Identification of cellulose-binding peptides and its application for cellulase reaction

显示随机和线性七肽/十肽的噬菌体文库应用于结晶纤维素。用酶联免疫吸附法（elisa）定量分析所得噬菌体克隆的结合亲和力。获得的克隆具有比文库更大的表观亲和常数，表明分离到了具有特征序列的纤维素结合肽。经高效液相色谱法测定，具有鉴定序列的合成肽的亲和常数为10^5 ~ 6 mol/L，与纤维素结合域天然蛋白的亲和常数一致。

Phage libraries displaying random and linear hepta/dedecapeptides were applied to crystalline cellulose. Binding affinities of obtained phage clones were quantitatively analyzed by enzymelinked immunosorbent assays (ELISAs). Clones were obtained with greater apparent affinity constants than those of the library, suggesting the isolation of cellulose-binding peptides with characteristic sequences. Furthermore, synthetic peptides with identify sequences showed the affinity constant, which was determined by high performance liquid chromatography, 10^5-10^6 mol/L corresponding to that of natural protein from cellulose binding domain.