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Freeze-drying Process (freeze-drying + process)
Selected AbstractsSolute crystallization in mannitol,glycine systems,implications on protein stabilization in freeze-dried formulationsJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 11 2003Abira Pyne Abstract The use of mannitol in combination with glycine has resulted in stable freeze-dried protein formulations. Our objectives were to (1) study solute crystallization in ternary systems containing mannitol, glycine, and water during all the stages of freeze drying as a function of processing conditions and formulation variables; (2) investigate the effect of sodium phosphate buffer salts on the crystallization of both mannitol and glycine and vice versa; and (3) investigate the effects of these excipients in a freeze-dried lactate dehydrogenase (LDH) formulation. X-ray powder diffractometry (XRD) and differential scanning calorimetry (DSC) were used to study the frozen aqueous solutions. Phase transitions during primary and secondary drying were monitored by simulating the entire freeze-drying process in situ in the sample chamber of the diffractometer. LDH activity after freeze drying was determined spectrophotometrically. In frozen aqueous solutions containing mannitol and glycine, each solute influenced the extent of crystallization of the other. The solutes crystallized as ,-mannitol and ,-glycine during primary drying. Glycine had a stronger tendency to crystallize, while it was easier to influence mannitol crystallization. The buffer salts inhibited the crystallization of mannitol and glycine. However, in some cases, during primary drying, glycine crystallization was followed by that of disodium hydrogen phosphate dodecahydrate. The latter underwent dehydration forming an amorphous anhydrate. It was possible to correlate the extent of crystallization of mannitol and glycine in the lyophile with the retention of protein activity. An increase in buffer concentration decreased the crystallinity of mannitol and glycine. This translated to increased retention of protein activity. © 2003 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 92:2272,2283, 2003 [source] Stabilization of alum-adjuvanted vaccine dry powder formulations: Mechanism and applicationJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 2 2003Yuh-Fun Maa Abstract Studies were performed to elucidate the mechanism of alum gel coagulation upon freezing and drying and its relationship to vaccine potency loss and to develop a novel freeze-drying process for the production of stable alum-adjuvanted vaccine formulations suitable for conventional needle injection and epidermal powder immunization (EPI). The alum hydroxide-adjuvanted hepatitis-B surface antigen (Alum-HBsAg) and the alum phosphate-adjuvanted diphtheria and tetanus toxoids (Alum-DT) were dehydrated by freeze drying (FD), spray drying (SD), air drying (AD), or spray freeze drying (SFD). After drying by FD, SD, or AD, alum gels coagulated when examined by optical microscopy and particle size analysis. In addition, desorption of antigen molecules from the coagulated when examined by optical microscopy and particle size analysis. In addition, desorption of antigen molecules from the coagulated alum gel upon reconstitution appeared to be difficult, as indicated by attenuated band intensity on SDS-PAGE. In contrast, SFD alum gels turned a homogenous suspension upon reconstitution, suggesting minimal alum coagulation. In the mouse model, the in vivo immunogenicity of SFD Alum-HBsAg was preserved, whereas the FD Alum-HBsAg suffered significant immunogenicity loss. Grinding of coagulated FD Alum-HBsAg into smaller particles could partially recover the immunogenicity. In a guinea pig study using EPI, the SD Alum-DT formulation was not immunogenic, but the SFD Alum-DT formulations had a vaccine potency comparable to that of the untreated DT administered by I.M. injection. Overall, the relationship of coagulation of alum gel upon reconstitution and the loss of vaccine potency was established in this study. Alum gels became highly coagulated after dehydration by spray drying and traditional freeze-drying processes. However, freezing rate played a critical role in preserving the adjuvant effect of alum and fast freezing decreased the tendency of alum coagulation. Spraying the alum gel into liquid nitrogen represents the fastest freezing rate achievable and resulted in no discernible alum coagulation. Therefore, SFD presents a novel and effective drying process for alum-adjuvanted vaccine formulations and is particularly valuable for dry powder applications such as EPI. © 2003 Wiley-Liss, Inc. and the American Pharmaceutical Association J Pharm Sci 92:319,332, 2003 [source] Synthesis of Porous Silicon Nitride with Unidirectionally Aligned Channels Using Freeze-Drying ProcessJOURNAL OF THE AMERICAN CERAMIC SOCIETY, Issue 9 2002Takayuki Fukasawa Porous silicon nitride with macroscopically aligned channels was synthesized using a