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PublicationChemistrySelect
Year2016
Volume1
Pages3259–3270
International

ADVANTAGES OF HETEROFUNCTIONAL OCTYL SUPPORTS. PRODUCTION OF 1,2-DIBUTYRIN BY SPECIFIC AND SELECTIVE HYDROLYSIS OF TRIBUTYRIN CATALYZED BY IMMOBILIZED LIPASES.

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimization of biocatalysts and bioprocesses
Daniela B. Hirata1,2, Tiago L. Albuquerque1,3, Nazzoly Rueda1,4 Jose M. Sánchez-Montero5 Eduardo Garcia-Verdugo6, Raul Porcar6, Roberto Fernandez-Lafuente1,*
 
1. Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC, Cantoblanco, 28049 Madrid, Spain.
2. Instituto de Química, Universidade Federal de Alfenas, 37130-000 Alfenas, MG, Brazil.
3. Departamento de Engenharia Química, Universidade Federal Do Ceará, Campus Do Pici, CEP 60455-760, Fortaleza, CE, Brazil.
4. Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia.
5. Organic and Pharmaceutical Chemistry Dpt. Biotransformations Group. Facultad de Farmacia, UCM, 28040 Madrid
6. Dtp. Quimica Inorganica y Organica, Universidad Jaume I, Avda. Sos Baynat s/n, 12071, Castellón, Spain


Different lipases immobilized on octyl agarose or heterofunctional (glyoxyl or divinylsulfone) octyl supports have been compared in the selective and specific production of 1,2-dibutyrin by hydrolysis of tributyrin. The addition of cosolvents improved the solubility of the substrate thus improving the accumulation of 1,2-dibutyrin. The form B of the lipase from Candida antarctica was selected considering reaction both enzyme activity and reaction yields produced by this biocatalyst. Using this enzyme, the highest dibutyrin yields using 100 mM of tributyrin (over 80%) was obtained using a medium containing 50% of cosolvent. However, the use of higher tributyrin concentrations required increasing the concentration of cosolvent in order to increase the soluble fraction of substrate. Under these conditions, the enzyme is released to the medium if it is just physically adsorbed on the support. For this reason, the octyl-CALB biocatalyst is unsuitable for this reaction. Using octyl-glyoxyl-CALB in the presence of 75% cosolvent to facilitate substrate solubility, a conversion yield of 70% of dibutyrin could be achieved using 1 M of tributyrin as substrate. Using 500 mM tributyrin, the yield under these conditions increased to 80%. The biocatalyst could be reused for several cycles without any detrimental effect on its performance.
Keywords:1, heterofunctional supports, enzyme selectivity, enzyme specificity, glyoxyl-octyl supports, 2-dibutyrin.
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