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Title: Bioprocessing of lignite coals using reductive microorganisms

Technical Report ·
OSTI ID:5454505

Research continued on bioprocessing of lignite. This quarter results are as follows: Pseudomonas strain DLC-62 produces an extracellular enzyme activity which depolymerizes a water soluble lignite coal polymer at acidic pH's. The lignite depolymerase acts in a nonoxidative fashion, presumably hydrolytically. In the present work we find that the enzymes present in active extracellular culture filtrates of DLC-62 are composed almost exclusively of multiple esterases and peroxidases. One of the esterase isoforms was synthesized constitutively, while others were induced, albeit variably, by coal. The two peroxidase isoforms were constitutively expressed. In liquid medium, both activities were maximally expressed approximately 36--48 hours after entry of cells into stationary phase. Partially purified esterases, from periplasmic, cytoplasmic, and membrane fractions of the cells, were incubated with coal polymer. Under these conditions, they exhibited no depolymerizing activity. However, crude ultra-filtered culture filtrates containing both esterases and peroxidases were active. In the latter case, however, coal depolymerizing activity was independent of extraneously added H{sub 2}O{sub 2}. This finding was extended to culture filtrates of the actinomycete Streptomyces viridosporus T7A. Concentrated culture filtrates from strain T7A also contained esterases and peroxidases, and they depolymerized coal. The esterases of strain DLC-62 have been partially purified by Fast Protein Liquid Chromatography (FPLC) and are currently being further characterized. 13 refs., 10 figs, 1 tab.

Research Organization:
Idaho Univ., Moscow, ID (United States). Dept. of Bacteriology and Biochemistry
Sponsoring Organization:
USDOE; USDOE, Washington, DC (United States)
DOE Contract Number:
FG22-88PC88919
OSTI ID:
5454505
Report Number(s):
DOE/PC/88919-T5; ON: DE91016792
Country of Publication:
United States
Language:
English