Characterization of Nasutitermes globiceps (Isoptera: Termitidae) Esterases Maria Claudia C. Ruvolo-Takasusuki 1,2 and Thaı ´s Collet 1 Received 15 Oct. 1999 —Final 11 May 2000 Esterases of Nasutitermes globiceps termites which occur on the Upper Parana ´ River floodplain (Brazil) were characterized. The electrophoretic pattern of the termite esterases Nasutitermes globiceps was obtained by starch gel electro- phoresis. Six esterase activity zones were obtained and numbered, with ester- ase-1 being the most anodall one and esterase-6 the most cathodal one. Ester- ase-2 was detected only with substrates derived from the 4-methylumbelliferyl radical. The esterases of N. globiceps present wide substrate specificity, having been observed with substrates derived from -naphthyl (acetate, propionate, and butyrate) and -naphthyl (acetate, butyrate) and from 4-methylumbelliferyl (acetate, propionate and butyrate). Esterase-6 is a caste-specific enzyme detected in soldiers. Only esterases 1, 3 and 5 were detected in nymphs. No genetic polymorphism has been detected thus far in the esterases of Nasutitermes globiceps. This study suggests that allozyme variation can be explored to understand Nasutitermes social structure. KEY WORDS: esterases; termites; Nasutitermes globiceps; castes; expression during development. INTRODUCTION Termites are important constituents of tropical and subtropical ecosystems (Schaella, 1996). They consume a wide variety of dead plant matter such as litter, leaf-fall, grasses and wood. Different termite species live in the same habitat, consuming material in proportionally different quantities (Lepage et al., 1993). Termites comprise as much as 50% of the total soil biomass in the central 1 Departamento de Biologia Celular e Gene ´tica, Universidade Estadual de Maringa ´—UEM, Av. Colombo 5790, 87020-900 Maringa ´, PR, Brazil. 2 To whom correspondence should be addressed. e-mail: mccrtakasusuki@uem.br. Biochemical Genetics, Vol. 38, Nos. 11/12, 2000 367 0006-2928/00/1200 – 0367$18.00/0 © 2000 Plenum Publishing Corporation