Immobilized lipase-mediated acidolysis of butteroil with conjugated linoleic acid: batch reactor and packed bed reactor studies

2001 ◽  
Vol 11 (4-6) ◽  
pp. 623-632 ◽  
Author(s):  
Hugo S Garcia ◽  
José A Arcos ◽  
Kurt J Keough ◽  
Charles G Hill
2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Hsiao-Ching Chen ◽  
Hen-Yi Ju ◽  
Tsung-Ta Wu ◽  
Yung-Chuan Liu ◽  
Chih-Chen Lee ◽  
...  

An optimal continuous production of biodiesel by methanolysis of soybean oil in a packed-bed reactor was developed using immobilized lipase (Novozym 435) as a catalyst in atert-butanol solvent system. Response surface methodology (RSM) and Box-Behnken design were employed to evaluate the effects of reaction temperature, flow rate, and substrate molar ratio on the molar conversion of biodiesel. The results showed that flow rate and temperature have significant effects on the percentage of molar conversion. On the basis of ridge max analysis, the optimum conditions were as follows: flow rate 0.1 mL/min, temperature52.1∘C, and substrate molar ratio 1 : 4. The predicted and experimental values of molar conversion were83.31±2.07% and82.81±.98%, respectively. Furthermore, the continuous process over 30 days showed no appreciable decrease in the molar conversion. The paper demonstrates the applicability of using immobilized lipase and a packed-bed reactor for continuous biodiesel synthesis.


2015 ◽  
Vol 29 (5) ◽  
pp. 3168-3175 ◽  
Author(s):  
Sarah M. Meunier ◽  
Amin R. Rajabzadeh ◽  
Trevor G. Williams ◽  
Raymond L. Legge

2000 ◽  
Vol 83 (3) ◽  
pp. 371-377 ◽  
Author(s):  
H.S. Garcia ◽  
K.J. Keough ◽  
J.A. Arcos ◽  
C.G. Hill

2011 ◽  
Vol 88 (12) ◽  
pp. 1925-1933 ◽  
Author(s):  
Roberta Claro da Silva ◽  
Fabiana Andreia Schaffer De Martini Soares ◽  
Thaís Gonzaga Fernandes ◽  
Anna Laura Donadi Castells ◽  
Kelly Caroline Guimarães da Silva ◽  
...  

2001 ◽  
Vol 8 (3) ◽  
pp. 213-216 ◽  
Author(s):  
Yoshiyuki Watanabe ◽  
Yoshimasa Miyawaki ◽  
Shuji Adachi ◽  
Kazuhiro Nakanishi ◽  
Ryuichi Matsuno

2009 ◽  
Vol 62 (9) ◽  
pp. 1034 ◽  
Author(s):  
Jeck Fei Ng ◽  
Stephan Jaenicke

Recombinant Escherichia coli overexpressing the gene LbADH, which encodes for an alcohol dehydrogenase from Lactobacillus brevis, was successfully transformed and cultured. The cells are able to catalyze the reduction of pro-chiral ketones, e.g. ethyl acetoacetate into R-(–)ethyl hydroxybutyrate (EHB) with high conversion and enantiomeric excess >99%. Immobilizing the whole cells in alginate beads leads to a catalyst with improved stability and ease of handling while maintaining the high activity of the free cells. The whole-cell catalyst was tested in a stirred batch reactor (CSTR) and in a continuously operated packed-bed reactor. An Mg2+ concentration of 2 mM was crucial for maintaining the activity of the biocatalyst. After a partial optimization of the process conditions, a productivity of 1.4 gEHB gwcw–1 h–1 could be maintained in a continuous flow reactor over a prolonged period of time.


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