Abstract
BackgroundLignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource. However, saccharification and the production of bioproducts derived from plant cell wall biomass are complex and lengthy processes. The understanding of termite gut biology and feeding strategies may improve the current state of biomass conversion technology and bioproduct production.ResultsThe study herein shows comprehensive functional characterization of crude body extracts from Coptotermes gestroi along with global proteomic analysis of the termite's digestome, targeting the identification of glycoside hydrolases 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 glycosidic 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 liquid chromatography with tandem mass spectrometry recognized proteins, by enzymatic functional assays and by following the degradation products of specific 8-amino-1,3,6-pyrenetrisulfonic acid labeled oligosaccharides through capillary zone electrophoresis.ConclusionsHere we describe the first global study on the enzymatic repertoire involved in plant polysaccharide degradation by the lower termite C. gestroi. The biochemical characterization of whole body termite extracts evidenced their 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, GH10, GH11, GH16, GH43 and CBM 27) and pectinases (GH28 and GH29).
Highlights
Lignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource
Biochemical characterization Here we describe the first global study of an enzymatic repertoire involved in plant polysaccharide degradation by C. gestroi
The crude extract was highly active on hydrolyzing glucose-containing polysaccharides, in both the linear and branched forms (Figure 1A), such as bglucan from barley; lichenan, a b-1-3:1-4 glucose linked polysaccharide; and laminarin, a b-1-3:1-6 glucose linkage polysaccharide
Summary
Lignocellulosic materials have been moved towards the forefront of the biofuel industry as a sustainable resource. The key mitigation action is replacing petroleum and its derivatives with renewable energy sources [1] In this context, lignocellulosic materials, which are an abundant glycoside hydrolases (GHs), proteins with carbohydratebinding modules (CBMs), glycoside transferases (GTs), laccases, peroxidases and detoxification proteins, such as superoxide dismutase and catalases [3]. Lignocellulosic materials, which are an abundant glycoside hydrolases (GHs), proteins with carbohydratebinding modules (CBMs), glycoside transferases (GTs), laccases, peroxidases and detoxification proteins, such as superoxide dismutase and catalases [3] These proteins are normally produced by fungi, bacteria, protozoa and even by animals [4], such as worms, beetles, cockroaches and termites, that carry complex symbiotic systems with cellulolytic microorganisms in their guts [5]. One of the best ways to understand termite digestomes is by coupling classical biochemical characterization with genomic and proteomic tools [8,9] based on a metagenomic platform for bioprospecting novel glycoside hydrolases [10]
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