Some implications of structural collapse during freeze-drying using Erwinia caratovora L-asparaginase as a model.
Some implications of structural collapse during freeze-drying using Erwinia caratovora L-asparaginase as a model.
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使用欧文氏菌 L-天冬酰胺酶作为模型冷冻干燥过程中结构崩溃的一些影响。
DOI：
10.1002/jctb.280580110
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发表时间：
2007
影响因子：
3.4
通讯作者：
L. Irons
中科院分区：
文献类型：
--
作者：
G. Adams;L. Irons
当酶欧文氏菌caratovora L-天冬酰胺酶在乳糖和氯化钠的混合物中冷冻干燥时，生物活性和蛋白质结构在干燥过程中得以保留。然而，通过改变制剂中赋形剂的比例，可以获得药学上可接受或不可接受的产品，如通过干燥饼外观、水分含量或重构容易性的标准所评估的。
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.