scholarly journals THE OPTIMIZATION OF ENZYMATIC SYNTHESIS FOR LAUROYL-N-METHYL GLUCAMIDE SURFACTANTS

2011 ◽  
Vol 11 (3) ◽  
pp. 223-228 ◽  
Author(s):  
Zuhrina Masyithah ◽  
Seri Bima Sembiring ◽  
Zul Alfian ◽  
Tjahjono Herawan
Keyword(s):  
Optimum Condition ◽  
Lauric Acid ◽  
Enzymatic Synthesis ◽  
Immobilized Lipase ◽  
Interactive Effect ◽  
Palm Kernel ◽  
Effect Of Temperature ◽  
Molar Ratio ◽  
Reaction Yield ◽  
Substrate Molar Ratio

The optimization of enzymatic synthesis for lauroyl-N-methyl glucamide surfactants is studied. The fraction of palm kernel oil namely lauric acid (AL) was amidificationed with N-methyl glucamine (MGL) to produce lauroyl-N-methyl glucamide. Study was carried out by using immobilized lipase from Candida antarctica (Novozyme 435®), and tert-amylalcohol as a solvent. Response Surface Methodology (RSM) based on a five level, three variable design was employed, firstly, for studying the interactive effect of various parameters on the reaction, and secondly, for the optimization. The reaction parameters observed were Novozyme concentration, substrate molar ratio, and temperature. Simultaneously increasing Novozyme concentration, substrate molar ratio, and temperature improves the reaction yield and the effect of temperature is noted more significant. The expected optimum condition was at molar ratio MGL:AL 1:1, the Novozyme concentration of 8% and the reaction temperature of 50-55 °C. The reactions at the optimum condition produce the convertion of lauric acid of 64.5% and yield of 96.5%. With the optimization procedure the higher alkyl glucamide yield was achieved.

scholarly journals SINTESIS STEARAMIDA DARI ASAM STEARAT DAN UREA MENGGUNAKAN PELARUT CAMPURAN : PENGARUH TEMPERATUR DAN WAKTU REAKSI

2018 ◽  
Vol 7 (1) ◽  
pp. 5-8 ◽  
Author(s):  
Muhammad Syukri ◽  
Zuhrina Masyithah
Keyword(s):  
Reaction Time ◽  
Optimum Condition ◽  
Stearic Acid ◽  
Mixed Solvent ◽  
Effect Of Temperature ◽  
Molar Ratio ◽  
Solvent Ratio ◽  
Hydrophilic Group ◽  
Substrate Molar Ratio

Surfactant is a molecule which has hydrophilic group and a lipophilic group which can unify a mixture consisting of water and oil. Stearamide is one kind of surfactant non-ionic which has used on any aplication. This study aims to know about optimum of temperature and time on synthesis of stearamide from stearic acid and urea with zirconium (IV) chloride in mixed solvent. This study will be observed the effect of temperature and reaction time on the synthesis of stearamide surfactant from stearic acid and urea with zirconium (IV) chloride as catalyst in mixed solvent. This research was conducted at temperature of 45°C, 55°C, 65°C, 75°C, 85°C and 95°C, reaction time of 1 hr, 2 hr, 3 hr, 4 hr, 5 hr, 6 hr, 7 hr and 8 hr, substrate molar ratio at 1:6 (w/w), solvent ratio at 2:1 (v/v), weight of catalyst 3% (%w), and stirring speed at 250 rpm. Based on this research, the optimum condition to synthesis stearamide surfactant was obtained at 85 oC and reaction time at 3 hours.

