Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study

Abstract. The application of small angle neutron scattering (SANS) to the characterisation of sol–gel hosts containing biomolecules offers the opportunity to explore the relationship between gel structure and catalyst. A model system involving the immobilisation of Candida antarctica lipase B (CALB)...

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Main Authors: L. E. Rodgers, L. J. R. Foster
Other Authors: The Pennsylvania State University CiteSeerX Archives
Format: Text
Language:English
Subjects:
Online Access:http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.651.9133
http://www.ncnr.nist.gov/programs/sans/pdf/publications/0507.pdf
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spelling ftciteseerx:oai:CiteSeerX.psu:10.1.1.651.9133 2023-05-15T14:02:50+02:00 Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study L. E. Rodgers L. J. R. Foster The Pennsylvania State University CiteSeerX Archives application/pdf http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.651.9133 http://www.ncnr.nist.gov/programs/sans/pdf/publications/0507.pdf en eng http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.651.9133 http://www.ncnr.nist.gov/programs/sans/pdf/publications/0507.pdf Metadata may be used without restrictions as long as the oai identifier remains attached to it. http://www.ncnr.nist.gov/programs/sans/pdf/publications/0507.pdf Candida antarctica lipase SANS text ftciteseerx 2016-01-08T16:26:07Z Abstract. The application of small angle neutron scattering (SANS) to the characterisation of sol–gel hosts containing biomolecules offers the opportunity to explore the relationship between gel structure and catalyst. A model system involving the immobilisation of Candida antarctica lipase B (CALB) was investigated. Gels were produced by fluoride-catalysed hydrolysis of fixed ratios of tetramethylorthosilicate (TMOS) and methyltrimethoxysilane (MTMS). Phase separation between the enzyme and the evolving sol–gel matrix was minimised by incorporating glycerol into the sol–gel precursor solution. The potential stabilising effect of the NaF catalyst upon the enzyme was also investigated. Scattering studies were conducted on both immobilised lipase, and lipase in free solution. Scattering studies on free enzyme provided evidence of multiple populations of enzyme aggregates and showed that choice of solvent affected the degree of aggregation. Both NaF and glycerol affected neutron scattering, indicating changes in lipase conformation. Increasing glycerol concentration increased the degree of aggregation and produced differences in solvent packing on the surface of protein molecules. Initial evidence from SANS data indicated that the presence of the enzyme during gel formation conferred structural changes on the gel matrix. Modelling the effect of sol–gel encapsulation on lipase requires comparison of data from free enzyme to the immobilised form. Removal of the enzyme from the sol–gel structure, post gelation, is necessary to better characterise the modified matrix. This methodological problem will be the subject of future investigations. Text Antarc* Antarctica Unknown
institution Open Polar
collection Unknown
op_collection_id ftciteseerx
language English
topic Candida antarctica
lipase
SANS
spellingShingle Candida antarctica
lipase
SANS
L. E. Rodgers
L. J. R. Foster
Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study
topic_facet Candida antarctica
lipase
SANS
description Abstract. The application of small angle neutron scattering (SANS) to the characterisation of sol–gel hosts containing biomolecules offers the opportunity to explore the relationship between gel structure and catalyst. A model system involving the immobilisation of Candida antarctica lipase B (CALB) was investigated. Gels were produced by fluoride-catalysed hydrolysis of fixed ratios of tetramethylorthosilicate (TMOS) and methyltrimethoxysilane (MTMS). Phase separation between the enzyme and the evolving sol–gel matrix was minimised by incorporating glycerol into the sol–gel precursor solution. The potential stabilising effect of the NaF catalyst upon the enzyme was also investigated. Scattering studies were conducted on both immobilised lipase, and lipase in free solution. Scattering studies on free enzyme provided evidence of multiple populations of enzyme aggregates and showed that choice of solvent affected the degree of aggregation. Both NaF and glycerol affected neutron scattering, indicating changes in lipase conformation. Increasing glycerol concentration increased the degree of aggregation and produced differences in solvent packing on the surface of protein molecules. Initial evidence from SANS data indicated that the presence of the enzyme during gel formation conferred structural changes on the gel matrix. Modelling the effect of sol–gel encapsulation on lipase requires comparison of data from free enzyme to the immobilised form. Removal of the enzyme from the sol–gel structure, post gelation, is necessary to better characterise the modified matrix. This methodological problem will be the subject of future investigations.
author2 The Pennsylvania State University CiteSeerX Archives
format Text
author L. E. Rodgers
L. J. R. Foster
author_facet L. E. Rodgers
L. J. R. Foster
author_sort L. E. Rodgers
title Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study
title_short Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study
title_full Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study
title_fullStr Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study
title_full_unstemmed Effect of Sol–Gel Encapsulation on Lipase Structure and Function: A Small Angle Neutron Scattering Study
title_sort effect of sol–gel encapsulation on lipase structure and function: a small angle neutron scattering study
url http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.651.9133
http://www.ncnr.nist.gov/programs/sans/pdf/publications/0507.pdf
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source http://www.ncnr.nist.gov/programs/sans/pdf/publications/0507.pdf
op_relation http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.651.9133
http://www.ncnr.nist.gov/programs/sans/pdf/publications/0507.pdf
op_rights Metadata may be used without restrictions as long as the oai identifier remains attached to it.
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