An efficient procedure for the selection of high affinity clones from a heptapeptide phage display library was developed. Lysozyme was used as a model protein to demonstrate the selection strategy. Effect of bovine serum albumin (BSA) concentration on screening the phage library was discussed and proper BSA concentration on plate blocking was determined. The elution procedure was improved by alternatingly eluting the bound phages with glycine-HCl buffer (pH 2.2) and high-concentration target protein solution. The modified method was compared with others including the conventional protocol, and the results confirmed that the modified procedure could yield high affinity phages that might be lost by other screening methods. Through comparison of the DNA sequences of foreign peptides of the clones showing specificity to lysozyme molecules, the HWWW motif was found to be the necessary amino acid sequence for the affinity. The electrostatic and hydrophobic interactions are considered to contribute to the affinity for the protein. Moreover, protein chromatography with the immobilized HWWWPAS on Sepharose gel indicated the strong binding affinity of the peptide for lysozyme.