A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements
Circular dichroism measurements, using synchrotron radiation, showed that the secondary structure of Candida antarctica lipase does not differ significantly when changed from an aqueous to organic solvent environment. Thus, we may conclude that a major conformational change is not the reason for the...
Published in: | Enzyme and Microbial Technology |
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2005
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Online Access: | http://wrap.warwick.ac.uk/7492/ https://doi.org/10.1016/j.enzmictec.2004.04.020 |
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ftuwarwick:oai:wrap.warwick.ac.uk:7492 2023-05-15T13:42:46+02:00 A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements 2005-01-06 http://wrap.warwick.ac.uk/7492/ https://doi.org/10.1016/j.enzmictec.2004.04.020 unknown ELSEVIER SCIENCE INC UNSPECIFIED (2005) A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements. ENZYME AND MICROBIAL TECHNOLOGY, 36 (1). pp. 70-74. doi:10.1016/j.enzmictec.2004.04.020 <http://dx.doi.org/10.1016/j.enzmictec.2004.04.020 > TP Chemical technology Journal Article NonPeerReviewed 2005 ftuwarwick https://doi.org/10.1016/j.enzmictec.2004.04.020 2022-03-16T20:05:09Z Circular dichroism measurements, using synchrotron radiation, showed that the secondary structure of Candida antarctica lipase does not differ significantly when changed from an aqueous to organic solvent environment. Thus, we may conclude that a major conformational change is not the reason for the different product produced by the enzyme when used in organic solvent. Significant changes in the lipase's alpha-helix content were found at the extremes of pH 4.2 and 9.0; this is in keeping with the permanent loss of activity of the enzyme at such a pH. (C) 2004 Elsevier Inc. All rights reserved. Article in Journal/Newspaper Antarc* Antarctica The University of Warwick: WRAP - Warwick Research Archive Portal Enzyme and Microbial Technology 36 1 70 74 |
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The University of Warwick: WRAP - Warwick Research Archive Portal |
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ftuwarwick |
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unknown |
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TP Chemical technology |
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TP Chemical technology A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements |
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TP Chemical technology |
description |
Circular dichroism measurements, using synchrotron radiation, showed that the secondary structure of Candida antarctica lipase does not differ significantly when changed from an aqueous to organic solvent environment. Thus, we may conclude that a major conformational change is not the reason for the different product produced by the enzyme when used in organic solvent. Significant changes in the lipase's alpha-helix content were found at the extremes of pH 4.2 and 9.0; this is in keeping with the permanent loss of activity of the enzyme at such a pH. (C) 2004 Elsevier Inc. All rights reserved. |
format |
Article in Journal/Newspaper |
title |
A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements |
title_short |
A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements |
title_full |
A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements |
title_fullStr |
A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements |
title_full_unstemmed |
A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements |
title_sort |
study of the secondary structure of candida antarctica lipase b using synchrotron radiation circular dichroism measurements |
publisher |
ELSEVIER SCIENCE INC |
publishDate |
2005 |
url |
http://wrap.warwick.ac.uk/7492/ https://doi.org/10.1016/j.enzmictec.2004.04.020 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
UNSPECIFIED (2005) A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements. ENZYME AND MICROBIAL TECHNOLOGY, 36 (1). pp. 70-74. doi:10.1016/j.enzmictec.2004.04.020 <http://dx.doi.org/10.1016/j.enzmictec.2004.04.020 > |
op_doi |
https://doi.org/10.1016/j.enzmictec.2004.04.020 |
container_title |
Enzyme and Microbial Technology |
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36 |
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1 |
container_start_page |
70 |
op_container_end_page |
74 |
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1766172669707812864 |