Formulation factors affecting foam properties during vacuum foam-drying
Tristan Osanlóo, Daniel LU
; Mahlin, Denny
; Bjerregaard, Simon
; Bergenståhl, Björn
LU
and Millqvist-Fureby, Anna
LU
(2024)
In International Journal of Pharmaceutics
652.
- Abstract
This paper explores how vacuum foam-drying of a protein is influenced by formulation parameters by investigating the foam structure, physical properties of the foam, and the stability of the protein. Recombinant human bile salt-stimulated lipase was used as a model of a protein drug. The stability of the lipase was evaluated through activity measurements. Two disaccharides (sucrose and trehalose), strongly tending to an amorphous form, were used as matrix formers, and the physical properties were assessed through residual water content, glass transition temperature, and crystalline state. Moreover, some formulations included surfactants with different sizes and structures of the head group. The alkyl chain length was kept constant to... (More)
This paper explores how vacuum foam-drying of a protein is influenced by formulation parameters by investigating the foam structure, physical properties of the foam, and the stability of the protein. Recombinant human bile salt-stimulated lipase was used as a model of a protein drug. The stability of the lipase was evaluated through activity measurements. Two disaccharides (sucrose and trehalose), strongly tending to an amorphous form, were used as matrix formers, and the physical properties were assessed through residual water content, glass transition temperature, and crystalline state. Moreover, some formulations included surfactants with different sizes and structures of the head group. The alkyl chain length was kept constant to only investigate the impact of the surfactant head group, in the presence of the lipase, on the foamability and surface coverage of the lipase. The study demonstrated that the lipase allowed for a dry, solid foam with a foam overrun of up to 2600 %. The wall thickness of the dry, solid foam was estimated to be 20–50 µm. Clear differences between sucrose and trehalose as matrix former were identified. The lipase showed no tendency to lose activity because of the drying and rehydration, despite a proportion of the lipase covering the surfaces of the dry material.
(Less)
- author
- Tristan Osanlóo, Daniel
LU
; Mahlin, Denny
; Bjerregaard, Simon
; Bergenståhl, Björn
LU
and Millqvist-Fureby, Anna
LU
- organization
- publishing date
- 2024-03-05
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Lipase, Matrix former, Protein formulations, Solid-state properties, Surface composition, Vacuum foam-drying
- in
- International Journal of Pharmaceutics
- volume
- 652
- article number
- 123803
- publisher
- Elsevier
- external identifiers
-
- pmid:38218506
- scopus:85184501646
- ISSN
- 0378-5173
- DOI
- 10.1016/j.ijpharm.2024.123803
- language
- English
- LU publication?
- yes
- id
- 7cf94ba6-f026-4a76-846e-087e9de581d1
- date added to LUP
- 2024-02-22 13:57:34
- date last changed
- 2024-04-21 23:56:12
@article{7cf94ba6-f026-4a76-846e-087e9de581d1,
abstract = {{<p>This paper explores how vacuum foam-drying of a protein is influenced by formulation parameters by investigating the foam structure, physical properties of the foam, and the stability of the protein. Recombinant human bile salt-stimulated lipase was used as a model of a protein drug. The stability of the lipase was evaluated through activity measurements. Two disaccharides (sucrose and trehalose), strongly tending to an amorphous form, were used as matrix formers, and the physical properties were assessed through residual water content, glass transition temperature, and crystalline state. Moreover, some formulations included surfactants with different sizes and structures of the head group. The alkyl chain length was kept constant to only investigate the impact of the surfactant head group, in the presence of the lipase, on the foamability and surface coverage of the lipase. The study demonstrated that the lipase allowed for a dry, solid foam with a foam overrun of up to 2600 %. The wall thickness of the dry, solid foam was estimated to be 20–50 µm. Clear differences between sucrose and trehalose as matrix former were identified. The lipase showed no tendency to lose activity because of the drying and rehydration, despite a proportion of the lipase covering the surfaces of the dry material.</p>}},
author = {{Tristan Osanlóo, Daniel and Mahlin, Denny and Bjerregaard, Simon and Bergenståhl, Björn and Millqvist-Fureby, Anna}},
issn = {{0378-5173}},
keywords = {{Lipase; Matrix former; Protein formulations; Solid-state properties; Surface composition; Vacuum foam-drying}},
language = {{eng}},
month = {{03}},
publisher = {{Elsevier}},
series = {{International Journal of Pharmaceutics}},
title = {{Formulation factors affecting foam properties during vacuum foam-drying}},
url = {{http://dx.doi.org/10.1016/j.ijpharm.2024.123803}},
doi = {{10.1016/j.ijpharm.2024.123803}},
volume = {{652}},
year = {{2024}},
}