Stability of enzymes and proteins in dried glassy systems: effect of simulated sunlight conditions.
The purpose of the present work was to study the effects of simulated sunlight conditions on enzyme inactivation and structural damage in dehydrated glassy systems. Freeze-dried samples containing different enzymes (lactase, invertase, lysozyme and amyloglucosidase) were exposed to light using a medium-pressure metal halide HPA 400 W lamp. After 1 h of light exposure, the samples showed a significant reduction (more than 50%) in the denaturation peak area as analyzed by DSC, and this could be attributed to protein denaturation. For most of the pure enzymes, the loss of enzymic activity after 1 h of light exposure was around 50%. In the case of enzymes included in anhydrous model systems (trehalose, raffinose, maltodextrin, and dextran), the remaining activity also decreased dramatically during the light treatment. We showed that the light exposure in dehydrated systems generated both the loss of enzymic activity and structural changes such as denaturation (observed by DSC) and protein fragmentation and aggregation (observed by electrophoresis). Overall, we can conclude that a short exposure to the light produces dramatic changes in the enzymic activity in dehydrated systems with or without protective matrices.
Departamento de Industrias and Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, 1428 Buenos Aires, Argentina. lespinos@di.fcen.uba.ar
Luis
L
Espinosa
Carolina
C
Schebor
Norma S
NS
Nudelman
Jorge
J
Chirife
D002152:Calorimetry, Differential Scanning; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D005898:Glass; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013472:Sunlight
D004798:Enzymes; D011506:Proteins