158
Views
11
CrossRef citations to date
0
Altmetric
ORIGINAL ARTICLE

Reaction design for evaluation of the substrate range of hydrolases

, &
Pages 228-234 | Published online: 11 Jul 2009
 

Abstract

Biocatalytic acylation reactions involving 24 alcohols, 8 acyl donors and 6 hydrolases were analysed using an original method. The reaction outcome was determined by semi-automated semi-automated solid-phase microextraction and GC/MS (SPME-GC/MS) allowing rapid evaluation of the success rate of each enzyme. Using Candida antarctica Lipase B (CALB), in 36% of the cases (46 reactions) quantitative conversion of the starting alcohol was observed, with an average isolated yield of 96%. The platform was then used to screen other enzymes with the CALB non-reacting substrates, allowing the design and optimisation of some efficient enzymatic reactions. Modification of the odour profile of rose essential oils by enzymatic treatment was also carried out.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.