scholarly journals Cocoa olein glycerolysis with lipase Candida antarctica in a solvent free system

2020 ◽  
Vol 71 (4) ◽  
pp. 383
Author(s):  
L. S. Zamorano ◽  
P. Calero Magaña ◽  
E. García Cisneros ◽  
A. V. Martínez ◽  
L. F. Martín
Keyword(s):  
Reaction Times ◽  
Candida Antarctica ◽  
Solvent Free ◽  
Raw Material ◽  
Molar Ratio ◽  
Free Acidity ◽  
Glycerol Content ◽  
Free System ◽  
Free Process ◽  
Solvent Free System

In this paper we present the valorization of cocoa olein obtained from the acid fat-splitting of soapstocks. The aim is to develop a solvent free process (enzymatically catalyzed) to maximize the production of a final product with high content of monoglycerides (MAG) and diglycerides (DAG). The effect of the enzyme dose, glycerol content, reaction times as well as the modification of the raw material and pressure were studied. The yield of the reaction increased up to 90-95% when using a vacuum of 2-3 mbar at 65 °C, enough to evaporate the water which is generated as a by-product, an enzyme dose of 1% and molar ratio oil:glycerol of 1:2. The highest yield in terms of MAG and DAG production was obtained by starting from a raw material which was rich in free acidity (FFA), rendering oil with 33.4 and 44.2% MAG and DAG, respectively. Short reaction times (6-8 h) were observed compared to previously reported results (24 h).

scholarly journals Kinetic model for FAME production using inmobilized Lipase in a solvent- free system

2019 ◽  
Vol 9 (2) ◽  
pp. 99-108
Author(s):  
John Henry Castro Posada ◽  
Angela Adriana Ruíz Colorado
Keyword(s):  
Mass Transfer ◽  
Kinetic Model ◽  
Relative Error ◽  
Solvent Free ◽  
Thermomyces Lanuginosus ◽  
Molar Ratio ◽  
Free Form ◽  
Process Conditions ◽  
Free System ◽  
Solvent Free System

A kinetic model was developed to describe FAME production from refined, bleached and deodorized palm oil (RBDPO) in a solvent-free system, using Thermomyces lanuginosus lipase, in free and immobilized form. The limitations of substrate mass transfer, enzymatic inhibition and discontinuous feeding of alcohol were considered. The kinetic model for the enzyme in free and immobilized form was validated experimentally, under the same process conditions (34°C, 0.145mg protein/g oil, 4.1:1 Methanol: Oil molar ratio). The kinetic model predicted a FAME content of 73.47 wt % at 9 hours, with a relative error of 0.140% using the enzyme in free form, while the FAME content predicted by the kinetic model was 47.04 wt % at 9 hours with a relative error of 0.026 using the enzyme in immobilized form. The decrease in the percentage of esters using the enzyme in immobilized form was attributed to limitations by external mass transfer.

Studies on the Esterification Synthesis of Alkyl Oleates in Solvent-Free System by Candida Sp. Lipase

2013 ◽  
Vol 634-638 ◽  
pp. 599-603
Author(s):  
Hui Zhong ◽  
Zheng Fang ◽  
Bao Hua Zou ◽  
Xin Li ◽  
Kai Guo
Keyword(s):  
Oleic Acid ◽  
High Selectivity ◽  
Enzyme Concentration ◽  
Solvent Free ◽  
Hydroxyl Group ◽  
Molar Ratio ◽  
High Yield ◽  
Free System ◽  
Candida Sp ◽  
Solvent Free System

The alkyl oleates were prepared by esterification of oleic acid with alkyl alcohols catalyzed by the lipase from Candida sp. 99-125 in solvent-free system. The influence of several factors, including enzyme concentration, temperature, molar ratio between oleic acid and alkyl alcohols and the structures of alcohols, was also investigated. The results indicated that the reactions catalyzed by lipase at 20 oC, in the presence of 5% (w/w) lipase, on the molar ratio of 1:1 between oleic acid and alcohols, afforded products in high yield and showed high selectivity to the alcohols with less hindrance on hydroxyl group. The lipase from Candida sp. 99-125 was identified to be an effective catalyst in the esterification of alcohol and oleic acid at low temperature.

scholarly journals Optimization of enzymatic synthesis of ethyl hexanoate in a solvent free system using response surface methodology (RSM)

Biocatalysis ◽  
2018 ◽  
Vol 4 (1) ◽  
pp. 14-26 ◽  
Author(s):  
Sarita D. Gawas ◽  
Nidya Lokanath ◽  
Virendra K. Rathod
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Solvent Free ◽  
Molar Ratio ◽  
Esterification Reaction ◽  
Enzymatic Esterification ◽  
Ethyl Hexanoate ◽  
Free System ◽  
Acid Ratio ◽  
Solvent Free System

Abstract The present paper demonstrates application of biocatalysis to the synthesis of ethyl hexanoate, i.e. pineapple flavour ester, in a solvent free system. In order to evaluate the effect of various process parameters on reaction conversion, response surface methodology (RSM) complemented by central composite design (CCD) was employed. A maximum conversion of 88.57% was obtained while changing one factor at a time, at optimum conditions of temperature (50 °C), enzyme dose (2%), molar ratio acid to alcohol (1:3), speed of agitation 250 rpm and reaction time of 120 min. Based on this RSM study, the optimum predicted conditions were: 1:3.39 alcohol to acid ratio, 2.35% enzyme loading and 48.83 oC, for a predicted conversion of 90.99%. The activation energy for the enzymatic esterification was determined and calculated to be 25.76 kJ/mol. The positive values of Gibbs-free energy (ΔG), enthalpy (ΔH) and negative value of entropy (ΔS) revealed that the esterification reaction was non-spontaneous and an endothermic reaction. The reaction seems to follow bi-substrate Ping Pong Bi Bi mechanism with inhibition by both substrates.

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