scholarly journals Production of biodiesel by enzymatic catalysis from the castor oil: an analytical chemical study

2020 ◽  
Vol 9 (3) ◽  
pp. 73-79
Author(s):  
Joao Carlos da Costa Assuncao

The study aimed at the development of a method for obtaining biodiesel by transesterification by via methylic from castor oil using biocatalysts. Seven varieties of lipase (PPL, Candida rugosa, OS cepacea, OS cepacea immobilized on diatomaceous earth, Novozyme 435, Lipozyme and Lipozyme RM) and seven enzymatic sources from a vegetable origin (latex of the species Ficus benjamina, Manihot glaziovii Muell. Arg., Calotropis procera, Jatropha curcas L., Ficus pumila, Euphorbia tirucalli L.) were tested. Enzymatic sources of plant origin were submitted, initially, the hydrolytic activity tests to evaluate their potential as biocatalysts and, from the results obtained, two samples were selected for the experiments further synthesis of biodiesel. Validation of the method of production of biodiesel evaluated linearity, reproducibility (precision), recovery (accuracy) and the limits of detection and quantification. Among the sources of enzymes used in the synthesis of biodiesel presented the best result was the commercial enzyme Novozym 435 with 55.33% conversion yield of biodiesel in initial tests. Were conducted new tests for optimization of reactional parameters co-solvent, alcohol: oil ratio, amount of enzyme and solvent for recovery of the enzyme, which enabled a maximum yield of biodiesel to 98.84%.

2019 ◽  
Vol 21 (24) ◽  
pp. 6658-6666 ◽  
Author(s):  
Wenjie Xue ◽  
Lei Shi ◽  
Xinqing Chen ◽  
Minghuang Qiu ◽  
Cunhui Zhou ◽  
...  

A non-noble metal (Mo) catalyst for the oligomerization of methyllinoleate via castor oil was successfully prepared to directly synthesize bio-lubricatant oil. The obtained oligomers were produced at a maximum yield of 70.8%.


2013 ◽  
Vol 291-294 ◽  
pp. 300-306 ◽  
Author(s):  
Hong Yuan ◽  
Qing Shu

Two cesium phosphotungstate-derived solid acid catalysts (Cs2.5H0.5PW12 and Cs0.5H2.5PW12) were prepared. The resulting catalysts were characterized by powder X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FTIR), N2 adsorption and desorption isotherm and temperature programmed desorption of ammonia(NH3-TPD). The Cs2.5H0.5PW12 and Cs0.5H2.5PW12 were respectively used to catalyze the tranesterification of castor oil and methanol for the synthesis of biodiesel with the assistance of microwave. Results shown microwave radiation can greatly enhance the transesterification process when compared with conventional heating method. Cs2.5H0.5PW12 showed better catalyst performance than Cs0.5H2.5PW12. A maximum yield of 90% was obtained from the using of 30:1 molar ratio of methanol to castor oil and 15 wt % mass ratio of catalyst to castor oil at 343 K under microwave radiation after 4h.


Author(s):  
V.H. Wilson ◽  
V. Yalini

Fossil fuel is getting exhausted at a fast rate and contributes to high carbon monoxide emissions. Biodiesel, being environmentally friendly, has better performance than diesel. Castor oil is an easily available vegetable oil in India. But its high viscosity leads to blockage of the fuel lines. The amount of free fatty acid more than 1% leads to soap formation which necessitates the biodiesel production in a two step process. The first step of acid catalyzed esterification process reduces the free fatty acid content of castor oil to below 1%. The second step of transesterification process converts the preheated oil to castor biodiesel. This two step process gave a maximum yield of 90%.The methyl castor oil (biodiesel) is blended with diesel in different proportions on volume basis as 15:85 (B15), 25:75 (B25), and 35:65 (B35). These blended oils are used to run a single cylinder four stroke compression ignition engine with different coatings of pistons, to study and compare the engine performance and emission characteristics at different load conditions.


2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Bhagya Sri Kaja ◽  
Stephen Lumor ◽  
Samuel Besong ◽  
Bettina Taylor ◽  
Gulnihal Ozbay

Candida rugosa lipase is a food-grade enzyme that is extensively utilized in the dairy processing industry for milk fat hydrolysis. The enzyme is mainly employed to modify the fatty acid chain length that results in the enhancement of flavors. The hydrolytic activities of C. rugosa lipase (fungal source) in its free and immobilized forms were investigated at different pH and temperature settings. The main objective of this study was to understand how different support materials (Celite-545, Sephadex G-25, and chitosan) and immobilization techniques alter lipase activity and stability. Our results indicated that hydrolytic activity increased significantly with immobilization on Celite-545. In general, immobilization resulted in considerable improvements in the stability of the enzyme with variations in pH and temperature. Immobilization on Celite-545 led to the highest catalytic efficiency. Remarkable improvements in the recovery and reusability of the immobilized lipases were noted. Comparatively, the acetone immobilization procedure resulted in higher activities than alcohol immobilization. In conclusion, the activity of C. rugosa lipase was enhanced most significantly when immobilized on Celite-545 using acetone as an adsorption solvent.


