A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements

R. W. McCabe; A. Rodger; A. Taylor

doi:10.1016/j.enzmictec.2004.04.020

A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements

R. W. McCabe, A. Rodger, A. Taylor

Research output: Contribution to journal › Article › peer-review

30 Citations (Scopus)

Abstract

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 α-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.

Original language	English
Pages (from-to)	70-74
Number of pages	5
Journal	Enzyme and Microbial Technology
Volume	36
Issue number	1
DOIs	https://doi.org/10.1016/j.enzmictec.2004.04.020
Publication status	Published - 6 Jan 2005
Externally published	Yes

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10.1016/j.enzmictec.2004.04.020

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abstract = "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 α-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.",

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AU - McCabe, R. W.

AU - Rodger, A.

AU - Taylor, A.

PY - 2005/1/6

Y1 - 2005/1/6

N2 - 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 α-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.

AB - 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 α-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.

KW - Candida antarctica lipase B

KW - Circular dichroism

KW - Secondary structure

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DO - 10.1016/j.enzmictec.2004.04.020

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JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

IS - 1

ER -

A study of the secondary structure of Candida antarctica lipase B using synchrotron radiation circular dichroism measurements

Abstract

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