[Problem] It is an object of the present invention to provide a method for collecting seawater that contains plankton and producing DHMBA, which is an antioxidant, from the plankton contained in the seawater.

[Solution] The method of the present invention includes: filtering collected seawater containing the plankton using a filter; taking out a cell content from the plankton remaining on the filter; subsequently heating/pressurizing the cell content taken out; and producing 3,5-dihydroxy-4-miethoxybenzyl alcohol from the heated/pressurized product. The plankton is a diatom. [Selected Drawing] FIG. 1

An application of a branched-chain α-ketoacid dehydrogenase complex in preparation of malonyl coenzyme A. A method for preparing malonyl-CoA using a branched-chain α-ketoacid dehydrogenase complex, the method comprising introducing a gene encoding a branched-chain α-ketoacid dehydrogenase complex into a biological cell strain to obtain a recombinant cell strain capable of expressing the gene encoding the branched-chain α-ketoacid dehydrogenase complex; culturing the recombinant cell strain to prepare malonyl-CoA; the branched-chain α-ketoacid dehydrogenase complex is the following M1) or M2): M1) a set of proteins consisting of a bkdF protein, a bkdG protein, a bkdH protein and a lpdA1 protein; M2) a set of proteins consisting of a bkdA protein, a bkdB protein, a bkdC protein and the lpdA1 protein. Experimental results show that by using the branched-chain α-ketoacid dehydrogenase complex, not only malonyl-CoA can be prepared, but also a target product using malonyl-CoA as an intermediate product can further be prepared.

An application of a branched-chain α-ketoacid dehydrogenase complex in preparation of malonyl coenzyme A. A method for preparing malonyl-CoA using a branched-chain α-ketoacid dehydrogenase complex, the method comprising introducing a gene encoding a branched-chain α-ketoacid dehydrogenase complex into a biological cell strain to obtain a recombinant cell strain capable of expressing the gene encoding the branched-chain α-ketoacid dehydrogenase complex; culturing the recombinant cell strain to prepare malonyl-CoA; the branched-chain α-ketoacid dehydrogenase complex is the following M1) or M2): M1) a set of proteins consisting of a bkdF protein, a bkdG protein, a bkdH protein and a lpdA1 protein; M2) a set of proteins consisting of a bkdA protein, a bkdB protein, a bkdC protein and the lpdA1 protein. Experimental results show that by using the branched-chain α-ketoacid dehydrogenase complex, not only malonyl-CoA can be prepared, but also a target product using malonyl-CoA as an intermediate product can further be prepared.

Methods for producing phloroglucinol as well as methods of using type III polyketide synthases as phloroglucinol synthases, in particular the type III polyketide synthases of algae, such as eukaryotic ochrophyte algae, are described herein. In addition, polypeptides that have phloroglucinol synthase activity, the isolated nucleic acid molecules encoding these type III polyketide synthases, and the vectors and the host cells comprising such nucleic acid molecules are also described.

Methods for producing phloroglucinol as well as methods of using type III polyketide synthases as phloroglucinol synthases, in particular the type III polyketide synthases of algae, such as eukaryotic ochrophyte algae, are described herein. In addition, polypeptides that have phloroglucinol synthase activity, the isolated nucleic acid molecules encoding these type III polyketide synthases, and the vectors and the host cells comprising such nucleic acid molecules are also described.

Transgenic host cells, vectors useful for making transgenic host cells, and kits useful for making transgenic host cells are described. Also described are transgenic plants. In some embodiments, transgenic host cells express a 4-hydroxyphenylacetaldehyde synthase (4HPAAS). In some embodiments, transgenic host cells express a tyrosol:UDP-glucose 8-O-glucosyltransferase (T8GT). The transgenic host cells are useful for biosynthesis of one or more of salidroside, icariside D2, tyrosol, and 4-hydroxypenylacetaldehyde.

A method of producing a mixture of pure feedstock-based native polyphenols from a feedstock. Contaminant polyphenols are first removed from an enzyme solution for converting feedstock to a product to produce a polyphenol reduced enzyme solution. The polyphenol reduced enzyme solution is combined with the feedstock and the feedstock is converted to a product and by-product. Heretofore, there has been no process available to reduce or remove the contaminant phenols introduced to the feedstock by commercial enzyme solutions. This method allows for the removal of contaminant phenols prior to introduction to the processing stream and subsequent harvesting of pure feedstock—based native polyphenols. The pure feedstock-based polyphenols are removed from the product or by-product to produce a pure mixture of feedstock-based polyphenols.

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.

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.

Described herein are non-natural variants of prenyltronsfcrases having at least one amino acid substitution as compared to its corresponding natural or unmodified prenyltransferascs. The variants are capable of an increased rate of formation of prenylated aromatic compounds, such as cannabinoids, as compared to a wild type control The prcnyltransferase variants can be expressed in an engineered microbe having a pathway to such cannabinoids, and optionally can include one or more other pathway transgencs to promote formation of substrate(s) for the prcnyltransferases. Therapeutically useful cannabinoids can be purified from engineered cells and cell cultures.