The present invention relates to an enzymatic synthesis of 4′-ethynyl-2′-deoxy nucleosides and analogs thereof, for example EFdA, that eliminates the use of protecting groups on the intermediates, improves the stereoselectivity of glycosylation and reduces the number of process steps needed to make said compounds. It also relates to the novel intermediates employed in the process.

The present invention relates to an enzymatic synthesis of 4′-ethynyl-2′-deoxy nucleosides and analogs thereof, for example EFdA, that eliminates the use of protecting groups on the intermediates, improves the stereoselectivity of glycosylation and reduces the number of process steps needed to make said compounds. It also relates to the novel intermediates employed in the process.

An eco-compatible method is used to synthesize 2H-HBO optionally substituted at the β-position of the lactone function from LGO or a saturated form of LGO such as dihydrolevoglucosenone (2H-LGO) or LGO hydrate (OH-LGO) via a biocatalytic reaction using a cyclohexanone monooxygenase (CHMO).

An eco-compatible method is used to synthesize 2H-HBO optionally substituted at the β-position of the lactone function from LGO or a saturated form of LGO such as dihydrolevoglucosenone (2H-LGO) or LGO hydrate (OH-LGO) via a biocatalytic reaction using a cyclohexanone monooxygenase (CHMO).

The present disclosure relates to the biosynthesis of indigoid dye precursors and their conversion to indigoid dyes. Specifically, the present disclosure relates to methods of using polypeptides to produce indigoid dye precursors from indole feed compounds, and the use of the indigoid dye precursors to produce indigoid dyes.

The present invention relates to processes for the preparation of sclareolide and related compounds by the biocatalytic cyclization of polyunsaturated carboxylic acid compounds, in particular of homofarnesylic acid and related compounds; and to a process for the preparation of ambroxide via the biocatalytic cyclization of homofarnesylic acid to sclareolide.

The present invention relates to processes for the preparation of sclareolide and related compounds by the biocatalytic cyclization of polyunsaturated carboxylic acid compounds, in particular of homofarnesylic acid and related compounds; and to a process for the preparation of ambroxide via the biocatalytic cyclization of homofarnesylic acid to sclareolide.

A recombinant microbial host cell having improved in vivo conversion of reticuline and derivatives thereof (such as thebaine and/or oripavine) to relevant downstream opioids (such as neopinone, oripavine, northebaine, nororipavine or morphinone) and related compounds (such as heroin, morphine, codeine, thebaine, oripavine, oxycodone, hydrocodone, hydromorphone, oxymorphone, buprenorphine, naltrexone, naloxone or nalbuphine), wherein the microbial (such as fungal) host cell is heterologously expressing at least one functional transporter protein capable of transporting reticuline or a derivative thereof (such as thebaine and/or oripavine) and a heterologously expressed enzyme capable of acting upon reticuline or a derivative thereof. The invention also relates to uses of the microbial host cells and methods of making an opioid compound and/or opioid precursor compound and/or opioid derivative of interest.

Disclosed is a mutant of acid phosphatase and an application thereof, belonging to the technical field of biological engineering. The disclosure provides a mutant of acid phosphatase PaAPase.sub.Mu3. By expressing the mutant of acid phosphatase PaAPase.sub.Mu3 in Escherichia coli and using a whole-cell conversion method, L-ascorbic acid is transformed into L-ascorbate-2-phosphate. Moreover, a catalytic system of the mutant of acid phosphatase PaAPase.sub.Mu3 is optimized from the aspects of reaction pH and temperature, so that a yield of L-ascorbate-2-phosphate can reach 90.1 g/L and a molar yield can reach 75.1%. Therefore, the problems of a high substrate cost, environmental pollution and the like before are greatly reduced, laying a foundation for the industrial green production of L-ascorbate-2-phosphate.

Disclosed is a mutant of acid phosphatase and an application thereof, belonging to the technical field of biological engineering. The disclosure provides a mutant of acid phosphatase PaAPase.sub.Mu3. By expressing the mutant of acid phosphatase PaAPase.sub.Mu3 in Escherichia coli and using a whole-cell conversion method, L-ascorbic acid is transformed into L-ascorbate-2-phosphate. Moreover, a catalytic system of the mutant of acid phosphatase PaAPase.sub.Mu3 is optimized from the aspects of reaction pH and temperature, so that a yield of L-ascorbate-2-phosphate can reach 90.1 g/L and a molar yield can reach 75.1%. Therefore, the problems of a high substrate cost, environmental pollution and the like before are greatly reduced, laying a foundation for the industrial green production of L-ascorbate-2-phosphate.