Factors Effecting Microbial Coal Solubilization

First reports of microbial coal solubilization appeared in the early 1980's (Fakoussa, 1981; Fakoussa and Truper, 1983; Cohen and Gabriele, 1982). These degradations, which occurred at ambient temperature and pressure, resulted in a dark brown to black viscous liquid and required days to weeks to occur. Rates and degrees of coal biodegradation varied from coal to coal. Hard coals were not extensively degraded (5-7%) while low-rank coals such as Leonardite, a sublignite, were completely solubilized. A correlation between degree of weathering or oxidation of coal and the coals susceptibility to biological attack was observed. This led to oxidative pretreatments as a method to enhance microbial degradation of coal (Strandberg and Lewis, 1986). Products of microbial degradation of coal are water soluble solids that do not have significant solubilities in organic solvents (Wilson, et. al., 1987; Quigley, et. al., 1987; Quigley, et. al., 1988a). Solutions of solubilized coal did not separate or form precipitates which suggested that they were true solutions and not colloidal suspensions. Biosolubilized coal contained more oxygen than starting material suggesting that microbial attack of coals involved oxidative cleavage of carbon-carbon bonds. This small change in oxygen content was the only change observed in coal structure during the biosolubilization process. Many coal solubilizing microorganisms have been isolated. Some are lignin degrading organisms such as Phanerochaete chrysosporium and various Streptomyces species (Gupta, et. al., 1988; Wilson, et. al., 1987). This was not unexpected since the structures of lignin and low-rank coals are similar. These organisms produce an enzyme complex, ligninase, that utilizes hydrogen peroxide to oxidatively cleave the bond between a and ß carbons of an aliphatic chain bound to an aromatic nucleus. Another important organism is Trametes versacolor (syn. Coriolus versacolor, Polyporus versacolor). Even though this organism produces a ligninase (Dodson, et.al., 1987), coal solubilization has been attributed to the enzyme laccase (Pyne, et. al., 1987). Laccase utilizes molecular oxygen to oxidatively cleave a - ß bonds using a mechanism similar to that observed for ligninases (Kawai, et. al., 1988). Other coal solubilizing microorganisms have been isolated from coal outcrops (Ward, 1985; Ward, 1988), but enzyme activities responsible for coal solubilization have not been identified. Research at the Idaho National Engineering Laboratory has focused on those mechanisms involved in coal biosolubilization. An