scholarly journals Immobilization of lipase on sepabeads and its application in pentyl octanoate synthesis in a low aqueous system

2008 ◽  
pp. 139-152 ◽  
Author(s):  
Zorica Knezevic-Jugovic ◽  
SvetlanaV. Saponjic ◽  
Dejan Bezbradica ◽  
Dusan Mijin
Keyword(s):  
Molecular Sieves ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Aqueous System ◽  
Molar Ratio ◽  
Process Conditions ◽  
Initial Water Content ◽  
Initial Water ◽  
Initial Substrate ◽  
Substrate Molar Ratio

The object of the study was to investigate the process conditions relevant for the pentyl octanoate production with the lipase from Candida rugosa immobilized on Sepabeads EC-EP carrier. This is an epoxide-containing commercial polymethacrylic carrier with suitable characteristics for enzyme immobilization. The immobilized lipase suitable for pentyl octanoate synthesis has been prepared by a direct lipase binding to polymers via their epoxide groups. The enzymatic activity was determined by both hydrolysis of olive oil in an aqueous system and esterification of n-pentanol with octanoic acid in a low aqueous system. The influence of several important reaction parameters such as temperature, initial water content, initial substrate molar ratio, enzyme loading and time of adding of molecular sieves in the system is carefully analyzed by means of an experimental design. Production of the ester was optimized and an ester production response equation was obtained, making it possible to predict ester yields from known values of the five main factors. Almost complete conversion (>99%) of the substrate to ester could be realized, using lipase loading as low as 37 mg/g dry support and in a relatively short time (24 h) at 45?C, when high initial substrate molar ratio of 2.2 is used.

scholarly journals The immobilization of lipase on Sepabeads: Coupling, characterization and application in geranyl butyrate synthesis in a low aqueous system

2008 ◽  
Vol 14 (4) ◽  
pp. 245-249 ◽  
Author(s):  
Zorica Knezevic-Jugovic ◽  
Jasmina Damnjanovic ◽  
Dejan Bezbradica ◽  
Dusan Mijin
Keyword(s):  
Molecular Sieves ◽  
Immobilized Enzyme ◽  
Candida Rugosa ◽  
Aqueous System ◽  
Molar Ratio ◽  
Esterification Reaction ◽  
Initial Water Content ◽  
Initial Water ◽  
Organic System ◽  
Geranyl Butyrate

Lipase from Candida rugosa immobilized on Sepabeads EC-EP was shown to catalyze the esterification of geraniol with butyric acid in a predominantly organic system. The immobilization procedure was adjusted to optimize the enzyme activity and the immobilized enzyme was then used for a geranyl butyrate synthesis as a study model. The immobilized enzyme showed favorable performances in an aqueous system and increased the stability in the presence of organic solvents. The response surface methodology and a 5-level-5-factor central composite rotatable design were performed to identify the factors that influence the ester production and to verify whether any changes should be made in their settings to improve this reaction. The initial water content, the reaction temperature, the enzyme concentration, acid/alcohol molar ratio and time of addition of molecular sieves were the variables investigated. The production of the ester was optimized and an ester production response equation was obtained, making it possible to predict ester yields from the known values of the five main factors. The temperature during the esterification reaction was identified as the factor having the greatest impact on the ester yield.

scholarly journals Enzymatic Synthesis of Isopropyl Acetate by Immobilized   Bacillus cereus Lipase in Organic Medium

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Madan Lal Verma ◽  
Wamik Azmi ◽  
Shamsher Singh Kanwar
Keyword(s):  
Acetic Acid ◽  
Bacillus Cereus ◽  
Water Activity ◽  
Molecular Sieves ◽  
Immobilized Lipase ◽  
Molar Ratio ◽  
Ester Synthesis ◽  
Initial Water ◽  
Isopropyl Acetate ◽  
Mg Addition

Selective production of fragrance fatty acid ester from isopropanol and acetic acid has been achieved using silica-immobilized lipase of Bacillus cereus MTCC 8372. A purified thermoalkalophilic extracellular lipase was immobilized by adsorption onto the silica. The effects of various parameters like molar ratio of substrates (isopropanol and acetic acid; 25 to 100 mM), concentration of biocatalyst (25–125 mg/mL), reaction time, reaction temperature, organic solvents, molecular sieves, and initial water activity were studied for optimal ester synthesis. Under optimized conditions, 66.0 mM of isopropyl acetate was produced when isopropanol and acetic acid were used at 100 mM: 75 mM in 9 h at 55°C in n-heptane under continuous shaking (160 rpm) using bound lipase (25 mg). Addition of molecular sieves (3 Å  × 1.5 mm) resulted in a marked increase in ester synthesis (73.0 mM). Ester synthesis was enhanced by water activity associated with pre-equilibrated saturated salt solution of LiCl. The immobilized lipase retained more than 50% of its activity after the 6th cycle of reuse.

