Immobilisation of β-galactosidase within a lipid sponge phase: structure, stability and kinetics characterisation
(2019) In Nanoscale 11(44). p.21291-21301- Abstract
- In the formulation of an active enzyme enclosed in a matrix for controlled delivery, it is a challenge to achieve a high protein load and to ensure high activity of the protein. For the first time to our knowledge, we report the use of a highly swollen lipid sponge (L3) phase for encapsulation of the large active enzyme, β-galactosidase (β-gal, 238 kDa). This enzyme has large relevance for applications in, e.g. the production of lactose free milk products. The formulation consisted of diglycerol monooleate (DGMO), and a mixture of mono-, di- and triglycerides (Capmul GMO-50) stabilised by polysorbate 80 (P80). The advantage of this type of matrix is that it can be produced on a large scale with a fairly simple and mild process as the... (More)
- In the formulation of an active enzyme enclosed in a matrix for controlled delivery, it is a challenge to achieve a high protein load and to ensure high activity of the protein. For the first time to our knowledge, we report the use of a highly swollen lipid sponge (L3) phase for encapsulation of the large active enzyme, β-galactosidase (β-gal, 238 kDa). This enzyme has large relevance for applications in, e.g. the production of lactose free milk products. The formulation consisted of diglycerol monooleate (DGMO), and a mixture of mono-, di- and triglycerides (Capmul GMO-50) stabilised by polysorbate 80 (P80). The advantage of this type of matrix is that it can be produced on a large scale with a fairly simple and mild process as the system is in practice self-dispersing, yet it has a well-defined internal nano-structure. Minor effects on the sponge phase structure due to the inclusion of the enzyme were observed using small angle X-ray scattering (SAXS). The effect of encapsulation on the enzymatic activity and kinetic characteristics of β-galactosidase activity was also investigated and can be related to the enzyme stability and confinement within the lipid matrix. The encapsulated β-galactosidase maintained its activity for a significantly longer time when compared to the free solution at the same temperature. Differences in the particle size and charge of sponge-like nanoparticles (L3-NPs) with and without the enzyme were analysed by dynamic light scattering (DLS) and zeta-potential measurements. Moreover, all the initial β-galactosidase was encapsulated within L3-NPs as revealed by size exclusion chromatography. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/024eb5c8-2eef-4e31-bfcc-866b870bafc6
- author
- Gilbert, Jennifer LU ; Valldeperas Badell, Maria LU ; Dhayal, Surender K. ; Barauskas, Justas LU ; Dicko, Cedric LU and Nylander, Tommy LU
- organization
- publishing date
- 2019-10-08
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nanoscale
- volume
- 11
- issue
- 44
- pages
- 11 pages
- publisher
- Royal Society of Chemistry
- external identifiers
-
- scopus:85074731946
- ISSN
- 2040-3372
- DOI
- 10.1039/C9NR06675F
- language
- English
- LU publication?
- yes
- id
- 024eb5c8-2eef-4e31-bfcc-866b870bafc6
- date added to LUP
- 2020-02-04 15:56:09
- date last changed
- 2023-11-20 00:10:02
@article{024eb5c8-2eef-4e31-bfcc-866b870bafc6, abstract = {{In the formulation of an active enzyme enclosed in a matrix for controlled delivery, it is a challenge to achieve a high protein load and to ensure high activity of the protein. For the first time to our knowledge, we report the use of a highly swollen lipid sponge (L3) phase for encapsulation of the large active enzyme, β-galactosidase (β-gal, 238 kDa). This enzyme has large relevance for applications in, e.g. the production of lactose free milk products. The formulation consisted of diglycerol monooleate (DGMO), and a mixture of mono-, di- and triglycerides (Capmul GMO-50) stabilised by polysorbate 80 (P80). The advantage of this type of matrix is that it can be produced on a large scale with a fairly simple and mild process as the system is in practice self-dispersing, yet it has a well-defined internal nano-structure. Minor effects on the sponge phase structure due to the inclusion of the enzyme were observed using small angle X-ray scattering (SAXS). The effect of encapsulation on the enzymatic activity and kinetic characteristics of β-galactosidase activity was also investigated and can be related to the enzyme stability and confinement within the lipid matrix. The encapsulated β-galactosidase maintained its activity for a significantly longer time when compared to the free solution at the same temperature. Differences in the particle size and charge of sponge-like nanoparticles (L3-NPs) with and without the enzyme were analysed by dynamic light scattering (DLS) and zeta-potential measurements. Moreover, all the initial β-galactosidase was encapsulated within L3-NPs as revealed by size exclusion chromatography.}}, author = {{Gilbert, Jennifer and Valldeperas Badell, Maria and Dhayal, Surender K. and Barauskas, Justas and Dicko, Cedric and Nylander, Tommy}}, issn = {{2040-3372}}, language = {{eng}}, month = {{10}}, number = {{44}}, pages = {{21291--21301}}, publisher = {{Royal Society of Chemistry}}, series = {{Nanoscale}}, title = {{Immobilisation of β-galactosidase within a lipid sponge phase: structure, stability and kinetics characterisation}}, url = {{http://dx.doi.org/10.1039/C9NR06675F}}, doi = {{10.1039/C9NR06675F}}, volume = {{11}}, year = {{2019}}, }