Investigation of the reversibility of freeze/thaw stress-induced protein instability using heat cycling as a function of different cryoprotectants.

Abstract:

:Formulation conditions have a significant influence on the degree of freeze/thaw (FT) stress-induced protein instabilities. Adding cryoprotectants might stabilize the induced FT stress instabilities. However, a simple preservation of protein stability might be insufficient and further methods are necessary. This study aims to evaluate the addition of a heat cycle following FT application as a function of different cryoprotectants with lysozyme as exemplary protein. Sucrose and glycerol were shown to be the most effective cryoprotectants when compared to PEG200 and Tween20. In terms of heat-induced reversibility of aggregates, glycerol showed the best performance followed by sucrose, NaCl and Tween20 systems. The analysis was performed using a novel approach to visualize complex interplays by a clustering and data reduction scheme. In addition, solubility and structural integrity were measured and confirmed the obtained results.

journal_name

Bioprocess Biosyst Eng

authors

Wöll AK,Hubbuch J

doi

10.1007/s00449-020-02327-3

subject

Has Abstract

pub_date

2020-07-01 00:00:00

pages

1309-1327

issue

7

eissn

1615-7591

issn

1615-7605

pii

10.1007/s00449-020-02327-3

journal_volume

43

pub_type

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