@article{oai:soar-ir.repo.nii.ac.jp:00017843,
 author = {Nishijima,  Hiroto and Nozaki,  Kouichi and Mizuno,  Masahiro and Arai,  Tsutomu and Amano,  Yoshihiko},
 issue = {5},
 journal = {BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY},
 month = {May},
 note = {The xylanase (Xyn10B) that strongly adsorbs on microcrystalline cellulose was isolated from Driselase. The Xyn10B contains a Carbohydrate-binding module family 1 (CBM1) (IrpCBM(Xyn10B)) at N-terminus. The canonical essential aromatic residues required for cellulose binding were conserved in IrpCBM(Xyn10B); however, its adsorption ability was markedly higher than that typically observed for the CBM1 of an endoglucanase from Trametes hirsuta (ThCBMEG1). An analysis of the CBM-GFP fusion proteins revealed that the binding capacity to cellulose (7.8 mu mol/g) and distribution coefficient (2.0L/mu mol) of IrpCBM(Xyn10B)-GFP were twofold higher than those of ThCBMEG1-GFP (3.4 mu mol/g and 1.2L/mu mol, respectively), used as a reference structure. Besides the canonical aromatic residues (W24-Y50-Y51) of typical CBM1-containing proteins, IrpCBM(Xyn10B) had an additional aromatic residue (Y52). The mutation of Y52 to Ser (IrpCBM(Y52S)-GFP) reduced these adsorption parameters to 4.4 mu mol/g and 1.5L/mu mol, which were similar to those of ThCBMEG1-GFP. These results indicate that Y52 plays a crucial role in strong cellulose binding., Article, BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY. 79(5):738-746 (2015)},
 pages = {738--746},
 title = {Extra tyrosine in the carbohydrate-binding module of Irpex lacteus Xyn10B enhances its cellulose-binding ability},
 volume = {79},
 year = {2015}
}