Characterization of the Wild-Type and Truncated Forms of a Neutral GH10 Xylanase from Coprinus cinereus: Roles of C-Terminal Basic Amino Acid-Rich Extension in Its SDS Resistance, Thermostability, and Activity
2017
Hang Hu, Nanjing Forestry University, Nanjing, China | Kaixiang Chen, Nanjing Forestry University, Nanjing, China | Lulu Li, Nanjing Forestry University, Nanjing, China | Liangkun Long, Nanjing Forestry University, Nanjing, China | Shaojun Ding, Nanjing Forestry University, Nanjing, China
A neutral xylanase (CcXyn) was identified from Coprinus cinereus. It has a single GH10 catalytic domain with a basic amino acid-rich extension (PVRRK) at the C-terminus. In this study, the wild-type (CcXyn) and C-terminus-truncated xylanase were heterologously expressed in Pichia pastoris and their characteristics were comparatively analyzed with aims to examine the effect of this extension on the enzyme function.
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