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New GH16 β‐glucanase from Paenibacillus barcinonensis BP‐23 releases a complex pattern of mixed‐linkage oligomers from barley glucan
Author(s) -
Cerda Liliana Alexandra,
Valenzuela Susana Valeria,
Diaz Pilar,
Pastor Francisco I. Javier
Publication year - 2015
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1348
Subject(s) - glucanase , glucan , enzyme , paenibacillus , hydrolysis , biochemistry , chemistry , escherichia coli , food science , biology , gene , 16s ribosomal rna
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 K m of 16.88 mg/mL and a V max 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 .