Selectivity of R-α-monobenzoate glycerol synthesis catalyzed by Candida antarctica lipase B immobilized on heterofunctional supports

N. Guajardo, C. Bernal, LORENA EVELYN WILSON SOTO, Z. Cabrera

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

The main goal of this work was to study different strategies of immobilization of Candida antarctica lipase B (CALB) in order to evaluate changes in the selectivity of this enzyme when R-α-monobenzoate glycerol (R-α-MBG) is obtained through of asymmetric esterification. CALB was immobilized on sepharose and silica functionalized with octyl groups (monofunctional supports) and undecanol-glyoxyl and octyl-epoxide groups (heterofunctional supports). Our results showed that the enzyme could be immobilized by all carriers, with activity yields ranging from 52% to 83%. CALB immobilized on silica octyl was the most active (367 IU g-1biocatalyst) with immobilization yields in terms of protein and expressed activity of 72% and 50% respectively and exhibited a higher half-life in 100% 1,4-dioxane at 50 °C (85,000 h). In contrast, CALB immobilized on heterofunctional silica support was the most selective biocatalyst, reaching an enantiomeric excess of 99% of R-α-MBG in 100% 1,4-dioxane. In terms of configuration the sepharose biocatalysts results in a S-enantiomer, while silica biocatalysts results in a R-enantiomer. The catalysis of asymmetric esterification of glycerol with benzoic acid to obtain R-α-MBG by CALB immobilized in heterofunctional silica is highly selective and, to our knowledge, is the most selective reported to date.

Original languageEnglish
Pages (from-to)1870-1877
Number of pages8
JournalProcess Biochemistry
Volume50
Issue number11
DOIs
StatePublished - Nov 2015
Externally publishedYes

Keywords

  • Asymmetric esterification
  • Heterofunctional supports
  • Immobilized CALB
  • R-α-Monobenzoate glycerol
  • Selectivity

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