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Abstract
The gene coding for a lichenase from Paenibacillus barcinonensis BP-23, a powerful carbohydrate-degrading strain, was obtained using a genome walking strategy and expressed in Escherichia coli for further characterization. The amino acid sequence deduced from lic16A revealed that the lichenase is a single-domain enzyme belonging to the GH16 family. Purified recombinant Lic16A showed exclusive activity on β-1,3-1,4-glucans, showing a Km of 16.88 mg/mL and a Vmax of 266.09 U/mg using lichenan as a substrate. Lic16A was stable at 55°C for at least 3 H in moderate pH conditions. Thin-layer chromatography analysis showed that the enzyme released a complex mixture of hydrolysis products, which consisted of different length oligosaccharides of intermediate mobility among cellooligomers. The health benefits of β-glucans's consumption and the increased interest for the use of their oligomers as prebiotics add interest to the study of Lic16A for the production of β-glucan-derived oligosaccharides and the evaluation of their biotechnological potential. This is the first report on β-1,3-1,4-glucanase produced by P. barcinonensis.
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