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From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase
2000
Protein Engineering Design & Selection
Naturally-occurring phytases having the required level of thermostability for application in animal feeding have not been found in nature thus far. We decided to de novo construct consensus phytases using primary protein sequence comparisons. A consensus enzyme based on 13 fungal phytase sequences had normal catalytic properties, but showed an unexpected 15-22°C increase in unfolding temperature compared with each of its parents. As a first step towards understanding the molecular basis of
doi:10.1093/protein/13.1.49
pmid:10679530
fatcat:h5yht75e4bdptdcth3i74rtena