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 - Funding Information:
This work was supported by Fondecyt , Chile (Project 1130981). Ms. Guajardo thanks CONICYT for her PhD scholarship. The authors also thank Professor Juan Pablo Soto of the Chemistry Institute of the Pontificia Universidad Católica de Valparaíso for chemical synthesis of α-MBG.
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
VL - 50
SP - 1870
EP - 1877
JO - Process Biochemistry
JF - Process Biochemistry
SN - 1359-5113
IS - 11
ER -