Ethyl esters production catalyzed by immobilized lipases is influenced byn-hexaneandter-amyl alcohol as organic solvents

Author(s)

Borges, Janaina Pires ^[1] ; Quilles Junior, Jose Carlos ^[2] ; Moreno-Perez, Sonia ^[3] ; Fernandez-Lorente, Gloria ^[4] ; Boscolo, Mauricio ^[2] ; Gomes, Eleni ^[4] ; da Silva, Roberto ^[2] ; Bocchini, Daniela Alonso ^[1] ; Guisan, Jose Manuel ^[5]

Affiliation

^[1] IQ UNESP, Dept Biochem & Chem Technol, Rua Prof Francisco Degni 55, BR-14800060 Araraquara, SP - Brazil

^[2] IBILCE UNESP, Dept Chem & Environm Sci, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil

^[3] CSIC, CIAL, Res Inst Food Sci, Dept Biotechnol & Food Microbiol, Campus UAM, Madrid 28049 - Spain

^[4] IBILCE UNESP, Dept Biol, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil

^[5] CSIC, Dept Catalysis, Campus UAM, Madrid 28049 - Spain

• Document type: Journal article
• Source: Bioprocess and Biosystems Engineering; JUN 2020.
• Web of Science Citations: 0

Abstract

Lipase stability in organic solvent is crucial for its application in many biotechnological processes as biocatalyst. One way to improve lipase's activity and stability in unusual reaction medium is its immobilization on inert supports. Here, lipases from different sources and immobilized through weak chemical interactions on hydrophobic and ionic supports had their transesterification ability dramatically dependent on the support and also on the solvent that had been used. The ethanolysis of sardine oil was carried out at the presence of cyclohexane and tert-amyl alcohol, in which Duolite A568-Thermomyces lanuginosalipase derivative achieved 49% of ethyl esters production after 24 h in cyclohexane. The selectivity of immobilized lipases was also studied and, after 3 h of synthesis, the reaction with Duolite A568-Thermomyces lanuginosaderivative in cyclohexane produced 24% ethyl ester of eicosapentaenoic acid and 1.2% ethyl ester of docosahexaenoic acid, displaying a selectivity index of 20 times the ethyl ester of eicosapentaenoic acid. Different derivatives ofCandida antarcticalipases fraction B (CALB) and phospholipaseLecitase (R) Ultra (Lecitase) were also investigated. Along these lines, a combination between these factors may be applied to improve the activity and selectivity of immobilized lipases, decreasing the total cost of the process. (AU)

• FAPESP's process: 13/00530-0 - Immobilization and stabilization of lipases from Candida antarctida: fraction b and its application in biocatalysis
• Grantee: José Carlos Quilles Junior
• Support type: Scholarships abroad - Research Internship - Master's degree
• FAPESP's process: 12/09054-3 - Immobilization of lipases on agarose and chitosan and application in biocatalysis.
• Grantee: José Carlos Quilles Junior
• Support type: Scholarships in Brazil - Master