The invention provides a non-naturally occurring microbial organism having a 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid pathway. The microbial organism contains at least one exogenous nucleic acid encoding an enzyme in the respective 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid pathway. The invention additionally provides a method for producing 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid. The method can include culturing a 6-aminocaproic acid, caprolactam or hexametheylenediamine producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding a 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid pathway enzyme in a sufficient amount to produce the respective product, under conditions and for a sufficient period of time to produce 6-aminocaproic acid, caprolactam, hexametheylenediamine or levulinic acid.

The purpose of the present invention is to provide a recombinant host cell which is capable of efficiently and easily producing a benzylisoquinoline alkaloid (BIA), in particular, tetrahydropapaveroline, 3-hydroxycoclaurine, 3-hydroxy-N-methylcoclaurine and/or reticuline, and a method for efficiently and easily producing these BIAs using the host cell. The present invention pertains to a recombinant host cell for producing a benzylisoquinoline alkaloid (BIA), in particular, tetrahydropapaveroline (THP), 3-hydroxycoclaurine, 3-hydroxy-N-methylcoclaurine and/or reticuline, in which a wild-type aromatic aldehyde synthase (AAS) or a mutant thereof and a wild-type aromatic amino acid decarboxylase (AAAD) or a mutant thereof are expressed.

The purpose of the present invention is to provide a recombinant host cell which is capable of efficiently and easily producing a benzylisoquinoline alkaloid (BIA), in particular, tetrahydropapaveroline, 3-hydroxycoclaurine, 3-hydroxy-N-methylcoclaurine and/or reticuline, and a method for efficiently and easily producing these BIAs using the host cell. The present invention pertains to a recombinant host cell for producing a benzylisoquinoline alkaloid (BIA), in particular, tetrahydropapaveroline (THP), 3-hydroxycoclaurine, 3-hydroxy-N-methylcoclaurine and/or reticuline, in which a wild-type aromatic aldehyde synthase (AAS) or a mutant thereof and a wild-type aromatic amino acid decarboxylase (AAAD) or a mutant thereof are expressed.

A protein hydrolysate composition derived from a microorganism, such as a chemoautotrophic microorganism, and methods of preparing and using the same are provided. The protein hydrolysate composition may be produced sustainably through fixation of carbon dioxide from biogenic or atmospheric sources. The protein hydrolysate composition finds use in supplementing culture media for serum-free culturing of animal cells as well as for growing other types of cells such as probiotics and lactic acid bacteria. Thus, the present disclosure provides sustainable, humane processes for culturing cells for pharmaceutical and nutraceutical application as well as for human consumption as a food ingredient or product, including cultured meat.

The disclosure discloses a mutant of nitrile hydratase derived from Caldalkalibacillus thermarum, and belongs to the technical field of enzyme engineering. The nitrile hydratase mutant Cal. t Nhase-A20V provided by the disclosure has a half-life of about 10 min at 70° C., which does not change much compared with the thermal stability of the wild enzyme. The specific enzyme activity of the mutant Cal. t Nhase-A20V is 128% of that of the wild enzyme. At the same time, the mutant also has better tolerance to a substrate and a product, and the final yield of nicotinamide produced by whole-cell catalysis reaches 598 g/L. Therefore, the nitrile hydratase mutant Cal. t Nhase-A20V provided by the disclosure has good enzymatic properties and is beneficial to future industrial production.

Disclosed herein are methods that may be used for the synthesis of benzylisoquinoline alkaloids (“BIAs”) such as alkaloid morphinan. The methods disclosed can be used to produce thebaine, oripavine, codeine, morphine, oxycodone, hydrocodone, oxymorphone, hydromorphone, naltrexone, naloxone, hydroxycodeinone, neopinone, and/or buprenorphine. Compositions and organisms useful for the synthesis of BIAs, including thebaine synthesis polypeptides, purine permeases, and polynucleotides encoding the same, are provided.

The present disclosure relates to methods of using transaminase polypeptides in the synthesis of chiral amines from prochiral ketones.

The present disclosure relates to methods of using transaminase polypeptides in the synthesis of chiral amines from prochiral ketones.

The present disclosure relates to the field of genetic engineering, especially relates to a xylose-induced genetically engineered bacteria used for producing ectoine as well as a construction method and use thereof The genetically engineered bacteria is constructed by heterologously expressing the ectABC gene cluster from Halomonas elongata on the E. coli chromosome, using the promoter of xylose transporter coding gene xylF to control the RNA polymerase from T7 bacteriophage, reconstructing a synthesis pathway of ectoine and constructing a plasmid-free system, and enhancing the expression of target genes by a strong promoter T7; the yiled of ectoine reached 12-16 g/L after 20-28 h fermentation in shake flask, and reached 35-50 g/L after 24-40 h fermentation in a 5 L fermentor.

The present disclosure relates to the field of genetic engineering, especially relates to a xylose-induced genetically engineered bacteria used for producing ectoine as well as a construction method and use thereof The genetically engineered bacteria is constructed by heterologously expressing the ectABC gene cluster from Halomonas elongata on the E. coli chromosome, using the promoter of xylose transporter coding gene xylF to control the RNA polymerase from T7 bacteriophage, reconstructing a synthesis pathway of ectoine and constructing a plasmid-free system, and enhancing the expression of target genes by a strong promoter T7; the yiled of ectoine reached 12-16 g/L after 20-28 h fermentation in shake flask, and reached 35-50 g/L after 24-40 h fermentation in a 5 L fermentor.