scholarly journals Lipase catalyzed synthesis of flavor esters in non-aqueous media: Optimization of the yield of pentyl 2-methylpropanoate by statistical analysis

2008 ◽  
Vol 73 (12) ◽  
pp. 1139-1151 ◽  
Author(s):  
Zorica Knezevic-Jugovic ◽  
Dejan Bezbradica ◽  
Zivana Jakovljevic ◽  
Suzana Brankovic-Dimitrijevic ◽  
Dusan Mijin
Keyword(s):  
Reaction Time ◽  
Aqueous Media ◽  
Candida Rugosa ◽  
Enzyme Concentration ◽  
Yield Response ◽  
Process Conditions ◽  
Initial Water Content ◽  
Initial Water ◽  
Ester Yield ◽  
Added Water

In this study, the synthesis of pentyl 2-methylpropanoate employing a commercial lipase from Candida rugosa was investigated, the emphasis being placed on analyzing the effects of various process conditions on the yield of ester. The response surface methodology (RSM) and five-level-five-factor central composite rotatable design (CCRD) were used to evaluate the effects of variables, namely the initial water content, 0.0-2.0% (w/v), the reaction temperature, 35-75?C, the enzyme concentration, 1.0-5.0 g dm-3, the acid/alcohol mole ratio, 1:2-5:2, and the reaction time, 4-48 h, on the yield (%) of ester. The production of pentyl 2-methylpropanoate was optimized and an ester yield response equation was obtained, enabling the prediction of ester yields from known values of the five main factors. It seems that the enzyme concentration, reaction time and acid/alcohol mole ratio predominantly determine the conversion process, while the amount of added water amount had no significant influence on the ester yield. Conversion of around 92 % of the substrate to ester could be realized using a concentration of lipase as low as 4.0 g dm-3 and in a relatively short time (26 h) at 35?C, when a high substrate mole ratio of 2.5 was used.

scholarly journals Green Synthesis of Decaglycerol Laurates by Lipase-Catalyzed Transesterification of Methyl Laurate with Decaglycerol

2019 ◽  
Vol 2019 ◽  
pp. 1-7
Author(s):  
Wenyue Wang ◽  
Changyao Liu ◽  
Guiju Zhang ◽  
Fan Yang ◽  
Xiaoyan Wang ◽  
...  
Keyword(s):  
Immobilized Lipase ◽  
Orthogonal Test ◽  
Methyl Laurate ◽  
Molar Ratio ◽  
Initial Water Content ◽  
Ionization Mass ◽  
Optimum Conditions ◽  
Initial Water ◽  
Reaction Optimization ◽  
Enzyme Dosage

Decaglycerol laurates have been widely used as emulsifiers in food, medicine, and cosmetic industries for many years. Currently, they are synthesized using alkaline catalysts under stringent conditions. Here, decaglycerol laurates were prepared through a green lipase-catalyzed process, employing the transesterification of methyl laurate with decaglycerol by the immobilized lipase (Novozym 435). Single-factor experiments and orthogonal test were used for reaction optimization. The optimum conditions were obtained as follows: reaction temperature of 65°C, a laurate/decaglycerol molar ratio of 2 : 1, an oscillating speed of 180 rpm, an enzyme dosage (based on amount of methyl laurate) of 8 wt.%, initial water content (based on the total substrate mass) of 5.0 wt.%, and reaction time of 4.5 h with 84.4% conversion of methyl laurate. The transesterification products were identified by electrospray ionization mass spectrometer. In addition, the surface activity of decaglycerol laurates was also characterized, and the surface tension of water was reduced to 33 mN·m−1 at a concentration magnitude of 10−5 g/mL.

scholarly journals Continuous Production of Lipase-Catalyzed Biodiesel in a Packed-Bed Reactor: Optimization and Enzyme Reuse Study

