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Stable high surface area lactate dehydrogenase particles produced by spray freezing into liquid nitrogen

Authors
Journal
European Journal of Pharmaceutics and Biopharmaceutics
0939-6411
Publisher
Elsevier
Publication Date
Volume
65
Issue
2
Identifiers
DOI: 10.1016/j.ejpb.2006.08.002
Keywords
  • Lactate Dehydrogenase (Ldh)
  • Spray Freezing Into Liquid (Sfl)
  • Spray Freeze-Drying (Sfd)
  • Gas–Liquid Interface
  • Atomization
Disciplines
  • Biology
  • Medicine

Abstract

Abstract Enzyme activities were determined for lactate dehydrogenase (LDH) powder produced by lyophilization, and two fast freezing processes, spray freeze-drying (SFD) and spray freezing into liquid (SFL) nitrogen. The 0.25 mg/mL LDH aqueous feed solutions included either 30 or 100 mg/mL trehalose. The SFL process produced powders with very high enzyme activities upon reconstitution, similar to lyophilization. However, the specific surface area of 13 m 2/g for SFL was an order of magnitude larger than for lyophilization. In SFD activities were reduced in the spraying step by the long exposure to the gas–liquid interface for 0.1–1 s, versus only 2 ms in SFL. The ability to produce stable high surface area submicron particles of fragile proteins such as LDH by SFL is of practical interest in protein storage and in various applications in controlled release including encapsulation into bioerodible polymers. The SFL process has been scaled down for solution volumes <1 mL to facilitate studies of therapeutic proteins.

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