TY - JOUR
T1 - Selectivity of R-α-monobenzoate glycerol synthesis catalyzed by Candida antarctica lipase B immobilized on heterofunctional supports
AU - Guajardo, N.
AU - Bernal, C.
AU - Wilson, L.
AU - Cabrera, Z.
N1 - Publisher Copyright:
© 2015 Elsevier Ltd.
PY - 2015/11
Y1 - 2015/11
N2 - 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.
AB - 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.
KW - Asymmetric esterification
KW - Heterofunctional supports
KW - Immobilized CALB
KW - R-α-Monobenzoate glycerol
KW - Selectivity
UR - http://www.scopus.com/inward/record.url?scp=84946499271&partnerID=8YFLogxK
U2 - 10.1016/j.procbio.2015.06.025
DO - 10.1016/j.procbio.2015.06.025
M3 - Article
AN - SCOPUS:84946499271
SN - 1359-5113
VL - 50
SP - 1870
EP - 1877
JO - Process Biochemistry
JF - Process Biochemistry
IS - 11
ER -