Elucidating The Lignocellulose Digestion Mechanism Coptotermes curvignathus Based on Carbohydrate-Active Enzymes Profle Using The Meta-Transcriptomic Approach
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Published:2023-12-15
Issue:5
Volume:52
Page:177-186
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ISSN:2462-151X
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Container-title:Malaysian Applied Biology
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language:
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Short-container-title:MAB
Author:
Hoe Pik Kheng,King Jie Hung,Ong Kian Huat,Bong Choon Fah,Mahadi Nor Muhammad
Abstract
Termites are efficient lignocellulose decomposers that thrive on woody materials and contribute to carbon mineralization in both tropical and subtropical regions. Due to hydrolytic stability and crosslinking between the polysaccharides (cellulose & hemicellulose) and the lignin via ester and ether linkages, termites would require a large variety of enzymes to degrade lignocellulose. Coptotermes curvignathus, an endemic species of termite from Southeast Asia, has been classified as an urban pest in the region and is known as the largest and most aggressive among the oriental Coptotermes spp. Its Carbohydrate-Active enzymes (CAZymes) are the main interest of this study. RNA of C. curvignathus was extracted and sequenced using Illumina Hiseq 2000 sequencing platform, and de novo assembled with Trinity pipeline. There were 101 CAZymes families in C. curvignathus digestome. CAZymes break down complex carbohydrates and glycoconjugates for a large body of biological roles and perform their function, usually with high specificity. Enzymes coding for glycosyl hydrolase (GH) families had the highest transcript abundance, accounting for about 93% of the total CAZymes reads. This was followed by CBM (≈1%), GT family (≈4%), CE family (<1%), AA family (<2%), and PL family (<1%). Due to the carbohydrate diversity exceeding the number of protein folds, CAZymes have evolved from a limited number of progenitors by acquiring novel specificities at substrate and product levels. Such a dizzying array of substrates and enzymes makes C. curvignathus a high-performance lignocellulose degrader.
Funder
Kementerian Sains, Teknologi dan Inovasi
Publisher
Persatuan Biologi Gunaan Malaysia
Subject
General Agricultural and Biological Sciences
Reference36 articles.
1. Agger, J., Viksø-Nielsen, A. & Meyer, A.S. 2010. Enzymatic xylose release from pretreated corn bran arabinoxylan: Differential effects of deacetylation and deferuloylation on insoluble and soluble substrate fractions. Journal of Agricultural and Food Chemistry, 58(10): 6141-6148. 2. Baumann, M.J., Eklöf, J.M., Michel, G., Kallas, A.M., Teeri, T.T., Czjzek, M. & Brumer, H. 2007. Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: Biological implications for cell wall metabolism. The Plant Cell, 19(6): 1947-1963. 3. Beaugrand, J., Chambat, G., Wong, V.W., Goubet, F., Rémond, C., Paës, G., Benamrouche, S., Debeire, P., O’Donohue, M. & Chabbert, B. 2004. Impact and efficiency of GH10 and GH11 thermostable endoxylanases on wheat bran and alkali-extractable arabinoxylans. Carbohydrate Research, 339(15): 2529-2540. 4. Bray, N.L., Pimentel, H., Melsted, P. & Pachter, L. 2016. Near-optimal probabilistic RNA-seq quantification. Nature Biotechnology, 34: 525-527. 5. Brennan, Y., Callen, W.N., Christoffersen, L., Dupree, P., Goubet, F., Healey, S., Hernández, M., Keller, M., Li, K., Palackal, N., Sittenfeld, A., Tamayo, G., Wells, S., Hazlewood, G.P., Mathur, E.J., Short, J.M., Robertson, D.E. & Steer, B.A. 2004. Unusual microbial xylanases from insects guts. Applied and Environmental Microbiology, 70(6): 3609-3617.
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