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

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Gilbert, JenniferLund University,Lunds universitet,NanoLund: Centre for Nanoscience,Annan verksamhet, LTH,Lunds Tekniska Högskola,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Other operations, LTH,Faculty of Engineering, LTH,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,University of Southampton (författare)

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

Artikel/kapitelEngelska2019

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2019
11 s.

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LIBRIS-ID:oai:lup.lub.lu.se:024eb5c8-2eef-4e31-bfcc-866b870bafc6
https://lup.lub.lu.se/record/024eb5c8-2eef-4e31-bfcc-866b870bafc6URI
https://doi.org/10.1039/C9NR06675FDOI

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Språk:engelska
Sammanfattning på:engelska

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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.

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NATURVETENSKAP Kemi Fysikalisk kemi hsv//swe
NATURAL SCIENCES Chemical Sciences Physical Chemistry hsv//eng

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Valldeperas Badell, MariaLund University,Lunds universitet,NanoLund: Centre for Nanoscience,Annan verksamhet, LTH,Lunds Tekniska Högskola,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Other operations, LTH,Faculty of Engineering, LTH,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,University of Southampton(Swepub:lu)fkem-mrv (författare)
Dhayal, Surender K.Chr. Hansen Holding A/S (författare)
Barauskas, JustasCamurus AB(Swepub:lu)fkem-jba (författare)
Dicko, CedricLund University,Lunds universitet,Tillämpad biokemi,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Pure and Applied Biochemistry,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)tbio-cdc (författare)
Nylander, TommyLund University,Lunds universitet,NanoLund: Centre for Nanoscience,Annan verksamhet, LTH,Lunds Tekniska Högskola,Fysikalisk kemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,LINXS - Institute of advanced Neutron and X-ray Science,Other operations, LTH,Faculty of Engineering, LTH,Physical Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Faculty of Engineering, LTH(Swepub:lu)fk1-tny (författare)
NanoLund: Centre for NanoscienceAnnan verksamhet, LTH (creator_code:org_t)

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Ingår i:Nanoscale11:44, s. 21291-213012040-3372

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Av författaren/redakt...: Gilbert, Jennife ...; Valldeperas Bade ...; Dhayal, Surender ...; Barauskas, Justa ...; Dicko, Cedric; Nylander, Tommy

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NATURVETENSKAP: NATURVETENSKAP; och Kemi; och Fysikalisk kemi

Artiklar i publikationen: Nanoscale

Av lärosätet: Lunds universitet

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