Extra tyrosine in the carbohydrate-binding module ofIrpex lacteusXyn10B enhances its cellulose-binding ability
作者： Hiroto Nishijima , Kouichi Nozaki , Masahiro Mizuno , Tsutomu Arai , Yoshihiko Amano
DOI: 10.1080/09168451.2014.996203
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摘要: The xylanase (Xyn10B) that strongly adsorbs on microcrystalline cellulose was isolated from Driselase. Xyn10B contains a Carbohydrate-binding module family 1 (CBM1) (IrpCBMXyn10B) at N-terminus. canonical essential aromatic residues required for binding were conserved in IrpCBMXyn10B; however, its adsorption ability markedly higher than typically observed the CBM1 of an endoglucanase Trametes hirsuta (ThCBMEG1). An analysis CBM-GFP fusion proteins revealed capacity to (7.8 μmol/g) and distribution coefficient (2.0 L/μmol) IrpCBMXyn10B-GFP twofold those ThCBMEG1-GFP (3.4 μmol/g 1.2 L/μmol, respectively), used as reference structure. Besides (W24-Y50-Y51) typical CBM1-containing proteins, IrpCBMXyn10B had additional residue (Y52). mutation Y52 Ser (IrpCBMY52S-GFP) reduced these parameters 4.4 μmol/g 1.5 L/μmol, which similar tho...
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