies by changing a signal peptide of the recombinant sequence to increase significantly expression level. The liraglutide intermediate polypeptide prepared by the invention has a purity up to 87% or more and a yield of more than 85%.

Provided are binding polypeptides (e.g., antibodies), and drug conjugates thereof, comprising an Fc domain with an altered glycosylation profile and reduced effector function. In particular embodiment, the Fc domain comprises: an asparagine residue at amino acid position 298, according to EU numbering; and a serine or threonine residue at amino acid position 300, according to EU numbering. Also provided are nucleic acids encoding the antigen-binding polypeptides, recombinant expression vectors and host cells for making such antigen-binding polypeptides. Methods of using the antigen-binding polypeptides disclosed herein to treat disease are also provided.