JOURNAL ARTICLE

Site‐Specific Immobilization of Genetically Engineered Variants of Candida antarctica Lipase B

Abstract

Keep still! A general strategy has been developed for the site-specific and covalent immobilization of biomolecules. The applicability of this protocol was demonstrated by using the industrially important lipase CalB. Two mutants that possess a free cysteine (Cys293 or C-terminal) were prepared and immobilized in an active conformation at the desired position. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2268/2006/z600198_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.

Keywords:
Candida antarctica Lipase Chemistry Computational biology Cysteine Covalent bond Directed evolution Mutant Biochemistry Biology Enzyme Gene Organic chemistry

Metrics

38
Cited By
2.29
FWCI (Field Weighted Citation Impact)
21
Refs
0.85
Citation Normalized Percentile
Is in top 1%
Is in top 10%

Citation History

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