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1 April 2017 Molecular Cloning and Characterization of a Putative β-glucosidase from the Formosan Subterranean Termite (Isoptera: Rhinotermitidae)
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Abstract

Beta-glucosidases play an important role in the hydrolysis of cellulose and are among the cellulases in termites responsible for cellulose degradation and regulation of gene expression. A cDNA encoding putative β-glucosidase (CfBGIa) from the Formosan subterranean termite, Coptotermes formosanus Shiraki, was successfully cloned. The full-length of the cDNA of CfBGIa was 2,195 base pairs (bp) with an open reading frame of 1,500 bp that encoded for a 499–amino acid protein. Excluding a putative signal peptide of the first 21 amino acid residues, the 478-residue mature CfBGIa has a calculated molecular mass of 54.49 kDa. Sequence assessment and phylogenetic analysis suggested that CfBGIa belongs to β-glucosidase cluster I (BG-I group) encoding digestive enzymes. Homology modeling shows a classical (β/α)8 barrel structure of glycosyl hydrolase family 1 including two catalytic residues, Glu193 and Glu402. Quantitative PCR analysis in different temperatures revealed a similar expression pattern between CfBGIa and Co. formosanus clone Glu1B β-glucosidase mRNA. Both genes were induced in low (4°C) and high (38°C) temperatures. CfBGIa may prove to be a supplement to the cellulase system to improve the cellulose digestion in the termite, and these results might contribute to mining novel cellulases for cellulosic conversion.

Xiaolin Liu, Wenjing Wu, Dandan Zhang, and Zhiqiang Li "Molecular Cloning and Characterization of a Putative β-glucosidase from the Formosan Subterranean Termite (Isoptera: Rhinotermitidae)," Journal of Entomological Science 52(2), 177-192, (1 April 2017). https://doi.org/10.18474/0749-8004-52.2.177
Received: 1 August 2016; Accepted: 1 October 2016; Published: 1 April 2017
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