The present disclosure relates to a non-naturally occurring enzyme that includes a first polypeptide that catalyzes the hydrolysis of a polyester to produce mono-(2-hydroxyethyl) terephthalate (MHET), a second polypeptide that catalyzes the cleavage of MHET to produce at least one of terephthalic acid or ethylene glycol, and a third polypeptide that links the first polypeptide with the second polypeptide.

Provided is a mutant of CRISPR nuclease FnCpf1. Compared with wild-type FnCpf1, the CRISPR nuclease FnCpf1 has the following mutations: K671R/E566V/D751G/N508H/N637S, K671R/E566V/D751G/F570L/N634D/R755K, K671R/E566V/D751G/S518G/K639R, K671R/E566V/D751G/F570L/E686D, K671R/E566V/D751G/K613N/N637S/N534K/G664V, K671R/E566V/D751G/K613N/F570L/G664S/N637Y, K671R/E566V/D751G/K613N/Y724C/F570L, or K671R/E566V/D751G/K613N/Y724C/F570L/R690I/L662I. The coding gene of the mutant has higher editing efficiency and wider editing range than the wild-type FnCpf1.

Described herein are engineered metabolic pathways in recombinant microorganism host cells which result in the production of 2-phenylethanol or 2-phenylacetic acid. Also described herein are methods of using the recombinant microorganisms for the production of 2-phenylethanol or 2-phenylacetic acid.

The present invention relates to fusion polypeptides, nucleic acid molecules encoding such fusion polypeptides and genetically modified cells comprising such nucleic acid molecules. Additionally, the present invention relates to a method for preparing a target peptide and target peptide mixtures.

The present invention relates to methods of improving cell lysis procedures and yields of intracellular biomolecules extracted from biomass. The methods comprise storing the microbial cells in ultra-low temperature (ULT) conditions for at least 10 minutes prior to lysing the cells.

A method of producing THB with improved efficiency is provided. Provided is a method of producing trihydroxybenzene (THB), the method comprising a step of heating a bacterial culture liquid comprising deoxy-scyllo-inosose (DOI) at a high temperature of no lower than 80° C. to obtain a product solution comprising trihydroxybenzene (THB).

A fusion protein includes heat shock protein 10 and brazzein protein. The fusion protein has an enhanced anti-oxidation activity and skin cell proliferation effect. It can be used as a cosmetic composition for ameliorating skin wrinkles. The cosmetic composition including the fusion protein can be advantageously used in future as a material of a functional cosmetic product.

Polypeptide products, methods, pharmaceutical compositions, and kits are provided for treating a subject exposed to, or at risk for exposure to, C. difficile microbial pathogens and toxin B produced by C. difficile (TcdB) pathogens. The methods, compositions and kits include a single domain, anti-TcdB VHH polypeptide (antibody), or toxin B binding portion thereof, that specifically binds to and/or neutralizes TcdB and treats or prevents illness and disease associated with C. difficile infection and TcdB intoxication. The anti-TcdB VHHs, or toxin B binding portion thereof, may be recombinantly produced.

A Escherichia coli strain for producing 5-aminolevulinic which has double pdxY genes is provided. A method of producing 5-aminolevulinic acid is provided, the method comprises providing the above Escherichia coli; and inoculating the above Escherichia coli into liquid modified M9 medium containing carbon source, IPTG, glycine, succinic acid and pyridoxal to cultivate the above Escherichia coli thereby producing 5-amino-levulinic. By the above Escherichia coli and the method of producing 5-aminolevulinic acid, the strain with high growth rate and 5-aminolevulinic productivity and the mothed of quickly producing 5-aminolevulinic acid with high 5-aminolevulinic productivity are provided.

A method for producing an objective substance such as vanillin and vanillic acid is provided. An objective substance is produced from a carbon source or a precursor of the objective substance by using a microorganism that is able to produce the objective substance, which microorganism has been modified so that the activity of an enzyme involved in SAM cycle (SAM cycle enzyme) is increased.