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Hsiao-Ching Chen ◽  
Hen-Yi Ju ◽  
Tsung-Ta Wu ◽  
Yung-Chuan Liu ◽  
Chih-Chen Lee ◽  
...  
Keyword(s):  
Flow Rate ◽  
Immobilized Lipase ◽  
Continuous Production ◽  
Packed Bed ◽  
Packed Bed Reactor ◽  
Molar Ratio ◽  
System Response ◽  
Biodiesel Synthesis ◽  
Substrate Molar Ratio ◽  
Molar Conversion

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.

scholarly journals Interesterification of Egg-Yolk Phosphatidylcholine with p-Methoxycinnamic Acid Catalyzed by Immobilized Lipase B from Candida Antarctica

Catalysts ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1181
Author(s):  
Magdalena Rychlicka ◽  
Anna Gliszczyńska
Keyword(s):  
Reaction Time ◽  
Design Method ◽  
Immobilized Lipase ◽  
Reaction Medium ◽  
Solvent System ◽  
Novozym 435 ◽  
Molar Ratio ◽  
Binary Solvent ◽  
Methoxycinnamic Acid ◽  
Substrate Molar Ratio

The p-methoxycinnamic acid (p-MCA) is one of the most popular phenylpropanoids, the beneficial impact of which on the human health is well documented in the literature. This compound has shown many valuable activities including anticancer, antidiabetic, and neuro- and hepatoprotective. However, its practical application is limited by its low bioavailability resulting from rapid metabolism in the human body. The latest strategy, aimed at overcoming these limitations, is based on the production of more stability in systemic circulation bioconjugates with phospholipids. Therefore, the aim of this research was to develop the biotechnological method for the synthesis of phospholipid derivatives of p-methoxycinnamic acid, which can play a role of new nutraceuticals. We developed and optimized enzymatic interesterification of phosphatidylcholine (PC) with ethyl p-methoxycinnamate (Ep-MCA). Novozym 435 and a binary solvent system of toluene/chloroform 9:1 (v/v) were found to be the effective biocatalyst and reaction medium for the synthesis of structured p-MCA phospholipids, respectively. The effects of the other reaction parameters, such as substrate molar ratio, enzyme dosage, and reaction time, on the degree of incorporation of p-MCA into PC were evaluated by use of an experimental factorial design method. The results showed that substrate molar ratio and biocatalyst load have significant effects on the synthesis of p-methoxycinnamoylated phospholipids. The optimum conditions were: Reaction time of three days, 30% (w/w) of Novozym 435, and 1/10 substrate molar ratio PC/Ep-MCA. Under these parameters, p-methoxycinnamoylated lysophosphatidylcholine (p-MCA-LPC) and p-methoxycinnamoylated phosphatidylcholine (p-MCA-PC) were obtained in isolated yields of 32% and 3% (w/w), respectively.

scholarly journals Biosynthesis of ethyl butyrate with immobilized Candida rugosa lipase onto modified Eupergit®C

Biocatalysis ◽  
2014 ◽  
Vol 1 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Daniele Spinelli ◽  
Simone Coppi ◽  
Riccardo Basosi ◽  
Rebecca Pogni
Keyword(s):  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Product Yield ◽  
Candida Rugosa Lipase ◽  
Maximum Activity ◽  
Ethyl Butyrate ◽  
Molar Ratio ◽  
Practical Applications ◽  
Solvent Free Conditions ◽  
Immobilized Candida Rugosa Lipase

AbstractLipase from Candida rugosa was immobilized onto the modified Eupergit®C. The support was treated with ethylenediamine and subsequently activated with glutaraldehyde. Enzyme immobilization efficiency was 85%. The optimum pH was close to 6.5 for both the free and immobilized lipase. Immobilized lipase retained its maximum activity in a temperature range of 55 – 60°C. Subsequently, ethyl butyrate synthesis was investigated using immobilized enzyme by esterification of butyric acid with ethanol in solvent-free conditions (23% product yield) and using hexane as a solvent (65% product yield). The acid-alcohol molar ratio and different enzyme amounts were tested as efficient reaction parameters. The biocatalyst maintained 60% of its activity when reused in 8 successive batch reactions in organic solvent. Therefore, the immobilized lipase has demonstrated its potential in practical applications such as short-chain ester synthesis for the food industry.

scholarly journals Synthesis of Isopropyl Ferulate Using Silica-Immobilized Lipase in an Organic Medium

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Ashok Kumar ◽  
Shamsher Singh Kanwar
Keyword(s):  
Ferulic Acid ◽  
Molecular Sieves ◽  
Isopropyl Alcohol ◽  
Immobilized Lipase ◽  
Inhibitory Effect ◽  
Organic Medium ◽  
Molar Ratio ◽  
Forward Reaction ◽  
Salt Ions ◽  
The Matrix

