Abstract
The effects of amphiphilic additives on inactivation of β-galactosidase during freeze-drying were studied in comparison with those of sugars and amino acids. The activity loss was greater when the enzyme was freeze-dried from solutions of lower enzyme concentration without additives. Well-known cryoprotectants such as sugars and amino acids provided concentration-dependent preservation of enzyme activity. Hydroxypropyl-β-cyclodextrin (HP-β-CD), 2,6-di- O-methyl-β-cyclodextrin (DM-β-CD), 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS) and sucrose fatty acid monoester stabilized the enzyme at much lower concentrations than-sugars and amino acids. Polyethylene glycol 400 (PEG 400), polyoxyethylene 9 lauryl ether (polydocanol) and sodium dodecyl sulfate (SDS), however, were ineffective or rather induced inactivation. High-performance size-exclusion chromatography indicated the formation of soluble aggregates during freeze-drying without additives, which was inhibited by the sugar ester. SDS-PAGE indicated that the aggregates were formed by noncovalent bonding
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