Recombinant Expression of an Alkali Stable GH10 Xylanase from Paenibacillus barcinonensis

Abstract

Xylanase A from Paenibacillus barcinonensis, a new species isolated from a rice field, has been cloned and expressed in Escherichia coli. Purified recombinant xylanase showed high activity on xylans from hardwoods and cereals, and exhibited K(m) and V(max) of 2.93 mg/mL and 50.67 U/mg on birchwood xylan. Xylanase A was highly active at 60 degrees C in alkaline pH values up to 9.5 and remained stable for at least 3 h in alkaline conditions. The amino acid sequence deduced from xynA revealed that it is a single domain xylanase belonging to the GH10 family. Thin layer chromatography analysis showed that the enzyme released a mixture of hydrolysis products including substituted xylooligomers from cereal arabinoxylans, while xylose, xylobiose, and aldotetraouronic acid were the main products released from glucuronoxylan from birchwood. The enzyme released a complex mixture of xylooligomers for acetylated xylan from eucalyptus, revealing its potential to depolymerize this widely used resource in the pulp and paper industry.