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Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/6497
Title: Investigation on the stability of freeze dried horseradish peroxidase and immunoglobulin G
Authors: Dai, Jialu
Issue Date: 2010
Abstract: Protein pharmaceuticals are in mass production due to the advances in the hybridoma and genetics engineering but its stability remains an issue. 2 ~ 10 °C should be maintained during the transportation and production to achieve stability, but this is expensive and not always available. Freeze drying is a potential alternative but its effect is unknown. The instability of horseradish peroxidase (HRP), a representative enzyme, in aqueous solution at 2 ~ 40 °C was investigated. The kinetics of the catalytic activity reduction was first order and the rate constants were calculated. Arrhenius activation energy is 61.52 kJ/mol. Then the instability of freeze dried powder HRP stored at 4 ~ 40 °C, under nitrogen protection or exposed to air were examined. The activity change is not temperature dependent but experienced a drop and then an increase as a function of time. The activity change of the HRP exposed to air and Fourier transform infrared spectra (FTIR) results indicated that the activity change was a result of oxidation. The enzyme can survive in an ambient temperature for more than one month under nitrogen protection but not I air. Finally, immunoglobulin G (IgG) which has a potential for human disease treatment was freeze dried with different formulations. The bioactivity of IgG was best preserved with hepes buffer saline and a mass ratio of IgG to trehloase (a disaccharide) at 1:1. FTIR showed that unfolding and conformational change can be effectively reduced by adding protectant. In summary, kinetics method can be applied to the protein instability analysis; freeze drying with the addition of protectant can preserve the protein.
Description: Thesis (M.Phil.)--Hong Kong University of Science and Technology, 2010
xi, 96 p. : ill. ; 30 cm
HKUST Call Number: Thesis MECH 2010 Dai
URI: http://hdl.handle.net/1783.1/6497
Appears in Collections:MECH Master Theses

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