Background:
Lignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource. However, saccharification and production of bioproducts derived from plant cell wall biomass are complex and entail lengthy processes. The understanding of a termite gut biology and feeding strategies may improve the current state of biomass conversion technology and bioproduct production.
Results:
The study herein shows comprehensive functional characterization of crude body extracts from C. gestroi along with global proteomic analysis of the termite's digestome, targeting the identification of glycoside hydrolases (GH) and accessory proteins responsible for plant biomass conversion. The crude protein extract from C. gestroi was enzymatically efficient over a broad pH range on a series of natural polysaccharides, formed by glucose-, xylose-, mannan- and/or arabinose-containing polymers, linked by various types of glycosydic bonds, as well as ramification types. Our proteomic approach successfully identified a large number of relevant polypeptides in the C. gestroi digestome. A total of 55 different proteins were identified and classified into 29 CAZy families. Based on the total number of peptides identified, the majority of components found in the C. gestroi digestome were cellulose-degrading enzymes. Xylanolytic enzymes, mannan- hydrolytic enzymes, pectinases, and starch-degrading and debranching enzymes were also identified. Our strategy enabled validation of LC-MS/MS recognized proteins, by enzymatic functional assays and following degradation products of specific APTS labeled oligosaccharides through capillary zone electrophoresis.
Conclusions:
Here we describe the first global study about the enzymatic repertoire involved in plant polysaccharide degradation by the lower termite C. gestroi. The biochemical characterization of whole body termite extracts evidenced the ability to cleave all types of glycosidic bonds present in plant polysaccharides. The comprehensive proteomic analysis, revealed a complete collection of hydrolytic enzymes including cellulases (GH1, GH3, GH5, GH7, GH9 and CBM 6), hemicellulases (GH2, 10, 11, 16, 43 and CBM 27) and pectinases (GH28 and GH29).Source:
http://www.biotechnologyforbiofuels.com/rss/