2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Nikola Milašinović ◽  
Sonja Jakovetić ◽  
Zorica Knežević-Jugović ◽  
Nedeljko Milosavljević ◽  
Marija Lučić ◽  
...  

This study reports the synthesis of polymeric matrices based onN-isopropylacrylamide and itaconic acid and its application for immobilization of lipase fromCandida rugosa. The lipase was immobilized by entrapment method. Free and immobilized lipase activities, pH and temperature optima, and storage stability were investigated. The optimum temperature for free and entrapped lipase was found to be 40 and 45°C, while the optimum pH was observed at pH 7 and 8, respectively. Both hydrolytic activity in an aqueous medium and esterolytic activity in an organic medium have been evaluated. Maximum reaction rate (Vmax) and Michaelis-Menten constants (Km) were also determined for immobilized lipase. Storage stability of lipase was increased as a result of immobilization process. Furthermore, the operational stability and reusability of the immobilized lipase in esterification reaction have been studied, and it was observed that after 10 cycles, the residual activity for entrapped lipase was as high as 50%, implying that the developed hydrogel and immobilized system could provide a promising solution for the flavor ester synthesis at the industrial scale.


Author(s):  
Vishwa Nath Verma

Calotropis (Asclepiadaceae) commonly known as “madar” is a useful medicinal plant. The two species i.e. Calotropis gigantea and Calotropis procera are to a great extent having a very similar chemical properties, but the colours of their flowers are different. The pH of latex of these two species has been found different in the present study. The temperature effects have been noticed on their pH values which is varying from 7.2 to 8.1 between the temperatures 25 °C to 45 °C and then remains constant for Calotropis gigantia. The milky latex contains hydrocarbons, fatty acids, sterols and terpenels. Seven spots have been observed on the TLC plates; out of which 3 were identified as calotoxin, uscharin and calactin. Aluminum, calcium, cadmiun, cobalt, chromium, copper, iron, magnese, magnesium, nickel, lead, and zinc metal elements were investigated in the latex and similarly in the leaves and bark from the AA spectra. The amount of magnese was found the highest in the latex of both species but calcium was found highest in leaves and bark of both species. Copper, chromium and lead were not found at all in latex but a very little amount of copper and lead were found in leaves and bark. The atomic absorption spectrophotometer was used to investigate the metals which were measured in the order of ppm.


2011 ◽  
Vol 65 (6) ◽  
pp. 667-673
Author(s):  
Nikola Milasinovic ◽  
Nedeljko Milosavljevic ◽  
Jovanka Filipovic ◽  
Zorica Knezevic-Jugovic ◽  
Melina Kalagasidis-Krusic

To overcome the problems of free enzyme application as catalysts in chemical reactions, i.e. high costs of isolation and purification processes, high sensitivity to process conditions, insufficient enzyme stability etc., a different immobilization techniques are to be used. Immobilization to/within solid support improves enzyme stability decreasing its denaturation. This paper deals with hydrogels of N-isopropylacrylamide and itaconic acid with incorporated nonionic surfactants (Triton X-100, Brij 30 and Tween 80) synthesized in distilled water at room temperature by free radical polymerization. These hydrogels were used as supports for immobilization of enzyme, lipase from Candida rugosa by post-entrapment method. The aim was to investigate the effect of the nonionic surfactants on the lipase binding capacity, as well as on its hydrolytic activity. In order to characterize the obtained hydrogels FT-IR analysis has been performed. Further, the swelling behaviour of these samples in buffer solution of pH 6.80 has been investigated. The dynamic - mechanical properties of hydrogels and detailed have been studied, too. The immobilized lipase showed somewhat reduced hydrolytic activity, as compared to the activity of free lipase as well as in comparison to the lipase immobilized to the reference sample (sample synthesized under the same polymerization conditions, but in the absence of surfactants). It was concluded that the addition of surfactants increased the hydrogel mesh size. The surfactant addition did not affect the dynamic - mechanical properties of the investigated hydrogels. The largest percentage of specific activity and yield of activity were presented by the reference sample, too. It is obvious that the absence of surfactants charged groups has no influence on the lipase binding capacity, and the obtained activity yields are to be expected.


2020 ◽  
Vol 6 (4) ◽  
pp. 0498-0504
Author(s):  
Otávio Domingues ◽  
Letícia Karen dos Santos ◽  
Rondinelli Donizetti Herculano ◽  
Danilo Luiz Flumignan ◽  
Ariela Veloso de Paula

Currently, the use of magnetic nanoparticles has aroused interest in industrial processes, and the combination of their properties with the immobilization of lipases has been developed in order to produce carriers of easy separation of the reaction medium. In this context, the objective of the present study was to immobilize Candida rugosa lipase in magnetic nanoparticles, such as magnetite and maghemite, by physical adsorption and covalent bonding. The biocatalysts were evaluated by infrared spectroscopy (FTIR) and hydrolytic activity analysis. Thus, from the analyses performed, the best biocatalyst obtained was the immobilized by covalent bond in maghemite, presenting a hydrolytic activity of 174.67 U/g.


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