Microbial oxidation of gaseous hydrocarbons: production of alcohols and methyl ketones from their corresponding n-alkanes by methylotrophic bacteria

Autor: Laski Ai, Barnabe N, Marczak I, Patel Rn, Hou Ct
Rok vydání: 1981
Předmět:
Zdroj: Canadian Journal of Microbiology. 27:107-115
ISSN: 1480-3275
0008-4166
DOI: 10.1139/m81-017
Popis: Cell suspensions of methane-utilizing bacteria oxidized n-alkanes (propane, butane, pentane, and hexane) to their corresponding alcohols and methyl ketones. The product alcohols and methyl ketones accumulated extracellularly. Methanol-grown cells of methane-utilizing bacteria did not oxidize n-alkanes. The product primary alcohol was detected in a cell-free system but only in a trace amount in the whole cell system due to further oxidation. The optimum conditions for in vivo formation of secondary alcohol and methyl ketone from n-alkanes were compared between two distinct types of C1-utilizing microbes: Methylococcus capsulatus M1 (type I membrane) and Methylosinus trichosporium OB3b (type II membrane). The production of acetone or 2-butanone from n-alkanes ceased after 3 h of incubation for strain OB3b and 5 h for strain M1. The amount of these methyl ketones did not decline during 30 h of incubation. The optimum pH for the in vivo production of methyl ketones from n-alkanes by both strains was around 7.0. However, secondary alcohols were accumulated at higher amounts around pH 6.0. The optimum temperature for the in vivo production of methyl ketones from n-alkanes was around 40 °C for strain M1 and around 30–35 °C for strain OB3b. Higher accumulation of secondary alcohol was detected at 30–40 °C for strain M1 and 25 °C for strain OB3b.The alkane hydroxylation enzyme was located in the cell-free particulate fraction precipitated between 10 000 and 40 000 × g centrifugation. The yield of primary and secondary alcohols from n-alkane in the cell-free system was about equal. Evidence obtained indicates that the hydroxylation of n-alkanes (both terminal and subterminal oxidations) is also catalyzed by the methane hydroxylation – alkene epoxidation enzyme system.
Databáze: OpenAIRE