Spray-drying of trypsin - Surface characterisation and activity preservation
Millqvist-Fureby, Anna LU ; Malmsten, Martin LU and Bergenståhl, Björn LU
(1999)
In International Journal of Pharmaceutics
188(2).
p.243-253
- Abstract
In the present study trypsin mixed with various carbohydrates, i.e. lactose, sucrose, mannitol, α-cyclodextrin and dextrin, was spray-dried in order to investigate the effects of spray-drying on this enzyme, with particular emphasis on the effects of interactions between trypsin and the surface formed during spray-drying. The protein was strongly over-represented at the surface of the powder particles, the surface coverage ranging from 10 to 65%, depending on the amount of trypsin in the solids (0.2-5%). This indicates that the protein adsorbs at the air/liquid interface of the spray- droplets, and that this surface is also largely preserved after drying. The surface concentration of protein in the spray-dried powders could be... (More)
In the present study trypsin mixed with various carbohydrates, i.e. lactose, sucrose, mannitol, α-cyclodextrin and dextrin, was spray-dried in order to investigate the effects of spray-drying on this enzyme, with particular emphasis on the effects of interactions between trypsin and the surface formed during spray-drying. The protein was strongly over-represented at the surface of the powder particles, the surface coverage ranging from 10 to 65%, depending on the amount of trypsin in the solids (0.2-5%). This indicates that the protein adsorbs at the air/liquid interface of the spray- droplets, and that this surface is also largely preserved after drying. The surface concentration of protein in the spray-dried powders could be controlled by adding a surfactant to the mixture before drying, since the surfactant adsorbs preferentially at the air/liquid interface of the spray droplets, thus expelling protein from the surface. In general, the residual activity of trypsin in these non-optimised formulations was 90% or higher, and in no case less than 82%. It was found that the loss of activity could partly be explained by inactivation of the protein adsorbed at the surface. For mannitol and sucrose, however, the level of inactivation was higher than could be explained by surface inactivation alone, and additional mechanisms must also be considered.
(Less)
- author
- Millqvist-Fureby, Anna
LU
; Malmsten, Martin
LU
and Bergenståhl, Björn
LU
- publishing date
- 1999-10-25
- type
- Contribution to journal
- publication status
- published
- keywords
- Activity preservation, Electron spectroscopy for chemical analysis (ESCA), Spray-drying, Surface analysis, Trypsin
- in
- International Journal of Pharmaceutics
- volume
- 188
- issue
- 2
- pages
- 11 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0032851375
- pmid:10518679
- ISSN
- 0378-5173
- DOI
- 10.1016/S0378-5173(99)00226-4
- language
- English
- LU publication?
- no
- id
- c172c885-d432-4daf-9892-bb9103028a64
- date added to LUP
- 2025-04-14 17:31:25
- date last changed
- 2025-06-23 23:05:19
@article{c172c885-d432-4daf-9892-bb9103028a64,
abstract = {{<p>In the present study trypsin mixed with various carbohydrates, i.e. lactose, sucrose, mannitol, α-cyclodextrin and dextrin, was spray-dried in order to investigate the effects of spray-drying on this enzyme, with particular emphasis on the effects of interactions between trypsin and the surface formed during spray-drying. The protein was strongly over-represented at the surface of the powder particles, the surface coverage ranging from 10 to 65%, depending on the amount of trypsin in the solids (0.2-5%). This indicates that the protein adsorbs at the air/liquid interface of the spray- droplets, and that this surface is also largely preserved after drying. The surface concentration of protein in the spray-dried powders could be controlled by adding a surfactant to the mixture before drying, since the surfactant adsorbs preferentially at the air/liquid interface of the spray droplets, thus expelling protein from the surface. In general, the residual activity of trypsin in these non-optimised formulations was 90% or higher, and in no case less than 82%. It was found that the loss of activity could partly be explained by inactivation of the protein adsorbed at the surface. For mannitol and sucrose, however, the level of inactivation was higher than could be explained by surface inactivation alone, and additional mechanisms must also be considered.</p>}},
author = {{Millqvist-Fureby, Anna and Malmsten, Martin and Bergenståhl, Björn}},
issn = {{0378-5173}},
keywords = {{Activity preservation; Electron spectroscopy for chemical analysis (ESCA); Spray-drying; Surface analysis; Trypsin}},
language = {{eng}},
month = {{10}},
number = {{2}},
pages = {{243--253}},
publisher = {{Elsevier}},
series = {{International Journal of Pharmaceutics}},
title = {{Spray-drying of trypsin - Surface characterisation and activity preservation}},
url = {{http://dx.doi.org/10.1016/S0378-5173(99)00226-4}},
doi = {{10.1016/S0378-5173(99)00226-4}},
volume = {{188}},
year = {{1999}},
}