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Some implications of structural collapse during freeze‐drying using Erwinia caratovora L ‐asparaginase as a model
Author(s) -
Adams G. D. J.,
Irons L. I.
Publication year - 1993
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280580110
Subject(s) - erwinia , lactose , food science , chemistry , maillard reaction , sodium , chromatography , biochemistry , organic chemistry , gene
When the enzyme Erwinia caratovora L ‐asparaginase was freeze‐dried in mixtures of lactose and sodium chloride, biological activity and protein structure were preserved during drying. However, by altering the ratios of the excipients in the formulation it was possible to obtain products which were pharmaceutically acceptable or unacceptable as assessed by the criteria of dried cake appearance, moisture content or ease of reconstitution.