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.

Esterification of Oleic Acid and Bioalcohols Using Immobilized Lipase

2013 ◽  
Vol 724-725 ◽  
pp. 1154-1157 ◽  
Author(s):  
Sawittree Mulalee ◽  
Jiranan Chanprasert ◽  
Piboon Kerdpoksup ◽  
Netnapa Sawangpanya Sawangpanya ◽  
Muenduen K.M. Phisalaphong
Keyword(s):  
Oleic Acid ◽  
Fatty Acid ◽  
Immobilized Lipase ◽  
Biodiesel Production ◽  
Novozym 435 ◽  
Molar Ratio ◽  
Optimal Conditions ◽  
Free System ◽  
Solvent Free System ◽  
Significant Attention

Biodiesel has been receiving significant attention as a renewable and nonpolluting fuel. In this study, oleic acid and bioalcohols (ethanol and butanol) were used as substrates for biodiesel production. The reactions were performed in a solvent-free system using immobilized lipase (Novozym 435) as biocatalyst in a batch esterification process. The optimal conditions were 45°C, oleic acid to alcohol molar ratio of 1:2, Novozym 435 loading at 5% based on oleic acid weight and 250 rpm, in which the free fatty acid (FFA) conversion at 91.0% was obtained after 12 hours of the reaction.

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 Lipase-catalyzed transesterification of rendering plant fat – Short Communication

2010 ◽  
Vol 56 (No. 3) ◽  
pp. 122-125 ◽  
Author(s):  
A. Prošková ◽  
Z. Kopicová ◽  
J. Kučera ◽  
L. Škarková
Keyword(s):  
Short Communication ◽  
Immobilized Enzyme ◽  
Immobilized Lipase ◽  
Covalent Bond ◽  
Novozym 435 ◽  
Optimum Temperature ◽  
Optimum Conditions ◽  
Soluble Lipase ◽  
Good Accordance ◽  
Higher Temperature

Soluble lipase (Lipozyme CALB L) was immobilized by covalent bond to chitosan pellets prepared from Aspergillus niger mycelium. This immobilized enzyme was compared with commercial immobilized lipase of the same origin (Novozym 435). Novozym 435 is also lipase CALB L commercially immobilized by sorption on poly-(methyl acrylate). Novozym 435 shows much higher conversion of rendering plant fat in methanol under optimum conditions, having, at the same time, lower optimum temperature and lower stability at higher temperature. Lipozyme CALB L immobilized on chitosan leads to a low conversion, regardless its higher thermal stability. Novozym 435 gives conversion of about 50% of theoretical value, which is in good accordance with basically catalyzed transesterification of rendering plant fat described elsewhere. Lipozyme CALB L immobilized on chitosan gives conversion of about 10% of theoretical value only. The use of Novozym 435 in two-step system (enzyme-acid) seems to be more convenient compared with traditional two-step system (base-acid)

Studies on the Immobilized-Lipase-Catalyzed Esterification of Alkyl Oleates in Solvent-Free Systems

2013 ◽  
Vol 645 ◽  
pp. 19-23 ◽  
Author(s):  
Hui Zhong ◽  
Zheng Fang ◽  
Bao Hua Zou ◽  
Xin Li ◽  
Kai Guo
Keyword(s):  
Oleic Acid ◽  
Low Temperature ◽  
High Selectivity ◽  
Immobilized Lipase ◽  
Enzyme Concentration ◽  
Molar Ratio ◽  
High Yield ◽  
Secondary Alcohols ◽  
Tertiary Alcohols ◽  
Candida Sp

The esterification of oleic acid with alkyl alcohols in solv ent-free systems was catalyzed by an immobilized lipase from Candida sp . 99-125. The influence of several factors, including enzyme concentration, temperature, molar ratio between oleic acid and alkyl alcohols, and structure of alcohol was also investigated. The results indicated that the reactions catalyzed by lipase at 20 o C, in the presence of 3% (w/w) lipase, on the molar ratio of 1:1 between oleic acid and alcohols, afforded products in high yield. It showed high selectivity to primary and low selectivity to secondary alcohols and tertiary alcohols because of the sterically hindered effect. Methanol has certain toxicity on the activity of the lipase. 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.

Study on Synthesis of Nitrophenyl Isocyanates Using Triphosgene

2012 ◽  
Vol 550-553 ◽  
pp. 1039-1042 ◽  
Author(s):  
Gui Rong Cao ◽  
Xue Yan Zhao ◽  
Rui Jie Xiao
Keyword(s):  
Reaction Time ◽  
Reaction Temperature ◽  
Molar Ratio ◽  
Optimal Conditions ◽  
Optimum Reaction

In this paper, triphosgene respectively reacting with o-nitrophenyl aniline, m-nitrophenyl aniline and p-nitrophenyl aniline to synthesize corresponding isocyanates. The effects of reactants molar ratio, reaction time and reaction temperature on the yield were investigated. As a result, using 1,2-dichloroethane as reaction solvent, the optimum molar ratio of the three kinds of nitroaniline and triphosgene were all 2.5:1, the optimum reaction time of synthesis of o-nitrophenyl isocyanate, m-nitrophenyl isocyanate and p-nitrophenyl isocyanate respectively was 6h, 5.5h and 5h; the optimum reaction temperature of synthesis of the three kinds of nitrophenyl isocyanates were all 75°C. Under the optimal conditions, the yield of o-nitrophenyl isocyanate, m-nitrophenyl isocyanate and p-nitrophenyl isocyanate could respectively be 80.3%, 83.7% and 83.5%. The products were characterized by meltingtest, ebulliometry, IR, and HPLC

