Methods are provided for biological conversion of anhydrosugars, such as anhydrosugars found in a pyrolysis oil, to fatty acid alkyl esters. The methods can include use of a genetically modified Escherichia coli (E. coli) bacteria that can convert levoglucosan and/or other anhydrosugars into fatty acid alkyl esters without requiring formation and conversion of an intermediate compound external to the bacteria. Optionally, the methods can be used in combination with methods for production and/or separation of increased amounts of levoglucosan from pyrolysis of biomass.

Processes for producing reduced coenzyme Q.sub.10 (CoQ.sub.10) are provided. The processes may include preparing a reaction mixture, which includes oxidized CoQ.sub.10, a reductase, a supplement coenzyme, a coenzyme regeneration enzyme, and a substrate of the coenzyme regeneration enzyme, and providing a condition so that components of the reaction mixture react to produce the reduced CoQ.sub.10.

The present invention provides methods and compositions for the treatment of cardiovascular disorders comprising: a therapeutically effective amount of thioredoxin-1 or a thioredoxin-1 derivative in a pharmaceutical carrier to ameliorate one or more symptom of a cardiovascular disorder.

The present disclosure provides, among other features, an enzyme electrode in which an enzyme is immobilized via more appropriate bonds. An enzyme electrode according to the present disclosure includes an electrode and a modified protein having an amino acid sequence obtained by substituting at least one lysine residue in a protein that is a reductase or a dehydrogenase with a non-lysine amino acid residue, in which the modified protein is immobilized on a surface of the electrode.

The present disclosure provides, among other features, an enzyme electrode in which an enzyme is immobilized via more appropriate bonds. An enzyme electrode according to the present disclosure includes an electrode and a modified protein having an amino acid sequence obtained by substituting at least one lysine residue in a fusion protein between a thioredoxin reductase and a thioredoxin with a non-lysine amino acid residue, in which the modified protein is immobilized on a surface of the electrode.

Seminaphthofluorophore-selenium probes are disclosed. The probes include a seminaphthofluorophore scaffold substituted with at least one diselenide moiety having a formula YC(Q)O(CH.sub.2).sub.mSeSe(CH.sub.2).sub.nOR.sup.f, where R.sup.f is hydrogen or C.sub.1-C.sub.3 alkyl, Q is O or S, Y is O or N(R.sup.g) where R.sup.g is H or alkyl, and m and n independently are integers. The probes may be used to detect presence of a thioredoxin reductase.

Disclosed are compositions and methods for decreasing the viscosity and/or cohesiveness of and/or increasing the liquefaction of excessively or abnormally viscous or cohesive mucus or sputum. The composition contains a protein or peptide containing a thioredoxin monocysteinic active site in a reduced state and optionally further contains a reducing system.

This disclosure provides an E. coli strain, which lacks thioredoxin reductase activity encoded by trxB and thioredoxin 1 activity encoded by trxA, and glutathione reductase activity encoded by gor. Said E. coli strain expresses a mutated AhpC protein having glutathione reductase activity and a cytosolic prokaryotic disulfide isomerase. The E. coli strain has an oxidative cytosol and can be used to efficiently produce proteins having disulfide bonds.

Disclosed are compositions and methods for decreasing the viscosity and/or cohesiveness of and/or increasing the liquefaction of excessively or abnormally viscous or cohesive mucus or sputum. The composition contains a protein or peptide containing a thioredoxin monocysteinic active site in a reduced state and optionally further contains a reducing system.

This disclosure provides an E. coli strain, which lacks thioredoxin reductase activity encoded by trxB and thioredoxin 1 activity encoded by trxA, and glutathione reductase activity encoded by gor. Said E. coli strain expresses a mutated AhpC protein having glutathione reductase activity and a cytosolic prokaryotic disulfide isomerase. The E. coli strain has an oxidative cytosol and can be used to efficiently produce proteins having disulfide bonds.