Rationalizing Protein Design
We are on a mission to help scientists to rapidly identify and select the right protein for their specific applications. Based on the combination of a highly intuitive web software and substantial expertize in bioinformatics, we can support you to optimize your screening and experimental efforts. In a reliable, time and cost effective manner.
Starting with experimentally resolved or 3D-modeled structures, our solution enables in silico prediction of mutations for stability and thermal resistance changes.
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Applications
Modified proteins with controlled stability, through amino acid substitutions is of extreme importance in a whole range of applications where proteins are used for their catalytic or other functional activities, sometimes under unusual conditions. In various industries, including agro-food, biopharmaceutical and environment our solution enables to identify optimized proteins that will eventually increase the productivity and reduce the cost.
Food Industry
Research manager
Working with dezyme was both a valuable and rewarding experience.
The challenge was to predict and characterize modified versions of an enzyme of interest for agro-food applications. Dezyme experts team rapidly identified in silico three relevant mutants. After various experimental in-house tests, mutants' thermostability was strongly improved compared to the wild-type. Dezyme's support have been mainly beneficial to our process improvement.
Zhong-Liu Wu
Scientific at Chengdu Institute of Biology
Dezyme software allowed us to increase significantly the thermostability of feruloyl esterase A.
Dezyme PoPMuSiC algorithm helped us in thermostabilizing Feruloyl esterases. FaeA is a key enzyme involved in the hydrolysis of lignocellulose biomass. Two amino acid substitutions identified by the PoPMuSiC software, greatly increased the thermostability of FaeA. The construction of the double mutant led to significant enhanced thermostability, and increased catalytic efficiency.
Zhang & Wu, Bioresource Technology 102 (2011) 2093–2096