Influence of compressed fluids treatment on the activity of Yarrowia lipolytica lipase

被引:34
作者
De Oliveira, D
Feihrmann, AC
Dariva, C
Cunha, AG
Bevilaqua, JV
Destain, J
Oliveir, JV
Freire, DMG [1 ]
机构
[1] Univ Fed Rio de Janeiro, Inst Quim, Ctr Technol, BR-21945970 Rio de Janeiro, Brazil
[2] Univ Reg Integrada Alto Uruguai & Missoes, Dept Food Engn, BR-99700000 Erechim, RS, Brazil
[3] CENPES, Petrobras Res & Dev Ctr, Petrobras, Brazil
[4] Univ Liege, Ctr Wallon Biol Ind, Gembloux, Belgium
关键词
lipases; enzyme immobilization; compressed gases; enzyme activity; supercritical fluids;
D O I
10.1016/j.molcatb.2006.01.016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This work investigated the influence of temperature, pressure, exposure times and depressurization rate on the activity of a non-commercial immobilized lipase from Yarrowia lipolytica (YLL) submitted to compressed carbon dioxide, propane and n-butane. A high-pressure cell was employed in the experiments, in the pressure range of 10-280 bar, varying the temperature from 35 to 75 degrees C, exposure times from I to 6 h, and adopting distinct decompression rates. Results showed that significant activity losses were obtained when the treatment was conducted in carbon dioxide, while negligible losses were observed in both propane and n-butane. For the treatment with carbon dioxide, within the range studied, the decompression rate affected positively enzyme activity, while the exposure time and temperature presented an opposite effect on the non-commercial immobilized lipase from Y lipolytica (YLL). Additionally, the performance of two commercial immobilized lipases (Lipozyme IM and Novozym 435) and the immobilized YLL in the three solvents was compared. Immobilized YLL has shown to be more suitable than Lipozyme IM for enzyme-catalyzed reactions using compressed propane and n-butane as solvents, but with inferior performance compared to Novozym 435 treated in these solvents. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:117 / 123
页数:7
相关论文
共 42 条
[1]   Lipase immobilisation: an equilibrium study of lipases immobilised on hydrophobic and hydrophilic/hydrophobic supports [J].
Al-Duri, B ;
Yong, YP .
BIOCHEMICAL ENGINEERING JOURNAL, 2000, 4 (03) :207-215
[2]   Novozym 435 activity in compressed gases. Water activity and temperature effects [J].
Almeida, MC ;
Ruivo, R ;
Maia, C ;
Freire, L ;
de Sampaio, TC ;
Barreiros, S .
ENZYME AND MICROBIAL TECHNOLOGY, 1998, 22 (06) :494-499
[3]  
Angus S., 1976, INT THERMODYNAMIC TA
[4]   Effects of high pressure processing on polyphenoloxidase enzyme activity of grape musts [J].
Castellari, M ;
Matricardi, L ;
Arfelli, G ;
Rovere, P ;
Amati, A .
FOOD CHEMISTRY, 1997, 60 (04) :647-649
[5]   The role of the reaction medium in lipase-catalyzed esterifications and transesterifications [J].
Cernia, E ;
Palocci, C ;
Soro, S .
CHEMISTRY AND PHYSICS OF LIPIDS, 1998, 93 (1-2) :157-168
[6]  
CHEN H, 2000, PRINCIPLES DESIGN AP, P1, DOI DOI 10.2118/59043-MS
[7]  
CHI YM, 1988, AGR BIOL CHEM TOKYO, V52, P1541
[8]   Optimization of enzymatic production of biodiesel from castor oil in organic solvent medium [J].
Débora de Oliveira ;
Marco Di Luccio ;
Carina Faccio ;
Clarissa Dalla Rosa ;
João Paulo Bender ;
Nádia Lipke ;
Silvana Menoncin ;
Cristiana Amroginski ;
José Vladimir de Oliveira .
Applied Biochemistry and Biotechnology, 2004, 115 (1-3) :771-780
[9]   A kinetic study of lipase-catalyzed alcoholysis of palm kernel oil [J].
de Oliveira, D ;
Alves, TLM .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2000, 84-6 (1-9) :59-68
[10]   Improvement of lipase production from Yarrowia lipolytica [J].
Destain, J ;
Roblain, D ;
Thonart, P .
BIOTECHNOLOGY LETTERS, 1997, 19 (02) :105-107