Batch operational stability of immobilized heterologous Rhizopus oryzae lipase during acidolysis of virgin olive oil with medium-chain fatty acids

被引:22
|
作者
Nunes, P. A. [1 ,2 ]
Pires-Cabral, P. [1 ,2 ]
Guillen, M. [3 ]
Valero, F. [3 ]
Ferreira-Dias, S. [1 ]
机构
[1] Univ Tecn Lisboa, Inst Super Agron, CEER Biosyst Engn, P-1349017 Lisbon, Portugal
[2] Univ Algarve, Inst Super Engn, P-8005139 Faro, Portugal
[3] Univ Autonoma Barcelona, Dept Engn Quim, EE, E-08193 Barcelona, Spain
关键词
Acidolysis; Biocatalysis; Enzyme deactivation; Heterologous Rhizopus oryzae lipase; Immobilization; Structured lipids; STRUCTURED TAG RICH; PICHIA-PASTORIS; INTERESTERIFICATION; TRIACYLGLYCEROLS; GLYCEROL;
D O I
10.1016/j.bej.2012.06.004
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Structured triacylglycerols containing medium-chain fatty acids (M) at positions sn-1,3 and long-chain fatty acids (L) at the sn-2 position (MLM type), were obtained by acidolysis of virgin olive oil with caprylic or capric acid, in solvent-free media, at 40 degrees C, catalyzed by a heterologous Rhizopus oryzae lipase (r-ROL) immobilized in Eupergir (R) C or in Lewatit VP OC 1600. The biocatalyst immobilized in Eupergit was reused in consecutive 23-h batches with rehydration of the biocatalyst between batches. A first-order deactivation was observed (half-life time, t(1/2) = 39.0 h for caprylic; t(1/2) = 54.3 h for capric acid). During acidolysis with capric acid catalyzed by r-ROL immobilized in Lewatit VP OC 1600, without rehydration, a first-order deactivation was observed (t(1/2) = 49.1 h); with rehydration, a considerable increase in stability was observed (t(1/2) = 234 h; Sadana's series-type inactivation kinetics model). (C) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:265 / 268
页数:4
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