The present disclosure belongs to the technical field of biocatalysis and biotransformation, and particularly relates to whole-cell biocatalysis method for producing α, ω-dicarboxylic acids and use thereof. The biosynthetic pathway designed in the present disclosure is divided into three modules to co-express several different enzymes in host cells respectively, and then the whole-cells are used to catalyze the production of α, ω-dicarboxylic acid from cycloalkanes, cycloalkanol and lactones in a cascade reaction. Compared with the chemical method, this process does not produce any harmful gases during the production process, does not require high temperature, high pressure, and complex metal catalysts, and is a green and environmental protection production method.

The present disclosure relates to processes that combine microbial production of organic intermediates and subsequent synthetic transformation to provide compounds of industrial value, including compounds used in fragrances.

The present disclosure relates to processes that combine microbial production of organic intermediates and subsequent synthetic transformation to provide compounds of industrial value, including compounds used in fragrances.

The invention relates to a polypeptide for the enzymatic detoxification of zearalenone, said polypeptide being a monooxygenase which converts the keto group in position 7 of zearalenone into an ester group, the monooxygenase in particular being an amino acid sequence selected from the group comprising sequence ID No. 1, 2 and 3 or a functional variant thereof. The functional variant and at least one of the amino acid sequences has a sequence identity of at least 60%, preferably at least 70%, more preferably at least 80% and most preferably 90%.

The invention relates to a polypeptide for the enzymatic detoxification of zearalenone, said polypeptide being a monooxygenase which converts the keto group in position 7 of zearalenone into an ester group, the monooxygenase in particular being an amino acid sequence selected from the group comprising sequence ID No. 1, 2 and 3 or a functional variant thereof. The functional variant and at least one of the amino acid sequences has a sequence identity of at least 60%, preferably at least 70%, more preferably at least 80% and most preferably 90%.

Described herein are biofilm bioreactors for synthesis at the interface between two liquids, and methods of using such bioreactors for the biotransformation of feedstocks into chemical products. Also contemplated is the extraction of such products.

The present invention provides for a fusion protein comprising: (a) a terpene synthase (TS), or a homolog thereof, (b) a peptide linker, and (c) a P450 enzyme, or a homolog thereof.

The present disclosure relates to processes that combine microbial production of organic intermediates and subsequent synthetic transformation to provide compounds of industrial value, including compounds used in fragrances.

The present disclosure relates to processes that combine microbial production of organic intermediates and subsequent synthetic transformation to provide compounds of industrial value, including compounds used in fragrances.

The present invention relates to a method for improving the heterologous synthesis of a polyketide by E. coli and use thereof. The yield of the polyketide heterologously synthesized by E. coli is significantly increased by attenuating the expression of seventy-two genes, such as sucC and talB, in a host strain, wherein the highest yield increase rate can reach 60% or more. Currently, erythromycin is the most clear model compound in the study on the biosynthesis of polyketids. The production strain of the present invention enables massive accumulation of 6-deoxyerythronolide (6-dEB), an erythromycin precursor, in the fermentation process, laying the foundation for the industrial production of the heterologous synthesis of erythromycin by E. coli.