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 Optimization of Enzymatic Synthesis of Betulinic Acid Amide in Organic Solvent by Response Surface Methodology (RSM)

2019 ◽  
Vol 19 (4) ◽  
pp. 849
Author(s):  
Nurul Atikah Amin Yusof ◽  
Nursyamsyila Mat Hadzir ◽  
Siti Efliza Ashari ◽  
Nor Suhaila Mohamad Hanapi ◽  
Rossuriati Dol Hamid
Keyword(s):  
Response Surface Methodology ◽  
Reaction Time ◽  
Response Surface ◽  
Reaction Temperature ◽  
Betulinic Acid ◽  
Enzymatic Synthesis ◽  
Acid Amide ◽  
Molar Ratio ◽  
Percentage Yield ◽  
Substrate Molar Ratio

Optimization of the lipase catalyzed enzymatic synthesis of betulinic acid amide in the presence of immobilized lipase, Novozym 435 from Candida antartica as a biocatalyst was studied. Response surface methodology (RSM) and 5-level-4-factor central-composite rotatable design (CCRD) were employed to evaluate the effects of the synthesis parameters, such as reaction time (20–36 h), reaction temperature (37–45 °C), substrate molar ratio of betulinic acid to butylamine (1:1–1:3), and enzyme amounts (80–120 mg) on the percentage yield of betulinic acid amide by direct amidation reaction. The optimum conditions for synthesis were: reaction time of 28 h 33 min, reaction temperature of 42.92 °C, substrate molar ratio of 1:2.21, and enzyme amount of 97.77 mg. The percentage yield of actual experimental values obtained 65.09% which compared well with the maximum predicted value of 67.23%. The obtained amide was characterized by GC, GCMS and 13C NMR. Betulinic acid amide (BAA) showed a better cytotoxicity compared to betulinic acid as the concentration inhibited 50% of the cell growth (IC50) against MDA-MB-231 cell line (IC50 < 30 µg/mL).

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 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 Identification and Optimisation of Lipase-Catalysed Synthesis of Betulinic Acid Amide in a Solvent System

2016 ◽  
Vol 2016 ◽  
pp. 1-5
Author(s):  
Nurul Atikah Binti Amin Yusof ◽  
Nursyamsyila Mat Hadzir ◽  
Siti Efliza Ashari
Keyword(s):  
Melting Point ◽  
Betulinic Acid ◽  
Enzymatic Synthesis ◽  
Acid Amide ◽  
Enzymatic Reaction ◽  
Solvent System ◽  
Molar Ratio ◽  
Optimum Conditions ◽  
Reaction Parameters ◽  
Substrate Molar Ratio

Betulinic acid amide was synthesized from the enzymatic reaction of betulinic acid and butylamine catalysed by Novozym 435. The effects of different reaction parameters, such as effect of reaction time, reaction temperature, amount of enzyme, and substrate molar ratio (betulinic acid : butylamine), were studied and conventionally optimised. Based on this study, the enzymatic synthesis of betulinic acid amide was found to be 64.6% at the optimum conditions of 24 h, 40°C, 100 mg enzyme, and 1 : 1 substrate molar ratio in 9 : 1 mixture of chloroform and hexane as solvent. The identification of final product was carried out using TLC, melting point, and FTIR and NMR showed the presence of betulinic acid amide.

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 FOUR-FACTOR RESPONSE SURFACE OPTIMIZATION OF THE ENZYMATIC SYNTHESIS OF WAX ESTER FROM PALM KERNEL OIL

2010 ◽  
Vol 8 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Erin Ryantin Gunawan ◽  
Dedy Suhendra
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Palm Kernel ◽  
Molar Ratio ◽  
Wax Ester ◽  
Central Composite Rotatable Design ◽  
Palm Kernel Oil ◽  
Kernel Oil ◽  
Substrate Molar Ratio ◽  
Central Composite

The synthesis of wax ester using refined, bleached and deodorized (RBD) palm kernel oil (PKO) and oley alcohol catalyzed by Lipozyme IM was carried out. Response surface methodology (RSM) based on a five-level, four-factor central composite rotatable design (CCRD) was used to evaluate the interactive effects of synthesis, of reaction time (5-20 h), temperature (20-50 oC), amount of enzyme (0.1-0.2 g) and substrate molar ratio (palm kernel oil to oleyl alcohol, 1:1-1:5) on the percentage yield of wax esters. The optimum condition conditions derived via RSM were reaction time 8.46 h, temperature 44.4 oC, amount of enzyme 0.182 g, substrate molar ratio 1 to 3.7. The actual experimental yield was 92.9 % under optimum condition, which good accordance to the maximum predicted value of 92.4 %.   Keywords: response surface methodology, central composite rotatable design, palm kernel oil, lipozyme, alcoholysis, wax ester

scholarly journals Enzymatic Glycerolysis of Palm Kernel Olein and Palm Kernel Stearin in different Ratios for Monolaurin Synthesis

