Abstract
A xylanase gene from Paecilomyces thermophila was functionally expressed in Pichia pastoris. The recombinant xylanase (xynA) was predominantly extracellular; in a 5l fermentor culture, the total extracellular protein was 8.1gl(-1) with an activity of 52,940Uml(-1). The enzyme was purified to homogeneity with a recovery of 48%. The recombinant xynA was optimally active at 75°C, as measured over 10min, and at pH 7. The enzyme was stable up to 80°C for 30min. It hydrolyzed birchwood xylan, beechwood xylan and xylooligosaccharides to produce xylobiose and xylotriose as the main products.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
