Transgenic plants with blue flower color, or their inbred or outbred progeny, or their propagules, partial plant bodies, tissues or cells, are provided. A buckwheat-derived C-glucosyltransferase (CGT) gene or its homolog is transferred into a host plant to cause delphinidin-type anthocyanins and flavone mono-C-glycosides to be copresent in the plant cells.

The invention discloses an alcohol dehydrogenase mutant and use thereof. The alcohol dehydrogenase mutant of the present invention has high thermal stability and enables high catalytic efficiency and high conversion rate (i.e. space time yield) in the asymmetric reduction of prochiral diaryl ketones to produce chiral diaryl alcohols. Therefore, the alcohol dehydrogenase mutant of the present invention has extremely high prospect of application in the production of chiral diaryl alcohols, such as (S)-(4-chlorophenyl)-(pyridin-2-yl)-methanol, (R)-(4-chlorophenyl)-(pyridin-2-yl)-methanol.

A method of producing electrical power includes: a cathode having a porphyrin precursor attached to a substrate, and having a first enzyme, wherein the first enzyme reduces oxygen; an anode having a first region of an anode substrate and having a gold nanoparticle composition located thereon, and having a second region of the anode substrate having an enzyme composition located thereon, wherein the enzyme composition includes a second enzyme, wherein the first region and second region are separate regions; and a neutral fuel liquid in contact with the anode and cathode, the neutral fuel liquid having a neutral pH and a fuel reagent; and operating the fuel cell to produce electrical power with the neutral fuel liquid having the neutral pH and the fuel reagent.

This document describes biochemical pathways for producing adipic acid, caprolactam, 6-aminohexanoic acid, hexamethylenediamine or 1,6-hexanediol by forming two terminal functional groups, comprised of carboxyl, amine or hydroxyl groups, in a C6 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on CoA-dependent elongation enzymes or analogues enzymes associated with the carbon storage pathways from polyhydroxyalkanoate accumulating bacteria.

A method of producing electrical power includes: a cathode having a porphyrin precursor attached to a substrate, and having a first enzyme, wherein the first enzyme reduces oxygen; an anode having a first region of an anode substrate and having a gold nanoparticle composition located thereon, and having a second region of the anode substrate having an enzyme composition located thereon, wherein the enzyme composition includes a second enzyme, wherein the first region and second region are separate regions; and a neutral fuel liquid in contact with the anode and cathode, the neutral fuel liquid having a neutral pH and a fuel reagent; and operating the fuel cell to produce electrical power with the neutral fuel liquid having the neutral pH and the fuel reagent.

Provided is: a transgenic plant that has a modified flower color; a self- or cross-fertilized descendant of the transgenic plant; or a propagule, a portion of a plant body, tissue, or cells from the transgenic plant or the self- or cross-fertilized descendant of the transgenic plant. The present invention causes both anthocyanin delphinidin and a flavone C-glycoside that is methylated at the hydroxyl group at the 7 position to be present in the cells of a plant.

The invention discloses an alcohol dehydrogenase mutant and use thereof. The alcohol dehydrogenase mutant of the present invention has high thermal stability and enables high catalytic efficiency and high conversion rate (i.e. space time yield) in the asymmetric reduction of prochiral diaryl ketones to produce chiral diaryl alcohols. Therefore, the alcohol dehydrogenase mutant of the present invention has extremely high prospect of application in the production of chiral diaryl alcohols, such as (S)-(4-chlorophenyl)-(pyridin-2-yl)-methanol, (R)-(4-chlorophenyl)-(pyridin-2-yl)-methanol.

The present invention relates to an Fe—S fusion protein acting as an electron transport chain, a novel carbon monoxide:formate oxidoreductase (CFOR) including the Fe—S fusion protein, novel Thermococcus strain BCF12 transformed with CFOR, and the use thereof. According to the present invention, two different enzymes may be physically linked directly to each other through the Fe—S fusion protein of the present invention, and thus electrons generated from any one enzyme may be transported directly to another enzyme through the Fe—S cluster of the Fe—S fusion protein. Accordingly, a reaction that produces a target substance with high efficiency by directly supplying electrons necessary for the production of the target substance is possible without leakage of electrons generated in any one enzyme. In addition, the present invention has an advantage in that the overall enzyme reaction rate and yield can be dramatically improved using a new electron transport reaction. Furthermore, it is possible to ensure the stability of each enzyme by allowing the enzymes to exist in a physically fixed state in cells.

An anode can include: an electrode substrate; a first region of the substrate having a catalyst composition located thereon, wherein the catalyst composition includes an inorganic or metallic catalyst; and a second region of the substrate having an enzyme composition located thereon, wherein the combination of the catalyst composition and enzyme composition converts a fuel reagent to carbon dioxide at neutral pH. The first region and second region can be separate regions. The catalyst of the catalyst composition can include gold nanoparticles. The catalyst can include an inorganic or metallic catalyst selected from vanadium oxide, titanium (III) chloride, Pd(OAc).sub.2, MnO, zeolite, alumina, graphitic carbon, palladium, platinum, gold, ruthenium, rhodium, iridium, or combinations thereof. The catalyst can be nanoparticle, nanorod, nanodot, or combination thereof. The catalyst can have sizes that range from about 10 to 20 nm.

A cathode can include: an electrode substrate; a porphyrin precursor attached to the substrate; and an enzyme coupled to the electrode substrate to be associated with the porphyrin precursor, the enzyme reduces oxygen. The cathode can include a conductive material associated with the porphyrin precursor and/or the enzyme. The cathode can include 1-pyrenebutanoic acid, succinimidyl ester (PBSE) associated with the porphyrin precursor and/or the enzyme and/or the conductive material. The cathode can include 2,5-dimethyl-1-phenyl-1H-pyrrole-3-carbaldehyde (DMY-Carb) associated with the 1-pyrenebutanoic acid, succinimidyl ester (PBSE) and/or the porphyrin precursor and/or the enzyme and/or the conductive material. The porphyrin precursor is attached to the substrate through covalent coupling. In some aspects, substrate is linked to the porphyrin precursor, the porphyrin precursor is linked to the conductive material, the conductive material is linked to the PBSE, the PBSE is linked to the DMY-carb, and the DMY-carb is linked to the enzyme.