Authors:
J. Lu Nanyang Technological University Division of Chemical and Biomolecular Engineering Nanyang Singapore

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X. Wang Nanyang Technological University Division of Chemical and Biomolecular Engineering Nanyang Singapore

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Y. Liu Nanyang Technological University Division of Chemical and Biomolecular Engineering Nanyang Singapore

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C. Ching Nanyang Technological University Division of Chemical and Biomolecular Engineering Nanyang Singapore

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Abstract  

The effect of excipients on the secondary structure of lyophilized proteins was studied through second-derivative Fourier transform infrared (FTIR) spectroscopic analysis. The glass transition temperature (Tg), denaturation temperature (Td) and moisture content were determined by differential scanning calorimetry (DSC) and thermogravimetry (TG). Tg, Td and the preservation of protein secondary structure were found to be dependent upon the type and amount of the excipient included in the formulation. Meanwhile, the lyophilized proteins easily adsorbed amounts of moisture during storage to reduce their Tgs and stability.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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