Inhibiting the Catalytic Activity of Family GH11 Xylanases by Recombinant Rice Xylanase-Inhibiting Protein

August 13, 2018

Title

Inhibiting the Catalytic Activity of Family GH11 Xylanases by Recombinant Rice Xylanase-Inhibiting Protein

Author

Ya-hui Dang, Ming-qi Liu, Qian Wang

Year

2018

Journal

Catalysis Letters

Abstract

ricexip, a xylanase-inhibiting protein (XIP)-type gene, was expressed in Escherichia coli BL21 (DE3). The recombinant protein, reEriceXIP significantly inhibited catalytic activity of several xylanases. Optimal inhibitory activity of reEriceXIP on xylanase (TfxA_CD214 and reBaxA454) occurred at 40 °C for 30 min. reEriceXIP decreased fluorescence intensity of xylanase and changed its secondary structure. reEriceXIP decreased global concentration of hydrolytes released from beechwood xylan.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Chemical stability, Biochemistry