The present invention discloses an engineering yeast strain for producing nervonic acids. The yeast strain over-expresses the genes related to enzymes required in a synthetic process of long-chain unsaturated fatty acids, such as fatty acid elongase, desaturase, diacylglycerol acyltransferase and the like, and optionally, further adjusts and controls the synthesis and decomposition route of triglyceride, the synthesis and decomposition route of sphingomyelin, and the synthesis and decomposition route and the oxidation-reduction balanced route of lipid subcell levels. The recombinant yeast strain can produce microorganism oil; and the content of the prepared nervonic acids accounts for 39.6% of the total fatty acids.

An enzyme for reducing cystine to cysteine is a fusion protein that includes the protein activities of thioredoxin (protein i) having KEGG database number EC 1.8.4.8 or EC 1.8.4.10 and thioredoxin reductase (protein ii) having KEGG database number EC 1.8.1.9. The thioredoxin (protein i) is the protein activity of thioredoxin 1 from E. coli and the thioredoxin reductase (protein ii) is the protein activity of the thioredoxin reductase from E. coli. The activity of the fusion protein is at least 100% of the activity of a mixture of the same but unfused individual proteins i and ii. The fusion protein has the enzyme activity to reduce cystine to cysteine. The coding sequences (cds) responsible for the activity of protein i and ii has been fused.

An allergen inactivation method includes an inactivation step of inactivating an allergen present in a reaction system by reduction via a reduced redox protein, and a reduction process of reducing an oxidized redox protein produced by oxidation of the reduced redox protein in the inactivating to the reduced redox protein by donating an electron from an electrode connected to an external power supply outside the reaction system to the oxidized redox protein.

The present disclosure provides activated formylglycine-generating enzymes (FGE), methods of producing activated FGE, and their use in methods of producing a protein comprising a formylglycine (FGly) residue. The methods of producing activated FGE, as well as methods of use of activated FGE in producing FGly-containing proteins, include both cell-based and cell-free methods. Compositions and kits that find use, e.g., in practicing the methods of the present disclosure are also provided.

In order to produce chondroitin sulfate in an animal-free manner, engineered E. coli host cells were modified so as to reduce expression of an endogenous gene for fructosyltransferase (kfoE); reduce expression of an endogenous gene for 3′-phosphoadenosine-5′-phosphosulfate reductase (cysH); and express one or more exogenous sulfotransferases. Expression of proteins forming ATP-binding cassette transporters were also reduced to limit export of glycosaminoglycans from the cells. The recombinant microorganisms are able produce all three components identified for chondroitin sulfate production—chondroitin, sulfate donor, and sulfotransferase. These modified E. coli are capable of complete, essentially one-step biosynthesis of chondroitin sulfate at a variety of sulfation levels from simple microbial media components and glucose. This is a major advantage over current production methods that depend on the natural distribution of chondroitin sulfate types in the animal tissue.

The present disclosure relates to preparations, formulations and uses of a protein or peptide having thioredoxin action for treating diseases and/or conditions. One aspect of the invention is a method to decrease viscoelasticity of mucus or sputum in a patient that has excessively viscous or cohesive mucus or sputum. The method includes contacting the mucus or sputum of the patient with a composition comprising a protein or peptide comprising a thioredoxin monocysteinic active site, wherein the protein or peptide does not contain any cysteine residues except for a single Cys at the N-terminal position of the thioredoxin monocysteinic active site.

A method of producing sulfur-containing amino acids or derivatives of the sulfur-containing amino acids.

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 present disclosure pertains to the field peptide stapling and/or macrocyclization, where a structural motif is used to improve the properties of amino acid sequences (e.g. protease resistance, cellular penetration, biological activity). Also within the scope of the disclosure are methods for unstapling the S,S-tetrazine-containing amino acid sequence. The disclosure is also directed to methods for the reductive removal of thiocyanates from an amino acid sequence with cysteine to recycle back to the native amino acid sequence.

The present invention relates to probiotic compositions. More specifically, the present invention relates to probiotic compositions that are useful in reducing inflammation and/or that exhibit increased colonization or persistence in the gastrointestinal tract of a mammal.