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Immobilisation of β-galactosidase within a lipid sponge phase: structure, stability and kinetics characterisation

Gilbert, Jennifer LU orcid ; Valldeperas Badell, Maria LU ; Dhayal, Surender K. ; Barauskas, Justas LU ; Dicko, Cedric LU orcid and Nylander, Tommy LU (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)
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author
; ; ; ; and
organization
publishing date
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
2025-10-14 10:46:04
@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}},
}