Immobilization of lipases has proved to be a useful technique for improving an enzyme's activity in organic solvents. In the present study, the performance of a silica-immobilized lipase was evaluated for the synthesis of isopropyl ferulate in DMSO. The biocatalyst was cross-linked onto the matrix with 1% glutaraldehyde. The effects of various parameters, molar ratio of ferulic acid to isopropyl alcohol (25 mM : 100 mM), concentration of biocatalyst (2.5–20 mg/mL), molecular sieves (25–250 mg/mL), and various salt ions, were studied consecutively as a function of percent esterification. Immobilized lipase at 25 mg/mL showed maximum esterification (~84%) of ferulic acid and isopropanol at a molar ratio of 25 mM : 100 mM, respectively, in DMSO at 45°C in 3 h under shaking (150 rpm). To overcome the inhibitory effect of water (a byproduct) if any, in the reaction mixture, molecular sieves (3 Å × 1.5 mm; 100 mg/mL) were added to the reaction mixture to promote the forward reaction. Salt ions like Ca2+, Cd2+, and Fe2+ enhanced the activity of immobilized biocatalyst while a few ions like Co2+, Zn2+, Mg2+, Mn2+, Al3+, and Na+ had mild inhibitory effect. Approximately, one third of total decrease in the esterification efficacy was observed after the 5th repetitive cycle of esterification.

scholarly journals Production and Characterization of Biodiesel Using Nonedible Castor Oil by Immobilized Lipase fromBacillus aerius

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Sunil Kumar Narwal ◽  
Nitin Kumar Saun ◽  
Priyanka Dogra ◽  
Ghanshyam Chauhan ◽  
Reena Gupta
Keyword(s):  
Castor Oil ◽  
Immobilized Lipase ◽  
Chemical Reactor ◽  
Molar Ratio ◽  
Free System ◽  
H Nmr ◽  
Solvent Free System ◽  
Substrate Molar Ratio ◽  
Optimized Conditions

A novel thermotolerant lipase fromBacillus aeriuswas immobilized on inexpensive silica gel matrix. The immobilized lipase was used for the synthesis of biodiesel using castor oil as a substrate in a solvent free system at 55°C under shaking in a chemical reactor. Several crucial parameters affecting biodiesel yield such as incubation time, temperature, substrate molar ratio, and amount of lipase were optimized. Under the optimized conditions, the highest biodiesel yield was up to 78.13%. The characterization of synthesized biodiesel was done through FTIR spectroscopy,1H NMR spectra, and gas chromatography.

scholarly journals Enzymatic Production of Biodiesel Using Immobilized Lipase on Core-Shell Structured Fe3O4@MIL-100(Fe) Composites

Catalysts ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 850 ◽  
Author(s):  
Xie ◽  
Huang
Keyword(s):  
Immobilized Lipase ◽  
Metal Organic Framework ◽  
Candida Rugosa ◽  
Covalent Immobilization ◽  
Molar Ratio ◽  
Core Shell ◽  
Enzymatic Production ◽  
Metal Organic ◽  
Significant Mass Loss ◽  
Significant Mass

In this research, core–shell structured Fe3O4@MIL-100(Fe) composites were prepared by coating Fe3O4 magnetite with porous MIL-100(Fe) metal-organic framework (MOF) material, which were then utilized as magnetic supports for the covalent immobilization of the lipase from Candida rugosa through amide linkages. By using the carbodiimide/hydroxysulfosuccinimide (EDC/NHS) activation strategy, the lipase immobilization efficiency could reach 83.1%, with an activity recovery of 63.5%. The magnetic Fe3O4@MIL-100(Fe) composite and immobilized lipase were characterized by several techniques. The characterization results showed that the Fe3O4 core was coated with MIL-100(Fe) shell with the formation of perfect core–shell structured composites, and moreover, the lipase was covalently tethered on the magnetic carrier. The immobilized lipase displayed a strong magnetic response and could be facilely separated by an external magnetic field. With this magnetic biocatalyst, the maximum biodiesel conversion attained 92.3% at a methanol/oil molar ratio of 4:1, with a three-step methanol addition manner, and a reaction temperature of 40 °C. Moreover, the biocatalyst prepared in the present study was recycled easily by magnetic separation without significant mass loss, and displayed 83.6% of its initial activity as it was reused for five runs, thus allowing its potential application for the cleaner production of biodiesel.

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