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...

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Bibliographic Details
Published in:Enzyme and Microbial Technology
Format: Article in Journal/Newspaper
Language:unknown
Published: ELSEVIER SCIENCE INC 2005
Subjects:
TP Chemical technology
Antarc*
Antarctica
Online Access:http://wrap.warwick.ac.uk/7492/
https://doi.org/10.1016/j.enzmictec.2004.04.020
id ftuwarwick:oai:wrap.warwick.ac.uk:7492
record_format openpolar
spelling 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
institution Open Polar
collection The University of Warwick: WRAP - Warwick Research Archive Portal
op_collection_id ftuwarwick
language unknown
topic TP Chemical technology
spellingShingle TP Chemical technology
A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements
topic_facet 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
container_volume 36
container_issue 1
container_start_page 70
op_container_end_page 74
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