Stable high surface area lactate dehydrogenase particles produced by spray freezing into liquid nitrogen.
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 0.1-1s, 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.
Engstrom
Josh D
JD
Department of Chemical Engineering, The University of Texas at Austin, Austin, TX 78712, USA.
Simpson
Dale T
DT
Cloonan
Carrie
C
Lai
Edwina S
ES
Williams
Robert O
RO
Barrie Kitto
G
G
Johnston
Keith P
KP
D000818:Animals; D002384:Catalysis; D004339:Drug Compounding; D004355:Drug Stability; D005079:Excipients; D005612:Freeze Drying; D005615:Freezing; D006813:Humidity; D007770:L-Lactate Dehydrogenase / Q000737:chemistry*; D008855:Microscopy, Electron, Scanning; D009206:Myocardium / Q000201:enzymology; D053758:Nanoparticles; D009584:Nitrogen; D011208:Powders; D013499:Surface Properties; D013552:Swine
D005079:Excipients; D011208:Powders; D007770:L-Lactate Dehydrogenase; D009584:Nitrogen