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 Statistical Optimization of Biodiesel Production from Salmon Oil via Enzymatic Transesterification: Investigation of the Effects of Various Operational Parameters

Processes ◽  
2021 ◽  
Vol 9 (4) ◽  
pp. 700
Author(s):  
Vegneshwaran V. Ramakrishnan ◽  
Deepika Dave ◽  
Yi Liu ◽  
Winny Routray ◽  
Wade Murphy
Keyword(s):  
Atlantic Salmon ◽  
Immobilized Lipase ◽  
Enzyme Concentration ◽  
Biodiesel Production ◽  
Molar Ratio ◽  
Operational Parameters ◽  
Enzymatic Transesterification ◽  
Optimum Parameters ◽  
Response Surface Modelling ◽  
The Relationship

The enzymatic transesterification of Atlantic salmon (Salmo salar) oil was carried out using Novozym 435 (immobilized lipase from Candida antartica) to produce biodiesel. A response surface modelling design was performed to investigate the relationship between biodiesel yield and several critical factors, including enzyme concentration (5, 10, or 15%), temperature (40, 45, or 50 °C), oil/alcohol molar ratio (1:3, 1:4, or 1:5) and time (8, 16, or 24 h). The results indicated that the effects of all the factors were statistically significant at p-values of 0.000 for biodiesel production. The optimum parameters for biodiesel production were determined as 10% enzyme concentration, 45 °C, 16 h, and 1:4 oil/alcohol molar ratio, leading to a biodiesel yield of 87.23%. The step-wise addition of methanol during the enzymatic transesterification further increased the biodiesel yield to 94.5%. This is the first study that focused on Atlantic salmon oil-derived biodiesel production, which creates a paradigm for valorization of Atlantic salmon by-products that would also reduce the consumption and demand of plant oils derived from crops and vegetables.

Lipase-Catalyzed Synthesis of Caffeic Acid Propyl Ester in Ionic Liquid

2013 ◽  
Vol 634-638 ◽  
pp. 555-558 ◽  
Author(s):  
Na Pang ◽  
Fang Qin Wang ◽  
Hong Sheng Cui ◽  
Xing Yu Zhao ◽  
Xi Liu ◽  
...  
Keyword(s):  
Ionic Liquid ◽  
Caffeic Acid ◽  
Reaction Temperature ◽  
Immobilized Lipase ◽  
Reaction Medium ◽  
Molar Ratio ◽  
Mass Ratio ◽  
Propyl Ester ◽  
Synthesis Properties ◽  
Reaction Media

Lipase-catalyzed esterification of caffeic acid with 1-propanol, to form caffeic acid propyl ester (CAPE), was investigated in ionic liquid using immobilized lipase. Ten ILs were used as the reaction medium; three types of lipases were selected as biocatalysts, and the lipase-catalyzed synthesis properties of CAPE were measured systematically in order to enhance the yield of CAPE. The results indicated that when [Bmim][Tf2N] was selected as reaction media, Novozym 435 was used as catalyst, the molar ratio of 1-propanol to CA was 10:1, the reaction temperature was 80 °C, and the mass ratio of catalyst to CA was 18:1, the highst yield of CAPE attained 41.0 %.

Enzymatic Esterification of Oleic Acid and Propanol by Novozym 435

2014 ◽  
Vol 705 ◽  
pp. 29-33 ◽  
Author(s):  
Sawittree Mulalee ◽  
Karnjana Sena ◽  
Muenduen Phisalaphong
Keyword(s):  
Oleic Acid ◽  
Molecular Sieve ◽  
Rotation Speed ◽  
Novozym 435 ◽  
Molar Ratio ◽  
Enzymatic Esterification ◽  
Optimal Conditions ◽  
External Mass Transfer ◽  
Initial Value ◽  
Optimal Rotation

Recently, demand of biolubricants has been continuously increased since it is environmentally friendly and renewable. Therefore, this research focused on the biolubricants production from enzymatic esterification of oleic acid and propanol using Novozym 435 as a biocatalyst. The esterification experiments were conducted under the optimal conditions, as follows: 45°C, oleic acid to propanol molar ratio of 1:2, Novozym 435 loading of 5% based on the weight of oleic acid. It was shown that the optimal rotation speed at 250 rpm could minimize the effect of external mass transfer limitations and maintained the enzyme activity. The conversion of oleic acid from the esterification for 6 h with isopropanol was 76.4%, which was lower than that with n-propanol (88.9%). Novozym 435 could be reused in the production of propyloleate for at least 5 cycles with maintaining FFA conversion of 94% of its initial value. Moreover, the use of molecular sieve to remove water during the reaction could significantly enhance the final FFA conversion from 88.9% to 94.7%.

Sign in / Sign up

Export Citation Format

Share Document