Characterization of Paenibacillus curdlanolyticus B-6 Xyn10D, a xylanase that contains a family 3 carbohydrate-binding module

Journal article

Authors/Editors

KHANOK RATANAKHANOKCHAI

Strategic Research Themes

No matching items found.

Publication Details

Author list: Sakka M., Higashi Y., Kimura T., Ratanakhanokchai K., Sakka K.

Publisher: American Society for Microbiology

Publication year: 2011

Journal: Applied and Environmental Microbiology (0099-2240)

Volume number: 77

Issue number: 12

Start page: 4260

End page: 4263

Number of pages: 4

ISSN: 0099-2240

eISSN: 1098-5336

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-79960088590&doi=10.1128%2fAEM.00226-11&partnerID=40&md5=b2550596df0df9fc4f79a76b5195070f

Languages: English-Great Britain (EN-GB)

View in Web of Science | View on publisher site | View citing articles in Web of Science

Abstract

Paenibacillus curdlanolyticus B-6 Xyn10D is a xylanase containing a family 3 carbohydrate-binding module (CBM3). Biochemical analyses using recombinant proteins derived from Xyn10D suggested that the CBM3 polypeptide has an affinity for cellulose and xylan and that CBM3 in Xyn10D is important for hydrolysis of insoluble arabinoxylan and natural biomass. ฉ 2011, American Society for Microbiology.

Keywords