Provided are a Blumea balsamifera monoterpene synthase BbTPS3 and related biological materials thereof and use thereof. BbTPS3 is: A1) a protein having the amino acid sequence shown in SEQ ID NO: 2; A2) a fusion protein obtained by linking protein-tags at the N-terminus or/and the C-terminus of the protein shown in SEQ ID NO: 2; and A3) a protein having at least 90% identity and the same function as the protein shown in A1), which is obtained by performing substitution and/or deletion and/or addition of one or more amino acid residues on the amino acid sequence shown in SEQ ID NO: 2. BbTPS3 can catalyze GPP to form l-borneol, and can be used to regulate and produce plant monoterpene compounds and cultivate Blumea balsamifera (L.) DC.

The present invention relates to genetically modified bacteria and methods of optimizing genetically modified bacteria for the production of a metabolite.

The present invention relates to genetically modified bacteria and methods of optimizing genetically modified bacteria for the production of a metabolite.

An integrated process and system for employing low conversion rWGS to prepare a gas fermentation feed stream from a CO.sub.2 source and a hydrogen source in order to produce at least one gas fermentation product. Low conversion rWGS reactors may (1) employ a wider selection of inorganic catalysts then rWGS reactors requiring high temperature operation, (2) allow for use of an electric heater instead of a fired heater to preheat feed stream to the low conversion rWGS reactor, and (3) extend rWGS catalyst life by reducing the amount of water produced in the rWGS reaction.

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.

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.

Microorganisms present within a plurality of microorganism clusters immobilized in a porous support material may collectively define a supported bio-catalyst. When the microorganisms are effective to convert methane into one or more oxidized carbon compounds (e.g., methanotrophic bacteria), the supported bio-catalysts may be utilized to remove methane from methane-containing gas streams, such as those obtained from mining ventilation. Methods for processing a methane-containing gas stream may comprise interacting the gas stream with the supported bio-catalyst in substantial absence of a liquid phase, and obtaining a methane-depleted gas stream downstream from the supported bio-catalyst. Systems for processing a methane-containing gas stream may comprise the supported bio-catalysts housed in one or more vessels fluidly coupled to a source of methane-containing gas stream. A gas concentration in the methane-containing gas stream and/or the methane-depleted gas stream may be used to determine a current state or anticipated remaining lifetime of the supported bio-catalyst.

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.

Described herein is a method of producing a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof by contacting at least one polypeptide with farnesyl diphosphate (FPP) with a polypeptide including a Haloacid dehalogenase (HAD)-like hydrolase domain and having bifunctional terpene synthase activity. The method may be performed in vitro or in vivo. Also described herein are amino acid sequences of polypeptides useful in the methods and nucleic acids encoding the polypeptides described. The described method further provides host cells or organisms genetically modified to express the polypeptides and useful to produce a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof.

Described herein is a method of producing a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof by contacting at least one polypeptide with farnesyl diphosphate (FPP) with a polypeptide including a Haloacid dehalogenase (HAD)-like hydrolase domain and having bifunctional terpene synthase activity. The method may be performed in vitro or in vivo. Also described herein are amino acid sequences of polypeptides useful in the methods and nucleic acids encoding the polypeptides described. The described method further provides host cells or organisms genetically modified to express the polypeptides and useful to produce a drimane sesquiterpene such as albicanol, drimenol and/or derivatives thereof.