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Scientia Pharmaceutica is published by MDPI from Volume 84 Issue 3 (2015). Articles in this Issue were published by another publisher in Open Access under a CC-BY (or CC-BY-NC-ND) licence. Articles are hosted by MDPI on as a courtesy and upon agreement with Austrian Pharmaceutical Society (Österreichische Pharmazeutische Gesellschaft, ÖPhG).
Open AccessArticle
Sci. Pharm. 2015, 83(2), 401-410; (registering DOI)

Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients

Department of Pharmaceutical Technology and Biopharmaceutics, University of Vienna, Althanstrasse 14, A-1090 Vienna, Austria.
Bioprocessing Technology Institute, A*STAR, 20 Biopolis Way, #06-01, Centros, 138668, Singapore.
Author to whom correspondence should be addressed.
Received: 21 January 2015 / Accepted: 4 March 2015 / Published: 4 March 2015
PDF [139 KB, uploaded 8 September 2016]


Protease activity from host cell lines may cause product loss or affect the quality of recombinant proteins. In this study, we showed that excipients like glycine and sorbitol reduce the proteolysis of an immunoglobulin M (IgM) in the presence of added proteases like α-chymotrypsin, papain, and pepsin. The activity of the proteases in the IgM-protective environments was conserved or even enhanced as tested using low molecular weight substrates. Thus, a higher resistance against proteolytic degradation appears to be caused by the conformational stabilization of the IgM due to preferential exclusion of sorbitol and glycine.
Keywords: IgM; Proteolysis; Conformational stability; Sorbitol; Glycine IgM; Proteolysis; Conformational stability; Sorbitol; Glycine
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MUELLER, M.; LOH, M.Q.T.; GAGNON, P. Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients. Sci. Pharm. 2015, 83, 401-410.

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