Stabilization of Arthrobacter viscosus Penicillin G Acylase
A wide array of additives, including polymers, sugars, and amino acids, was examined in order to enhance the Arthrobacter viscosus NRRL B-1973 penicillin G acylase (PGA) thermal stability and also to stabilize PGA against the lyophilization process stresses. Among all the tested additives, diethylaminoethyl dextran (DEAE dextran) was the upmost thermal stabilizer. As it brought about a 14.5 fold increase in the half-life of PGA from 0.931 h (for the control without additives) to 13.535 h and also reduced the first-order thermal denaturation constant at 60 °C from 0.745 h–1 to 0.051 h–1. On the other hand, arginine offered PGA maximum stabilization during the lyophilization process. Consequently, combination of DEAE dextran and arginine into a single formula offered PGA full protection against the lyophilization stresses.
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Document Type: Research Article
Publication date: December 1, 2013
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