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The directed evolution of proteins is a powerful technique to engineer novel enzymes with improved properties. Despite this, the identification of the underlying molecular changes occurring in the selected variants remains a challenging process. One approach is to characterize the differential protein expression of variants and identify those proteins that may have been causative to the enzyme performance improvement. Here we describe a versatile strategy of antibody microarray-based quantification of phage proteins and a parallel proteome-based approach to identify differentially expressed proteins in bacteriophage phiX174 phage lysate. We used the platform to monitor differential protein expression in phage variants expressing truncated proteins compared to the wild-type and then applied the phage lysate on a gold nanoparticles coated array for proteome screening. Of 76 unique proteins expressed in phiX174, 70 were expressed in at least one of the variants. Two new proteins and
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