2021 ◽  
Vol 1192 (1) ◽  
pp. 012018
Author(s):  
N Ngatirah ◽  
C Hidayat ◽  
ES Rahayu ◽  
T Utami
Keyword(s):  
Lauric Acid ◽  
Raw Materials ◽  
Palm Kernel ◽  
Solvent System ◽  
Wave Number ◽  
Molar Ratio ◽  
Ftir Analysis ◽  
Standard Type ◽  
Palm Kernel Olein ◽  
Kernel Oil

Abstract Monolaurin is known as a monoglyceride of lauric acid, which act as an emulsifier and antimicrobial. One potential of monolaurin raw materials is palm kernel oil (PKO), which can be fractionated into palm kernel olein (PKOo) and palm kernel stearin (PKS). This study aims to determine the enzymatic glycerolysis influence of PKOo and PKS mixture in different ratios and time, on monoacylglycerol (MAG), diacylglycerol (DAG), and triacylglycerol (TAG) profiles. The Glycerolysis process of PKOo-PKS fat blends were carried out in different ratios of (60:40, 40:60, and 20:80 w/w) using commercial lipases (Lypozime RM IM) at 50°C, with an oil:glycerol molar ratio of 1:4, in a tert-butanol solvent system, between 3 to 24 hours. The results showed that the glycerolysis of PKOo and PKS in different ratios yielded varying product reactions with similar compositions (1.8-3.9% MAG, 73.2-76.4% DAG, and 20.7-24.2% TAG). A higher and not significant MAG was observed during the period of 24 hours. Also, the monolaurin was obtained at the ratio of 40:60 PKOo:PKS, within the glycerolysis time of 3 to 24 hours, at approximately 2.18±0.59% and 3.47±0.62%, respectively. The FTIR analysis also showed that the monolaurin sample was identical to the standard type, with the formation of OH group at wave number and cluster C=O ester of 3368.64 cm-1 and 1734.03 cm-1, respectively.

scholarly journals Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse

Polymers ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 1802 ◽  
Author(s):  
Yesol Baek ◽  
Jonghwa Lee ◽  
Jemin Son ◽  
Taek Lee ◽  
Abdus Sobhan ◽  
...  
Keyword(s):  
Reaction Temperature ◽  
Enzymatic Synthesis ◽  
Immobilized Enzyme ◽  
Immobilized Lipase ◽  
Enzymatic Reaction ◽  
Optimization Method ◽  
Enzyme Concentration ◽  
Novozym 435 ◽  
Molar Ratio ◽  
Optimal Conditions

Octyl formate is an important substance used in the perfume industry in products such as cosmetics, perfumes, and flavoring. Octyl formate is mostly produced by chemical catalysts. However, using enzymes as catalysts has gathered increasing interest due to their environment-friendly proprieties. In the present study, we aimed to identify the optimal conditions for the synthesis of octyl formate through immobilized enzyme-mediated esterification. We investigated the effects of enzymatic reaction parameters including the type of immobilized enzyme, enzyme concentration, molar ratio of reactants, reaction temperature, and type of solvent using the optimization method of one factor at a time (OFAT). The maximum conversion achieved was 96.51% with Novozym 435 (15 g/L), a 1:7 formic acid to octanol ratio, a reaction temperature of 40 °C, and with 1,2-dichloroethane as solvent. Moreover, we demonstrated that the Novozym 435 can be reused under the optimal conditions without affecting the octyl formate yield, which could help reduce the economic burden associated with enzymatic synthesis.

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