Improved production of butyl butyrate with lipase from Thermomyces lanuginosus immobilized on styrene-divinylbenzene beads

被引:102
作者
Martins, Andrea B. [1 ]
Friedrich, John L. R. [1 ]
Cavalheiro, Jhonnattas C. [1 ]
Garcia-Galan, Cristina [3 ]
Barbosa, Oveimar [3 ,4 ]
Ayub, Marco A. Z. [2 ]
Fernandez-Lafuente, Roberto [3 ]
Rodrigues, Rafael C. [1 ]
机构
[1] Fed Univ Rio Grande Sul State, Inst Food Sci & Technol, Biocatalysis & Enzyme Technol Lab, BR-91501970 Porto Alegre, RS, Brazil
[2] Fed Univ Rio Grande Sul State, Inst Food Sci & Technol, Biochem Engn Lab, BiotecLab, BR-91501970 Porto Alegre, RS, Brazil
[3] ICP CSIC, Dept Biocatalysis, Madrid 28049, Spain
[4] Univ Ind Santander, Grp Invest Bioquim & Microbiol GIBIM, Escuela Quim, Bucaramanga, Colombia
关键词
Interfacial activated lipases; Esterification; Butyl butyrate; TLL; Styrene-divinylbenzene beads; CANDIDA-ANTARCTICA; ESTER SYNTHESIS;
D O I
10.1016/j.biortech.2013.02.052
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
Two immobilized preparations from Thermomyces lanuginosus lipase (TLL) were compared in the synthesis of butyl butyrate. The commercial Lipozyme TL-IM, and TLL immobilized on styrene-divinylbenzene beads (MCI-TLL) were tested in the esterification reaction using n-hexane as solvent. The variables temperature (30-60 degrees C), substrate molar ratio (1:1 to 5:1), added water (0-1%), and biocatalyst content (3-40%) were evaluated in terms of initial reaction rate for each biocatalyst. SDS-PAGE analysis revealed that MCI-TLL had an immobilized enzymatic load twice as high as Lipozyme TL-IM, but with an activity 3-fold higher. MCI-TLL presented high initial reaction rates up to 1.0 M butyric acid, while Lipozyme TL-IM showed a decrease in its activity above 0.5 M. Moreover, MCI-TLL allowed a productivity of 14.5 mmol g(-1) h(-1), while Lipozyme TL-IM 3.2 mmol g(-1) h(-1), both by mass of biocatalyst. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:417 / 422
页数:6
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