Encapsulation of Aspartic Protease in Nonlamellar Lipid Liquid Crystalline Phases
(2019) In Biophysical Journal 117(5). p.829-843- Abstract
Encapsulation of proteins within lipid inverse bicontinuous cubic phases (Q2) has been widely studied for many applications, such as protein crystallization or drug delivery of proteins for food and pharmaceutical purposes. However, the use of the lipid sponge (L3) phase for encapsulation of proteins has not yet been well explored. Here, we have employed a lipid system that forms highly swollen sponge phases to entrap aspartic protease (34 kDa), an enzyme used for food processing, e.g., to control the cheese-ripening process. Small-angle x-ray scattering showed that although the L3 phase was maintained at low enzyme concentrations (≤15 mg/mL), higher concentration induces a transition to more curved... (More)
Encapsulation of proteins within lipid inverse bicontinuous cubic phases (Q2) has been widely studied for many applications, such as protein crystallization or drug delivery of proteins for food and pharmaceutical purposes. However, the use of the lipid sponge (L3) phase for encapsulation of proteins has not yet been well explored. Here, we have employed a lipid system that forms highly swollen sponge phases to entrap aspartic protease (34 kDa), an enzyme used for food processing, e.g., to control the cheese-ripening process. Small-angle x-ray scattering showed that although the L3 phase was maintained at low enzyme concentrations (≤15 mg/mL), higher concentration induces a transition to more curved structures, i.e., transition from L3 to inverse bicontinuous cubic (Q2) phase. The Raman spectroscopy data showed minor conformational changes assigned to the lipid molecules that confirm the lipid-protein interactions. However, the peaks assigned to the protein showed that the structure was not significantly affected. This was consistent with the higher activity presented by the encapsulated aspartic protease compared to the free enzyme stored at the same temperature. Finally, the encapsulation efficiency of aspartic protease in lipid sponge-like nanoparticles was 81% as examined by size-exclusion chromatography. Based on these results, we discuss the large potential of lipid sponge phases as carriers for proteins.
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- author
- Valldeperas, Maria LU ; Talaikis, Martynas ; Dhayal, Surender K. ; Velička, Martynas ; Barauskas, Justas LU ; Niaura, Gediminas and Nylander, Tommy LU
- organization
- publishing date
- 2019-07-26
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Journal
- volume
- 117
- issue
- 5
- pages
- 829 - 843
- publisher
- Cell Press
- external identifiers
-
- pmid:31422820
- scopus:85070551024
- ISSN
- 0006-3495
- DOI
- 10.1016/j.bpj.2019.07.031
- language
- English
- LU publication?
- yes
- id
- 10bf6467-cadd-4ad1-b5ad-2a16efa82044
- date added to LUP
- 2019-08-26 12:40:32
- date last changed
- 2024-06-11 23:08:55
@article{10bf6467-cadd-4ad1-b5ad-2a16efa82044,
abstract = {{<p>Encapsulation of proteins within lipid inverse bicontinuous cubic phases (Q<sub>2</sub>) has been widely studied for many applications, such as protein crystallization or drug delivery of proteins for food and pharmaceutical purposes. However, the use of the lipid sponge (L<sub>3</sub>) phase for encapsulation of proteins has not yet been well explored. Here, we have employed a lipid system that forms highly swollen sponge phases to entrap aspartic protease (34 kDa), an enzyme used for food processing, e.g., to control the cheese-ripening process. Small-angle x-ray scattering showed that although the L<sub>3</sub> phase was maintained at low enzyme concentrations (≤15 mg/mL), higher concentration induces a transition to more curved structures, i.e., transition from L<sub>3</sub> to inverse bicontinuous cubic (Q<sub>2</sub>) phase. The Raman spectroscopy data showed minor conformational changes assigned to the lipid molecules that confirm the lipid-protein interactions. However, the peaks assigned to the protein showed that the structure was not significantly affected. This was consistent with the higher activity presented by the encapsulated aspartic protease compared to the free enzyme stored at the same temperature. Finally, the encapsulation efficiency of aspartic protease in lipid sponge-like nanoparticles was 81% as examined by size-exclusion chromatography. Based on these results, we discuss the large potential of lipid sponge phases as carriers for proteins.</p>}},
author = {{Valldeperas, Maria and Talaikis, Martynas and Dhayal, Surender K. and Velička, Martynas and Barauskas, Justas and Niaura, Gediminas and Nylander, Tommy}},
issn = {{0006-3495}},
language = {{eng}},
month = {{07}},
number = {{5}},
pages = {{829--843}},
publisher = {{Cell Press}},
series = {{Biophysical Journal}},
title = {{Encapsulation of Aspartic Protease in Nonlamellar Lipid Liquid Crystalline Phases}},
url = {{http://dx.doi.org/10.1016/j.bpj.2019.07.031}},
doi = {{10.1016/j.bpj.2019.07.031}},
volume = {{117}},
year = {{2019}},
}