Provided is an enzymatic process for preparing L-methionine from diethyl disulfide.

Disclosed is a serum albumin-thioredoxin fusion body which is improved in the activity thereof and is stable with respect to the activity. The serum albumin-thioredoxin fusion body is provided, which is characterized in that the thioredoxin is a modified from in which at least a cysteine residue located at position 73 from the N-terminal of an amino acid sequence for the thioredoxin or located at a position equivalent to the position 73 is substituted by another amino acid residue. the modified serum albumin-thioredoxin fusion body is superior in the activity and stability thereof, is reduced in immunogenicity and has superior safety compared with a fusion body in which the thioredoxin is non-modified form.

This disclosure relates to the field of protein preparation and mass spectrometry analysis. In some embodiments, the disclosure relates to compositions and methods for simplifying mass spectrometry analysis by reducing methionine oxidation of protein samples.

An AhpF protein has thioredoxin reductase, peroxidase, and chaperone activities and is derived from Pseudomonas aeruginosa, and a use therefor. By using a novel activity of the AhpF of Pseudomonas aeruginosa according to the present invention, it is possible to produce a plant having strong resistance to various environmental stresses such as oxidative stress or heat stress, thereby making it possible to contribute to increasing crop productivity and mass production of useful constituents. In addition, it is possible to prevent desertification and environmental pollution through the development of transformed plants having resistance to high temperatures and drying.

Fusion proteins that include N-acetylaspartate synthetase (ANAT) and at least one solubilizing partner, such as glutathione 5-transferase (GST), thioredoxin (TRX), or maltose binding protein (MBP), are described. Also described are methods of making the fusion proteins, methods of solubilizing the fusion proteins, methods of purifying the fusion proteins, and methods of using the fusion proteins.

Provided is a process for the preparation of L-methionine in an enzymatic reaction utilizing dimethyl disulfide (DMDS) a precursor of L-methionine, and an organic reducing compound. In the process, methyl mercaptan can be formed by the enzymatic hydrogenolysis of the DMDS.

Provided is an enzymatic process for preparing L-methionine from diethyl disulfide.

Certain embodiments are directed to methods and compositions for preventing treating bacterial infections. In certain embodiments the compositions comprise thioredoxin deficient bacteria.

Phototropin is a blue light receptor, which mediates a variety of blue-light elicited physiological processes in plants and algae. In higher plants these processes include phototropism, chloroplast movement and stomatal opening. In the green alga Chlamydomonas reinhardtii, phototropin plays a vital role in progression of the sexual life cycle and in the control of the eye spot size and light sensitivity Phototropin is also involved in blue-light mediated changes in the synthesis of chlorophylls, carotenoids, chlorophyll binding proteins. We compared the transcriptome of phototropin knock out (PHOT KO) mutant and wild-type parent to analyze differences in gene expression in high light grown cultures (500 mol photons m.sup.2 s.sup.1). Our results indicate the up-regulation of genes involved in photosynthetic electron transport chain, carbon fixation pathway, starch, lipid, and cell cycle control genes. With respect to photosynthetic electron transport genes, genes encoding proteins of the cytochrome b6f and ATP synthase complex were up regulated potentially facilitating proton-coupled electron transfer. In addition genes involved in limiting steps in the Calvin cycle Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), Sidoheptulose 1,7 bisphosphatase (SBPase), Glyceraldehyde-3-phosphate dehydrogenase (3PGDH) and that mediate cell-cycle control (CDK) were also up regulated along with starch synthase and fatty acid biosynthesis genes involved in starch and lipid synthesis. In addition, transmission electron micrographs show increased accumulation of starch granules in PHOT mutant compared to wild type, which is consistent with the higher expression of starch synthase genes. Collectively, the altered patterns of gene expression in the PHOT mutants were associated with a two-fold increase in growth and biomass accumulation compared to wild type when grown in environmental photobioreactors (Phenometrics) that simulate a pond environment. In conclusion, our studies suggest that phototropin may be a master gene regulator that suppresses rapid cell growth and promotes gametogenesis and sexual recombination in wild type strains.

The present invention relates to a method for cross-linking peptides using an activated furan-moiety. In particular, the present invention provides a method for cross-linking peptides comprising the steps of: a) providing a composition comprising furan-peptides, said furan-peptides comprising at least one amino acid comprising a furan-moiety; b) contacting said composition comprising furan-peptides with second peptides, thereby obtaining a mixture comprising furan-peptides and second peptides; c) adding an activation signal to said mixture of step b), thereby activating said furan-peptides to activated furan-peptides, and d) reacting said activated furan-peptides with said second peptides, thereby cross-linking said activated furan-peptides with said second peptides.