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Title

Enzymatic acylation of di- and trisaccharides with fatty acids: choosing the appropriate enzyme, support and solvent

AuthorsPlou Gasca, Francisco José ; Cruces Villalobos, María Ángeles; Ferrer, Manuel ; Fuentes, Gloria; Pastor Martínez, Eitel ; Bernabé, Manuel ; Christensen, Morten; Comelles, Francesc; Parra Juez, José Luis; Ballesteros Olmo, Antonio
KeywordsSugar esters
Lipases
Esterases
Proteases
Enzyme immobilization
Transesterification
Biocatalysis
Biotransformations
Sucrose
Maltose
Issue Date1-Oct-2009
SeriesJournal of Biotechnology, 96, 55-66 (2002)
AbstractEnzymatic synthesis of fatty acid esters of di- and trisaccharides is limited by the fact that most biological catalysts are inactivated by the polar solvents (e.g. dimethylsulfoxide, dimethylformamide) where these carbohydrates are soluble. This article reviews the methodologies developed to overcome this limitation, namely those involving control over the reaction medium, the enzyme and the support. We have proposed the use of mixtures of miscible solvents (e.g. dimethylsulfoxide and 2-methyl-2-butanol) as a general strategy to acylate enzymatically hydrophilic substrates. We observed that decreasing the hydrophobicity of the medium (i.e. lowering the percentage of DMSO) the molar ratio sucrose diesters vs. sucrose monoesters can be substantially enhanced. The different regioselectivity exhibited by several lipases and proteases makes feasible to synthesize different positional isomers, whose properties may vary considerably. In particular, the lipase from Thermomyces lanuginosus displays a notable selectivity for only one hydroxyl group in the acylation of sucrose, maltose, leucrose and maltotriose, compared with lipase from Candida antarctica. We have examined three immobilisation methods (adsorption on polypropylene, covalent coupling to Eupergit C, and silica-granulation) for sucrose acylation catalyzed by T. lanuginosus lipase. The morphology of the support affected significantly the reaction rate and/or the selectivity of the process
Publisher version (URL)doi:10.1016/S0168-1656(02)00037-8
URIhttp://hdl.handle.net/10261/17327
DOIdoi:10.1016/S0168-1656(02)00037-8
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