The present invention describes a novel process for preparing 3-chloro-2-vinylphenol which, owing to the chemoselectivity achieved, also allows direct conversion into (3-chloro-2-vinylphenyl)methane-sulphonate.

A chemoenzymatic method of producing a polyhydroxybenzene includes contacting glucose with one or more biocatalysts under conditions suitable for the formation of D-glucodialdose; and thermally treating D-glucodialdose in the presence of a dehydration catalyst under conditions suitable for the formation of the polyhydroxybenzene. A chemoenzymatic method of producing 1,2,3,4-tetrahydroxybenzene includes contacting glucose with a mutated copper radical oxidase and catalase under conditions suitable for the formation of D-glucodialdose; and subjecting D-glucodialdose and a dehydration catalyst to temperatures ranging from about 40 C. to about 100 C. suitable for the formation of 1,2,3,4-tetrahydroxybenzene.

A chemoenzymatic method of producing a polyhydroxybenzene includes contacting glucose with one or more biocatalysts under conditions suitable for the formation of D-glucodialdose; and thermally treating D-glucodialdose in the presence of a dehydration catalyst under conditions suitable for the formation of the polyhydroxybenzene. A chemoenzymatic method of producing 1,2,3,4-tetrahydroxybenzene includes contacting glucose with a mutated copper radical oxidase and catalase under conditions suitable for the formation of D-glucodialdose; and subjecting D-glucodialdose and a dehydration catalyst to temperatures ranging from about 40 C. to about 100 C. suitable for the formation of 1,2,3,4-tetrahydroxybenzene.

The present invention describes a novel process for preparing 3-chloro-2-vinylphenol which, owing to the chemoselectivity achieved, also allows direct conversion into (3-chloro-2-vinylphenyl)methane-sulphonate.

The present invention describes a novel process for preparing 3-chloro-2-vinylphenol which, owing to the chemoselectivity achieved, also allows direct conversion into (3-chloro-2-vinylphenyl)methane-sulphonate.

The present invention describes a novel process for preparing 3-chloro-2-vinylphenol which, owing to the chemoselectivity achieved, also allows direct conversion into (3-chloro-2-vinylphenyl)methane-sulphonate.

A catalyst composition comprises (i) a support; (ii) a dehydrogenation component comprising at least one metal or compound thereof selected from Groups 6 to 10 of the Periodic Table of Elements; and (iii) tin or a tin compound, wherein the tin is present in an amount of 0.01 wt % to about 0.25 wt %, the wt % based upon the total weight of the catalyst composition.

A catalyst composition comprises (i) a support; (ii) a dehydrogenation component comprising at least one metal or compound thereof selected from Groups 6 to 10 of the Periodic Table of Elements; and (iii) tin or a tin compound, wherein the tin is present in an amount of 0.01 wt % to about 0.25 wt %, the wt % based upon the total weight of the catalyst composition.

Disclosed are modified Type 1 O-methyltransferases (OMTs) and methods of using such modified OMTs. In some forms of the modified OMTs, the amino acid corresponding to Phe337 of Sorghum bicolor stilbene OMT (SbSOMT) is substituted with a polar amino acid. In some forms of the modified OMTs, the amino acid corresponding to Asn323 of Sorghum bicolor caffeic acid OMT (SbCOMT) is substituted with a hydrophobic amino acid. In some forms of the modified OMTs, the amino acid corresponding to Ile144 of SbSOMT is substituted with a polar amino acid. In some forms of the modified OMTs, the amino acid corresponding to Asn128 of SbCOMT is substituted with a hydrophobic amino acid.

Disclosed are modified Type 1 O-methyltransferases (OMTs) and methods of using such modified OMTs. In some forms of the modified OMTs, the amino acid corresponding to Phe337 of Sorghum bicolor stilbene OMT (SbSOMT) is substituted with a polar amino acid. In some forms of the modified OMTs, the amino acid corresponding to Asn323 of Sorghum bicolor caffeic acid OMT (SbCOMT) is substituted with a hydrophobic amino acid. In some forms of the modified OMTs, the amino acid corresponding to Ile144 of SbSOMT is substituted with a polar amino acid. In some forms of the modified OMTs, the amino acid corresponding to Asn128 of SbCOMT is substituted with a hydrophobic amino acid.