Endogenous origin of endo-β-1,4-glucanase in common woodlouse Porcellio scaber (Crustacea, Isopoda)
Because endogenous cellulases have been observed in arthropods, the potential ability to produce cellulose degrading enzymes was examined in the terrestrial isopod Porcellio scaber, an important decomposer of decayed plant material. cDNA fragments encoding portions of two novel endo-β-1,4-glucanase amino acid sequences were amplified by RT-PCR, and the amino acid sequences predicted were affiliated to endo-β-1,4-glucanases from other arthropods, where they cluster with endo-β-1,4-glucanases of decapod crustaceans. Hybridization in situ reveals the hepatopancreas to be the primary site of gene expression and provides direct evidence of the endogenous origin of endo-β-1,4-glucanase in P. scaber. Conservation of catalytically important amino acid residues suggests that both sequences translate into functional cellulases. Cellulolytic activity was detected in hepatopancreatic extract after separation by SDS-PAGE, which included CMC as substrate. This is the first evidence of endogenous cellulases in peracarid crustaceans and gives strong support for the involvement of isopod endo-β-1,4-glucanases in the degradation of cellulose in their diet.