Heterologous expression and characterization of a novel glycoside hydrolase family 55 β-1,3-glucanase, AcGluA, from Archangium sp. strain AC19

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 K m and V max 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 .