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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Stabilization studies on bacterially produced human paraoxonase 1 for improving its shelf life
Priyanka Bajaj1, Abhay H Pande
1Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar, Mohali, 160062, Punjab, India.
Abstract:
Human paraoxonase 1 (h-PON1) is a ~40 kDa multi-tasking enzyme that plays a major role in determining individual susceptibility towards various disease conditions. It is a strong candidate for the development of therapeutic intervention for various diseases and other conditions in humans. However, purified h-PON1 is unstable and there is a need to find condition(s) that can increase the shelf life of the enzyme. In this report, we present the results of our investigation on the effect of excipients on the stability of bacterially produced human PON1 when stored under different storage conditions. Our results show that (a) glycine and serine are most effective in stabilizing the enzyme when stored in aqueous buffer at 25 °C for 30 days, and (b) trehalose, maltose, and BSA exerted maximum stabilization effect when the enzyme was stored in freeze-dried form at 25 °C for 60 days. Results of this study can be used to increase the shelf life of purified h-PON1 enzyme.
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