The present invention relates to a cytochrome P450 enzyme comprising the amino acid sequence set forth in SEQ ID NO: 3, or a variant thereof having an amino acid sequence having at least 95% identity thereto and having CYP450 activity. The cytochrome P450 enzyme provided herein was isolated from Streptomyces eurythermus NRRL 2539 and has a wide substrate range and high activity, and may be used to oxidate organic compounds.

The present invention provides a process for the preparation of tofacitinib citrate of Formula I. Specifically, the present invention provides an enzymatic route for the preparation of tofacitinib of Formula II, which is converted to tofacitinib citrate of Formula I.

The present invention relates to processes to make neosaxitoxin, and analogues and variants thereof, and intermediates in the production of neosaxitoxin in recombinant host cells. Neosaxitoxin and the analogues and variants thereof may be used in the production of pharmaceutical compositions.

The disclosure provides biocatalysts that halogenate complex chemical compounds in specific and predictable ways. Also disclosed are halogenated complex organic compounds. The disclosure further provides methods for the halogenation of complex chemical compounds and methods of inhibiting the contraction of smooth muscle in mammals.

The present invention discloses a transaminase mutant and application thereof in preparation of sitagliptin intermediates, the transaminase mutant is obtained by substitution of tyrosine with proline at position 74, substitution of glutamic acid with aspartic acid at position 228, substitution of leucine with alanine at position 254 and substitution of methionine with threonine at position 290 of the amino acid sequence shown in SEQ ID NO: 2. The present invention uses wet cells or a purified transaminase as a biocatalyst and a sitagliptin precursor ketone or a prochiral carbonyl compound as a substrate to prepare a sitagliptin intermediate or a sitagliptin ester intermediate; the total yield of the method reaches about 82%, and e.e. value of the product reaches 99%.

Use of a stereoselective transaminase in the asymmetric synthesis of a chiral amine. In particular, provided is use of a polypeptide in the production of a chiral amine or a downstream product using a chiral amine as a precursor. Further provided is a method for producing a chiral amine, comprising culturing a strain expressing the polypeptide so as to obtain a chiral amine. Further provided are a chiral amine production strain and a method for constructing the chiral amine production strain. The stereoselective transaminase has a broad substrate spectrum and thus has a broad application potential in the preparation of a chiral amine.

Provided is use of immobilized transaminase in preparation of sitagliptin and/or (R)-3-amino-1-morpholine-4-(2,4,5-trifluorophenyl)-1-butanone. The immobilized transaminase comprises resin and a transaminase mutant, the amino acid sequence of the transaminase mutant is as shown in SEQ ID NO: 3 or SEQ ID NO: 7. Also provided is an immobilized transaminase, a transaminase mutant, a preparation method therefor and use thereof. The enzyme activity of the transaminase mutant in the catalysis of a ketoamide substrate is high, and the enzyme activity is still high after the transaminase mutant is prepared into the immobilized transaminase. When the transaminase mutant is used for catalyzing the ketoamide substrate to produce sitagliptin or an intermediate thereof, a screened solvent reaction system is combined, the immobilized transaminase is high in conversion rate and good in stereoselectivity and stability, the repeatability rate is improved, and the operation is simpler, thereby reducing the cost of production, and it is beneficial to industrial production.

The present invention discloses processes for obtaining a color from an algal biomass. The process includes subjecting an algal biomass to cavitation, thus at least partially disrupting cells of the algal biomass and extracting color from the disrupted, algal biomass.

Disclosed is yeast cells having peroxisomally localized GPP synthase and a peroxisomally localized enzyme that converts GPP into a monoterpenoids, cannabinoids, monoterpene indole alkaloids and prenylated aromatic compounds; or a precursor therefore, which yeast cells are capable of producing improved amounts of monoterpenoids, cannabinoids, monoterpene indole alkaloids and prenylated aromatic compounds, compared with the same yeast cells where the GPP synthase and the enzyme that converts GPP are located in the cytoplasm. Further disclosed is the use of the yeast cell for producing monoterpenoids, cannabinoids, monoterpene indole alkaloids and prenylated aromatic compounds.

A method of demethylizing an opioid to a nor-opioid is provided. The method comprises contacting an opioid with at least one enzyme. Contacting the opioid with the at least one enzyme converts the opioid to a nor-opioid. A method of converting a nor-opioid to a nal-opioid is provided. The method comprises contacting a nor-opioid with at least one enzyme. Contacting the nor-opioid with the at least one enzyme converts the nor-opioid to a nal-opioid.