Impact of the removal of N-terminal non-structured amino acids on activity and stability of xylanases from Orpinomyces sp. PC-2

摘要

Graphical abstractDisplay OmittedHighlights?Molecular dynamics analyses indicated that N-terminal tail could destabilize the XynA xylanase fromOrpinomyces.?N-terminal tail removal positively affected the expression and activity of xylanases.?Engineered xylanases showed high thermostability at 50°C.AbstractXylanases catalyze the random hydrolysis of xylan backbone from plant biomass and thus, they have application in the production of biofuels, Kraft pulps biobleaching and feed industry. Here, xylanases derived fromOrpinomycessp. PC-2 were engineered guided by molecular dynamics methods to obtain more thermostable enzymes. Based on these models, 27 amino acid