Heterologous expression and characterization of a novel glycoside hydrolase family 55 β-1,3-glucanase, AcGluA, from Archangium sp. strain AC19
2021
Wang, Yanxin | Li, Ding | Dong, Chaonan | Zhao, Yuqiang | Zhang, Lei | Yang, Fan | Ye, Xianfeng | Huang, Yan | Li, Zhoukun | Cui, Zhongli
Some microbial-associated molecular patterns (MAMPs), like glucan oligosaccharides, can be recognized by pattern recognition receptors (PRRs) of plant to elicit further immunity response. In this study, a novel glycoside hydrolase family 55 β-1,3-glucanase (AcGluA) from Archangium sp. strain AC19 was cloned and expressed in Escherichia coli. Among the reported β-1, 3-glucanases from the glycoside hydrolase 55 family, the purified AcGluA exhibited the highest activity on laminarin at pH 6.0 and 60 °C with 112.3 U/mg. Activity of AcGluA was stable in the range of pH 4.0–9.0 and at temperatures below 60 °C. The Kₘ and Vₘₐₓ of AcGluA for laminarin were 3.5 mg/ml and 263.5 μmol/(ml·min). AcGluA hydrolyzed laminarin into a series of oligosaccharides, suggesting it was an endo-β-1,3-glucanase. The high dose of oligosaccharides (1600 mg/l) had conspicuous biocontrol efficacy on the defense of rice seedlings to Magnaporthe oryzae, which provided a new idea for the development of green biopesticide.Key points• The AcGluA was determined bacteria-derived β-1,3-glucanases in the GH55 family.• The AcGluA showed the highest activity towards laminarin among reported GH55 family.• The hydrolysates of laminarin showed conspicuous biocontrol efficacy to M. oryzae.
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