The present invention relates to a process for the production of a dyed biopolymer comprising the steps of providing at least one biopolymer-producing microorganism, providing at least one dye-producing microorganism, culturing said at least one biopolymer-producing microorganism to produce at least a biopolymer, and culturing said dye-producing microorganism wherein said dye-producing microorganism produce at least a dye suitable to dye at least part of said biopolymer, whereby a dyed biopolymer is obtained. The present invention also relates to a dyed biopolymer, to process for the production of a dyed composite article comprising at least the dyed biopolymer and to articles comprising the dyed biopolymer.

The present disclosure provides engineered polypeptides having imine reductase activity, polynucleotides encoding the engineered imine reductases, host cells capable of expressing the engineered imine reductases, and methods of using these engineered polypeptides with a range of ketone and amine substrate compounds to prepare secondary and tertiary amine product compounds.

The use of a cytochrome P-450 enzyme comprising SEQ ID NO: 110, or a variant enzyme having at least 70% identity thereto and having CYP-450 activity, for the hydroxylation of an organic compound, wherein the amino acid residue at position 291 is not threonine.

An NADPH-regeneration system based on monomeric isocitrate dehydrogenase (IDH) and a use thereof. Specifically, the present invention relates to a recombinant vector including a polynucleotide encoding an isocitrate dehydrogenase recombinant protein derived from Corynebacterium glutamicum (CgIDH) and an isocitrate dehydrogenase recombinant protein derived from Azotobacter vinelandii (AvIDH), a method for producing the recombinant protein, and an NADPH-regeneration system using the recombinant protein produced by the method. The enzyme in a monomeric form that may be efficiently used in the NADPH-regeneration system in the transformant into which the recombinant vector was introduced, was found, and the NADPH-regeneration system using the enzyme in a monomeric form has a very high utility value as biological parts and biocatalyst materials that provides NADPH to the NADPH-dependent enzyme.

The present disclosure includes genetically engineered, non-pathogenic Streptomyces bacterium with exogenous, non-native Thaxtomin A (ThxA) biosynthetic gene clusters conferring the genetically engineered, non-pathogenic Streptomyces bacterium with the ability to produce thaxtomin A. Also included are methods of providing thaxtomin producing capability in non-native Streptomyces bacterial strains, methods of producing thaxtomin compounds with the genetically engineered Streptomyces bacteria of the present disclosure, and methods of producing thaxtomin compounds and nitro-tryptophan analogs, and fluorinated thaxtomin compounds, analogs, and intermediates with the genetically engineered Streptomyces bacteria of the present disclosure.

The invention relates to norcoclaurine synthases and substrate binding sites having one or more site-specific mutation which increase the activity, when compared to the wild type synthase, of the condensation of 4-HPAA and dopamine to (S)-norcoclaurine and/or 3,4-DhPAA and dopamine to (S)-norlaudanosoline. The inventors both identified specific mutations corresponding to at position 73, 75, 77, 82, 99, 114, 141, 142, 147, 152, 174 and/or 178 in the count according to SEQ ID No: 1, and sites corresponding to the binding domains defined in SEQ ID NO: 4 and 5, where the mutated increase of the activity may be positioned within these norcoclaurine synthases. These domains are conserved regions.

The present disclosure provides engineered carboxyesterase enzymes that have the ability to catalyze amide bond formation. Also provided are polynucleotides encoding the carboxyesterase enzymes, host cells capable of expressing the engineered carboxyesterase enzymes, and methods of using the engineered carboxyesterase enzymes to make commercially valuable amides. Also provided are amides that are made using the engineered carboxyesterase enzymes.

The present invention provides a dehydrogenase mutant L283V/L286V, and a preparation method and use thereof, and relates to the field of biomedicine technologies. An amino acid sequence of the mutant L283V/L286V is as shown in SEQ ID NO: 1; and the mutant is prepared by simultaneously mutating 283.sup.rd and 286.sup.th leucine of a dehydrogenase with an amino acid sequence as shown in SEQ ID NO: 3 into valine. The dehydrogenase mutant L283V/L286V shows high selectivity in catalyzing myosmine reduction reaction in a whole cell system to produce S-nornicotine, and has relatively high dehydrogenase and imine reductase activities, a short enzyme reduction time, and a high transformation rate. The product S-nornicotine obtained through the reaction has extremely high optical purity, which reduces the operation difficulty of subsequent purification.

The present invention provides kinase inhibitor analogs with improved properties, such as improved efficacy, pharmacokinetics, safety, and specificity. In some embodiments, the present invention provides lapatinib analogs that provide therapeutic benefits.

The present invention relates to an optimized metabolic pathway design in P. pastoris. In particular, to a recombinant polycistronic expression construct for stable expression of multiple genes of interest in a yeast cell, preferably in P. pastoris.