Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering
Candida antarctica Lipase B (CALB) formed a seemingly homogeneous solution in water, 1-ethyl-3-methylimidazolium dicyanamide ([C2mim][N(CN) 2]) or dimethyl sulfoxide (DMSO). However, dynamic light scattering (DLS) and small angle neutron scattering (SANS) demonstrated that the enzyme formed aggregat...
Published in: | Green Chemistry |
---|---|
Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2007
|
Subjects: | |
Online Access: | https://research.manchester.ac.uk/en/publications/05c04e56-3cc5-40e9-9ad4-489933e7a356 https://doi.org/10.1039/b700437k |
id |
ftumanchesterpub:oai:pure.atira.dk:publications/05c04e56-3cc5-40e9-9ad4-489933e7a356 |
---|---|
record_format |
openpolar |
spelling |
ftumanchesterpub:oai:pure.atira.dk:publications/05c04e56-3cc5-40e9-9ad4-489933e7a356 2024-06-23T07:47:08+00:00 Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering Sate, Daniel Janssen, Michiel H A Stephens, Gill Sheldon, Roger A. Seddon, Kenneth R. Lu, Jian R. 2007 https://research.manchester.ac.uk/en/publications/05c04e56-3cc5-40e9-9ad4-489933e7a356 https://doi.org/10.1039/b700437k eng eng https://research.manchester.ac.uk/en/publications/05c04e56-3cc5-40e9-9ad4-489933e7a356 info:eu-repo/semantics/closedAccess Sate , D , Janssen , M H A , Stephens , G , Sheldon , R A , Seddon , K R & Lu , J R 2007 , ' Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering ' , Green Chemistry , vol. 9 , no. 8 , pp. 859-867 . https://doi.org/10.1039/b700437k article 2007 ftumanchesterpub https://doi.org/10.1039/b700437k 2024-06-04T00:17:32Z Candida antarctica Lipase B (CALB) formed a seemingly homogeneous solution in water, 1-ethyl-3-methylimidazolium dicyanamide ([C2mim][N(CN) 2]) or dimethyl sulfoxide (DMSO). However, dynamic light scattering (DLS) and small angle neutron scattering (SANS) demonstrated that the enzyme formed aggregates in the non-aqueous solvents. In aqueous solution, SANS measurements revealed that CALB formed cylindrical nano-structures with a diameter of 5 nm and a length of 4 nm, equivalent to the dimensions of a single CALB molecule. The enzyme also formed cylindrical structures in DMSO but the diameter was 4 nm and the length was 12 nm, indicating that the enzyme had aggregated to form dimers or trimers. In [C2mim][N(CN)2], disc-shaped aggregates were formed, with an average diameter of 49 nm and a length of 3.8 nm, equivalent to the volume of 150 CALB molecules. In all cases, the hydrodynamic diameters measured by DLS matched the long axial lengths of the aggregates determined by SANS, indicating a good consistency between the two techniques. DLS measurements showed that CALB aggregates in [C 2mim][EtOSO3] and [C2mim][NO3] had a smaller diameter than in [C2mim][N(CN)2]. In all cases, the aggregation observed in the solvents was associated with loss of enzymatic activity. This journal is © The Royal Society of Chemistry. Article in Journal/Newspaper Antarc* Antarctica The University of Manchester: Research Explorer Green Chemistry 9 8 859 |
institution |
Open Polar |
collection |
The University of Manchester: Research Explorer |
op_collection_id |
ftumanchesterpub |
language |
English |
description |
Candida antarctica Lipase B (CALB) formed a seemingly homogeneous solution in water, 1-ethyl-3-methylimidazolium dicyanamide ([C2mim][N(CN) 2]) or dimethyl sulfoxide (DMSO). However, dynamic light scattering (DLS) and small angle neutron scattering (SANS) demonstrated that the enzyme formed aggregates in the non-aqueous solvents. In aqueous solution, SANS measurements revealed that CALB formed cylindrical nano-structures with a diameter of 5 nm and a length of 4 nm, equivalent to the dimensions of a single CALB molecule. The enzyme also formed cylindrical structures in DMSO but the diameter was 4 nm and the length was 12 nm, indicating that the enzyme had aggregated to form dimers or trimers. In [C2mim][N(CN)2], disc-shaped aggregates were formed, with an average diameter of 49 nm and a length of 3.8 nm, equivalent to the volume of 150 CALB molecules. In all cases, the hydrodynamic diameters measured by DLS matched the long axial lengths of the aggregates determined by SANS, indicating a good consistency between the two techniques. DLS measurements showed that CALB aggregates in [C 2mim][EtOSO3] and [C2mim][NO3] had a smaller diameter than in [C2mim][N(CN)2]. In all cases, the aggregation observed in the solvents was associated with loss of enzymatic activity. This journal is © The Royal Society of Chemistry. |
format |
Article in Journal/Newspaper |
author |
Sate, Daniel Janssen, Michiel H A Stephens, Gill Sheldon, Roger A. Seddon, Kenneth R. Lu, Jian R. |
spellingShingle |
Sate, Daniel Janssen, Michiel H A Stephens, Gill Sheldon, Roger A. Seddon, Kenneth R. Lu, Jian R. Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering |
author_facet |
Sate, Daniel Janssen, Michiel H A Stephens, Gill Sheldon, Roger A. Seddon, Kenneth R. Lu, Jian R. |
author_sort |
Sate, Daniel |
title |
Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering |
title_short |
Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering |
title_full |
Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering |
title_fullStr |
Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering |
title_full_unstemmed |
Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering |
title_sort |
enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering |
publishDate |
2007 |
url |
https://research.manchester.ac.uk/en/publications/05c04e56-3cc5-40e9-9ad4-489933e7a356 https://doi.org/10.1039/b700437k |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Sate , D , Janssen , M H A , Stephens , G , Sheldon , R A , Seddon , K R & Lu , J R 2007 , ' Enzyme aggregation in ionic liquids studied by dynamic light scattering and small angle neutron scattering ' , Green Chemistry , vol. 9 , no. 8 , pp. 859-867 . https://doi.org/10.1039/b700437k |
op_relation |
https://research.manchester.ac.uk/en/publications/05c04e56-3cc5-40e9-9ad4-489933e7a356 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1039/b700437k |
container_title |
Green Chemistry |
container_volume |
9 |
container_issue |
8 |
container_start_page |
859 |
_version_ |
1802651234223521792 |