freeze-drying process. Freezing of a water-based slurry of silicon nitride was done while unidirectionally controlling the growth direction of the ice. Pores were generated subsequently by sublimation of the columnar ice during freeze-drying. By sintering this green body, a porous silicon nitride with high porosity (over 50%) was obtained and its porosity was controllable by the slurry concentration. The porous Si3N4 had a unique microstructure, where macroscopically aligned open pores contained fibrous grains protruding from the internal walls of the Si3N4 matrix. It is hypothesized that vapor/solid phase reactions were important to the formation mechanism of the fibrous grains. [source] Stabilization of alum-adjuvanted vaccine dry powder formulations: Mechanism and applicationJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 2 2003Yuh-Fun Maa Abstract Studies were performed to elucidate the mechanism of alum gel coagulation upon freezing and drying and its relationship to vaccine potency loss and to develop a novel freeze-drying process for the production of stable alum-adjuvanted vaccine formulations suitable for conventional needle injection and epidermal powder immunization (EPI). The alum hydroxide-adjuvanted hepatitis-B surface antigen (Alum-HBsAg) and the alum phosphate-adjuvanted diphtheria and tetanus toxoids (Alum-DT) were dehydrated by freeze drying (FD), spray drying (SD), air drying (AD), or spray freeze drying (SFD). After drying by FD, SD, or AD, alum gels coagulated when examined by optical microscopy and particle size analysis. In addition, desorption of antigen molecules from the coagulated when examined by optical microscopy and particle size analysis. In addition, desorption of antigen molecules from the coagulated alum gel upon reconstitution appeared to be difficult, as indicated by attenuated band intensity on SDS-PAGE. In contrast, SFD alum gels turned a homogenous suspension upon reconstitution, suggesting minimal alum coagulation. In the mouse model, the in vivo immunogenicity of SFD Alum-HBsAg was preserved, whereas the FD Alum-HBsAg suffered significant immunogenicity loss. Grinding of coagulated FD Alum-HBsAg into smaller particles could partially recover the immunogenicity. In a guinea pig study using EPI, the SD Alum-DT formulation was not immunogenic, but the SFD Alum-DT formulations had a vaccine potency comparable to that of the untreated DT administered by I.M. injection. Overall, the relationship of coagulation of alum gel upon reconstitution and the loss of vaccine potency was established in this study. Alum gels became highly coagulated after dehydration by spray drying and traditional freeze-drying processes. However, freezing rate played a critical role in preserving the adjuvant effect of alum and fast freezing decreased the tendency of alum coagulation. Spraying the alum gel into liquid nitrogen represents the fastest freezing rate achievable and resulted in no discernible alum coagulation. Therefore, SFD presents a novel and effective drying process for alum-adjuvanted vaccine formulations and is particularly valuable for dry powder applications such as EPI. © 2003 Wiley-Liss, Inc. and the American Pharmaceutical Association J Pharm Sci 92:319,332, 2003 [source] The influence of additives and drying methods on quality attributes of fish protein powder made from saithe (Pollachius virens)JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 12 2010Gholam Reza Shaviklo Abstract BACKGROUND: Fish protein powder (FPP) is used in the food industry for developing formulated food products. This study investigates the feasibility of increasing the value of saithe (Pollachius virens) by producing a functional FPP. Quality attributes of spray and freeze-dried saithe surimi containing lyoprotectants were studied. A freeze-dried saithe surimi without lyoprotectants was also prepared as a control sample. RESULTS: The amount of protein, moisture, fat and carbohydrate in the FPPs were 745,928, 39,58, 21,32 and 10,151 g kg,1. Quality attributes of FPPs were influenced by the two drying methods and lyoprotectants. The highest level of lipid oxidation was found in the control and the second highest in the spray-dried FPP. The spray-dried fish protein had the lowest viscosity among all FPPs. Gel-forming ability of samples with lyoprotectants was higher than that of the control. Water-binding capacity, emulsion properties and solubility of the freeze-dried fish protein containing lyoprotectants were significantly higher than spray-dried and control samples. However, functional properties of spray-dried FPP were higher than the control sample. CONCLUSION: It is feasible to develop value-added FPP from saithe surimi using spray- and freeze-drying processes, but freeze-dried FPP containing lyoprotectant had superior functional properties and stability compared with spray-dried sample. Both products might be used as functional protein ingredients in various food systems. Copyright © 2010 Society of Chemical Industry [source] | ||||||||||