Methods for the fermentative production of four carbon alcohols is provided. Specifically, butanol, preferably isobutanol is produced by the fermentative growth of a recombinant bacterium expressing an isobutanol biosynthetic pathway.

The present invention relates to mutant alcohol dehydrogenase enzymes, microorganisms comprising the mutant alcohol dehydrogenase enzymes, and methods for the production of products by microbial fermentation using the microorganisms.

Methods for stabilizing an enzyme by storing the enzyme in the presence of a stabilized coenzyme are disclosed. In addition, an enzyme stabilized with a stabilized coenzyme as well as the use thereof in test elements for detecting analytes are also disclosed. Other aspects include unique compositions, methods, techniques, systems and devices involving enzyme stabilization.

The present invention relates to a microorganism that produces 1,4-butanediol and a method of producing 1,4-butanediol using same. The microorganism according to the present invention is able to efficiently produce 1,4-butanediol using ornithine as a carbon source, unlike naturally occurring microorganisms.

The present invention relates to a mutant ketoreductase, a nucleic acid encoding the mutant ketoreductase, a vector comprising the nucleic acid, a method for the enzymatic reduction of a prochiral ketone and the formation of a chiral alcohol with the mutant ketoreductase, the use of the mutant ketoreductase for the preparation of chiral alcohols as well as the use of the method for the preparation of pharmaceutically active morpholine compounds.

The present invention relates to a recombinant E. coli strain producing 1,3-butanediol from glucose and a method for producing 1,3-butanediol using same, in which a recombinant E. coli strain was developed in which a gene of a pathway necessary for biosynthesis of 1,3-BDO from acetyl-CoA is cloned, and a gene of a pathway that interferes with or competes with this pathway is removed, wherein an E. coli strain was developed in which the pathways and genes involved in the conversion of glucose to acetyl COA, the regeneration rate of NADPH used as a cofactor, and the efficient use of the TCA cycle pathway, which are necessary to improve the biosynthetic efficiency of 1,3-BDO, are modified and optimized.

The present invention provides engineered ketoreductase and phosphite dehydrogenase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase and phosphite dehydrogenase enzymes, as well as polynucleotides encoding the engineered ketoreductase and phosphite dehydrogenase enzymes, host cells capable of expressing the engineered ketoreductase and phosphite dehydrogenase enzymes, and methods of using the engineered ketoreductase and phosphite dehydrogenase enzymes to synthesize a chiral catalyst used in the synthesis of antiviral compounds, such as nucleoside inhibitors. The present invention further provides methods of using the engineered enzymes to deracemize a chiral alcohol in a one-pot, multi-enzyme system.

Described herein are processes of preparing gingerol compounds, whether in their diol form or as a derivative, and methods of using gingerol compounds to enhance the salty taste or the umami taste of a flavored article. Also described herein are compositions and flavored products containing such compounds. In some embodiments, the flavored products have reduced amounts of salt or umami-enhancing compounds (glutamates, arginates, purinic ribonucleotides, such as inosine monophosphate (IMP) and guanosine monophosphate (GMP)), relative to comparable flavored products that do not incorporate the gingerol compounds.

Provided is a method for biosynthesis of (R)--hydroxytetradecanoate compounds. The method comprises the following steps of: reacting -carbonyl tetradecanoate in a ketoreductase and a glucose dehydrogenase or a fusion enzyme thereof, glucose, NADP.sup.+ and a buffer solution to obtain (R)--hydroxytetradecanoate compounds. The method is an enzyme-catalyzed biosynthesis method having simple operations, conventional equipment and an environmentally friendly process, and the prepared product has high purity, high yield and a high ee value.

Methods and compositions for the oxidation of short alkanes by engineered microorganisms expressing enzymes are described, along with methods of use.