two termite species (Reticulitermes flavipes vs. Coptotermes formosanus) and two parts of gut systems (foregut/midgut vs. hingut) for each species. The study has revealed several features. First, biocatalysts from
both host species and symbiont work synergistically toward biomass degradation. In particular, about 38.2% of the total proteins in the R. flavipes foreg/midgut were endoglucanase from the termite host, which
indicated the crucial role of host enzyme for biomass conversion. Even though enzymes from both host and symbiont exist in different gut parts, the host enzymes are more enriched in the forgu/midgut part. The
observation correlates with traditional studies that most of the microbial species exist in the hindgut, yet also highlights that the synergistics of complementary functionalities between the host and the microbial
biocatalysts. Second, considering that major lignin and cellulytic enzymes exist in both foreg/midgut and hindgut, the termite gut biomass conversion can be considered as a continuous and simultaneous process.
Third, despite the similarity among different gut parts, comprehensive profile of lignin degrading enzymes including laccase, catalase, peroxidase, P450, esterase were more enriched in the foregut and midgut,
whilst much more diverse cellulytic enzymes were found in the hindgut. The results highlighted potential distinct functionality in different gut parts, which can be mimicked in the bioprocessing. We are currently
cloning and analyzing the major lignin degradation enzymes toward reverse design of biological pretreatment.