Abstract
The abundance and the diversity of oligo- and polysaccharides provide a wide range of biological roles attributed either to these carbohydrates or to their relevant enzymes, i.e., the glycoside hydrolases (GHs). The biocatalysis by these families of enzymes is highly attractive for the generation of products used in potential applications, e.g., pharmaceuticals and food industries. It is thus very important to extract and characterize such enzymes, particularly from plant tissues. In this study, we characterized novel sequences of class I chitinases from seedlings extract of the common oat (Avena sativa L.) using proteomics and sequence-structure-function analysis. These enzymes, which belong to the GH19 family of protein, were extracted from oat and identified using SDS-PAGE, trypsin digestion, LC-MS-MS, and sequence-structure-function analysis. The amino acid sequences of the oat tryptic peptides were used to identify cDNAs from the Avena sativa databases of the expressed sequence tags (ESTs) and transcriptome shotgun assembly (TSA). Based upon the Avena sativa sequences of ESTs and TSA, at least 4 predicted genes that encoded oat class I chitinases were identified and reported. The structural characterization of the oat sequences of chitinases provided valuable insights to the context.
Highlights
Glycoside hydrolases (GHs), for instance, chitinases, are good candidates for anti-pathogen agents, e.g., anti-insects and antifungal agents
Taken together these findings as well as the fact that oat seeds extract have previously denoted for their catalytic activity of highly abundant class I chitinases [13], the current study has proven the presence of many sequences of chitinases (GH19) and β-amylases (GH14) in 10day old oat seedlings extract
The continuing initiative to find novel plant carbohydrate-active enzymes (CAZymes) by such functional proteomics and genomic approaches is very interesting for the valorization of plant biomass as a substrate for various products in many areas, e.g., food and medicine
Summary
Glycoside hydrolases (GHs), for instance, chitinases, are good candidates for anti-pathogen agents, e.g., anti-insects and antifungal agents. Chitin, which an insoluble polysaccharide of β-(1,4)-linked Nacetyl-D-glucosamine residues, is the main constituent of cell walls of many fungal plant phytopathogens It can be decomposed by chitinases (EC 3.2.1.14) and plant chitinases are expressed during plant growth as well as plant and phytopathogen interactions. Most characterized chitinases are clustered into families 18 and 19 of the GHs based on primary structures similarities of their catalytic domains including class III and V and class I, II, IV, VI and VII chitinases, respectively [4, 5]. The glycan metabolism involved many kinds of carbohydrate-active enzymes (CAZymes), which are grouped into sequence-based families on the CAZY database [8], and the structural fold, as well as the catalytic mechanism, are highly conserved within these families. The most important CAZymes that depolymerize carbohydrate polymers are GHs [9]
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