Abstract
β-1,3-glucanases are the main digestive enzymes of plant and fungal cell wall. Transcriptomic analysis of the fungus-growing termite Macrotermes barneyi revealed a high expression of a predicted β-1,3(4)-glucanase (Mbbgl) transcript in termite gut. Here, we described the cDNA cloning, heterologous expression, and enzyme characterization of Mbbgl. Sequence analysis and RT-PCR results showed that Mbbgl is a termite-origin GH16 β-1,3(4)-glucanase. The recombinant enzyme showed the highest activity towards laminarin and was active optimally at 50 °C, pH 5.5. The enzyme displayed endo/exo β-1,3(4)-glucanase activities. Moreover, Mbbgl had weak transglycosylation activity. The results indicate that Mbbgl is an endogenous digestive β-1,3(4)-glucanase, which contributes to the decomposition of plant biomass and fungal hyphae. Additionally, the multiple activities, pH, and ion stabilities make Mbbgl a potential candidate for application in the food industry.
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This study was supported by the National Natural Science Foundation of China (Grant Nos. 31970119 and 31272370).
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The experiment was designed and performed by Chunjing Cao and Jingjing Li. The data was analyzed by Jingjing Li, Chunjing Cao, and Yutong Jiang. The first draft of the manuscript was written by Chunjing Cao, Jingjing Li, and Jinfeng Ni. The manuscript was reviewed and edited by Qihong Huang, Yulong Shen, and Jinfeng Ni. All authors commented on previous versions of the manuscript. All authors had read and approved the final manuscript.
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Li, J., Cao, C., Jiang, Y. et al. A Novel Digestive GH16 β-1,3(4)-Glucanase from the Fungus-Growing Termite Macrotermes barneyi. Appl Biochem Biotechnol 192, 1284–1297 (2020). https://doi.org/10.1007/s12010-020-03368-w
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DOI: https://doi.org/10.1007/s12010-020-03368-w