General esterases from eastern subterranean termite, Reticulitcnncs flmJipl'S (Kollar), workers were examined for activity and were characterized by electrophoretic and biochemical methods. Greater acti\~ty was observed toward a-naphthyl substrates when compared \vith p-nitrophenyl substrates. Tbe specific activity of the esterases increased with a corresponding increase in a-naphthyl acetate concentration. Maximal activities were observed \vith a buffer pH of 7.6 and an incubation temperature of 45°C. The calculated MichaelisMenten constant (Kill)was 72.53 J.LMand the Villa'was 33.77 J.LM/minlmgof protein. Nondenaturing polyacrylamide gel electrophoresis revealed the presence of seven esterase bands, which were named EI-E7. Bands EI-E4 (slowest gel mobility) were determined to be choIinesterases based on physostigmine inhibition. The remaining three bands were identificd as carbox)'lesterases based on inhibition by paraoxon. The molecular weights of the seven bands ranged from 71.5 to 97.2 kD.KEY WORDS Retil-1.tlitennesflavipes, esterase, termites SUBTEHHANEANTEHMITES CAUSE considerable damage to structures and wood products. An estimated $1.17 billion was spent in 1982 on termite prevention and control measures in the United States (Granovsky 1983). The eastern subterranean termite, Reticulitennes flavipes (Kollar), is one of the most economically important species in the United States (Mampe 1982). Karnble et al. (1984) estimated that a minimum of $1 million is spent annually in Nebraska as a result of damage caused by Reticulitemu~s spp.Despite the economic importance of subterranean termites, little is known about the metabolic and xenobiotie detoxifying systems of these insects. Esterases are important in the metabolism and physiology of animals and plants (Sivakumaran & Mayo 1991). These enzymes may hydrolyze endogenous substances, assume a part in intermedimy metabolism, or promote xenobiotic detoxification (Shen & Dowd 1991). Esterases are proteins that are defined by their ability to catalyze the hydrolysis of ester bonds within lipophilic compounds (Pantelouris & Amason 1966). They are primarily phase I enzymes which, in the presence of water, cleave the target compound into an alcohol and an acid. The ability of esterases to hydrolyze synthetic amides and esters is well documented (Eto 1974, Dauterman 1976, Junge 1984, Junge & Kless 1984, Wilkinson 1985.The hydrolases include the following esterases: arylesterases (A esterases, EC 3.1.1.2), carboxylesterases (B esterases, EC 3.1.1.1), and cholinesterases (B esterases, EC 3.1.1.8) (Augustinson 19.59, 1961). Carboxylesterases and cholinesterases aTe inhibited stoichiometrically by organophosphorolls or sulfhydryl reagents without concurrent hydrolysis (Aldridge 1953, Krisch 1971. The arylcsterases are resistant to inhibition by OP and SH compounds (Ahmad et al. 1986). Cholinesterase is inhibited by the methylcarbamate, physostigmine (eserine) (Beranek 1974).Because of the importance of esterases in physiology, metabolism, and xenobiotic det...