Bacteriophages capable of binding cellulose matrix were screened from a 15-mer phage peptides library. In the deduced amino acid sequences of the screened phages, a characteristic region containing a conserved aromatic residue [tyrosine (Y) or phenylalanine (F)] was found, which is similar to the normal cellulose binding domains found in fungal and bacterial cellulose catalysase. Dot-ELISA showed that the phage containing sequence as SWYL has higher affinity to cellulose fibre than other phages, such as those containing sequences as CWYGNC, CWYGEC and XSWYDXXSWFSX. Results indicated that SWYL maybe a good candidate for cellulose binding motif. This work laid basis for further study on cellulose binding motif.
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