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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Notes
P. Bajaj, G. Aggarwal, R.K. Tripathy, and A.H. Pande, Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1. (submitted for publication).
Abbreviations
- h-PON1:
-
Human paraoxonase 1
- bph-PON1:
-
Bacterially produced human paraoxonase 1
- CMC:
-
Carboxy methyl cellulose
- PAA:
-
Polyacrylic acid
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Acknowledgments
This work was supported by the research grants to AHP from NIPER, SAS Nagar. The authors thank Prof. K.P.R. Kartha, Department of Chemistry, NIPER-SAS Nagar, for his valuable assistance in writing the manuscript. Priyanka Bajaj (CSIR-SPM-SRF) is thankful to CSIR, New Delhi, for financial support in the form of CSIR Fellowship.
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Bajaj, P., Pande, A.H. Stabilization Studies on Bacterially Produced Human Paraoxonase 1 for Improving Its Shelf Life. Appl Biochem Biotechnol 172, 3798–3809 (2014). https://doi.org/10.1007/s12010-014-0806-5
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DOI: https://doi.org/10.1007/s12010-014-0806-5