Abstract: A process is disclosed for the microbiological production of ketones from C.sub.3 -C.sub.6 alkanes by contacting C.sub.3 -C.sub.6 alkanes under aerobic conditions with resting microbial cells derived from a methylotrophic microorganism or enzyme preparation derived from said cells, wherein the microorganism has been previously grown under aerobic conditions in a nutrient medium containing methane or dimethyl ether.

Abstract: Disclosed are newly discovered and isolated methylotrophic microorganism strains and their natural and/or artificial mutants which grow well under aerobic conditions in a culture medium in the presence of methane as the major carbon and energy source. The methane-grown microbial cells possess a high content of protein and can be utilized as such as feedstuffs. The methane-grown microbial cells or enzyme preparations thereof are also useful in converting C.sub.1 -C.sub.6 alkanes to alcohols, particularly methane to methanol, C.sub.3 -C.sub.6 alkanes to the corresponding C.sub.3 -C.sub.6 sec. alcohols and methyl ketones, C.sub.3 -C.sub.6 sec. alcohols to the corresponding methyl ketones, cyclic hydrocarbons to cyclic hydrocarbyl alcohols (e.g., cyclohexane to cyclohexanol) C.sub.2 -C.sub.4 alkenes selected from the group consisting of ethylene, propylene, butene-1 and butadiene to 1,2-epoxides, styrene to styrene oxide, and converting other oxidizable substrates to oxidized products.

Abstract: A process is disclosed for the microbiological production of ketones from C.sub.3 -C.sub.6 secondary alcohols by contacting C.sub.3 -C.sub.6 secondary alcohols under aerobic conditions with resting microbial cells derived from a microorganism of enzyme preparation derived from said cells, wherein the microorganism has been previously grown under aerobic conditions in a nutrient medium containing a methyl-radical donating compound. Typical methyl-radical donating compounds are: methane, methanol, dimethyl ether, methylamine, methyl formate, methyl carbonate, ethanol, propanol, butanol, etc. Isolation and purification of a novel C.sub.3 -C.sub.6 secondary alcohol dehydrogenase enzyme is also disclosed.

Abstract: Disclosed is a newly-discovered and isolated enzyme which is a nicotinamide adenine dinucleotide (NAD.sup.+)-linked C.sub.3 -C.sub.6 secondary alcohol-specific dehydrogenase. This enzyme, in the presence of oxygen and NAD, is capable of converting C.sub.3 -C.sub.6 secondary alcohols to the corresponding methyl ketones. The purified enzyme has a molecular weight of 95,000 .+-. 3,000 dalton as determined by acrylamide gel electrophoresis and contains two zinc atoms per molecule of protein. Primary alcohols are not oxidized by this enzyme.