Solvent condition in triolein hydrolysis by Rhizopus delemar lipase using an AOT reverse micellar system

Naoe, Kazumitsu; Awatsu, S.; Yamada, Yuka; Kawagoe, Mikio; Nagayama, Kazuhito; Imai, Masanao

doi:10.1016/j.bej.2003.10.001

Cited by 18 publications

(9 citation statements)

References 29 publications

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“…The extraction of protein using reverse micellar organic solvents is suitable for practical application on a large-scale and continuous processing because it corresponds to a liquid-liquid extraction [5,6]. It has been reported that several significant operating parameters govern the enzyme reaction in reverse micelles, such as water content [7][8][9][10][11], organic solvent [1,12,13], surfactant concentration [7,10,11,14] and cosurfactant concentration [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system

Naoe

Takeuchi

Kawagoe

et al. 2007

Journal of Chromatography B

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Section: Introductionmentioning

confidence: 99%

Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system

Naoe

Takeuchi

Kawagoe

et al. 2007

Journal of Chromatography B

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“…Reverse micellar systems used for enzymatic oil hydrolysis consist of small water droplets containing the enzyme and surrounded by surfactant molecules, which are dispersed in an oil-rich continuous phase containing the substrate. According to previous studies, , the best reaction conditions were obtained using AOT as the surfactant and iso -octane as the solvent. Consequently, this system was chosen to carry out the hydrolysis experiments.…”

Section: Experimental Sectionmentioning

confidence: 99%

Waste Frying Oil Hydrolysis in a Reverse Micellar System

Moya-Ramírez

García-Román

Fernández-Arteaga

2016

ACS Sustainable Chem. Eng.

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In this work we explore the feasibility of using reverse micelles to carry out the enzymatic hydrolysis of waste frying oils (WFO). The effect of some relevant parameters, such as the water/surfactant molar ratio (W 0), the oil volume fraction in the organic phase, and the enzyme concentration was studied. As a preliminary result, we observed that the extent of the reverse micellar system was slightly higher in mixtures containing WFO than when prepared with virgin oil. The hydrolysis extent was found to strongly depend on the amount of water inside the micelles, and an optimum value of 13.3 was found for W 0. Although the hydrolysis took place for every volume fraction of oil in the organic phase, the reaction conversion was limited at high oil fractions. A maximum hydrolysis extent was found at high enzyme concentrations, but the specific activity of the enzyme was much higher at low enzyme concentrations. An analysis of the product distribution showed that free fatty acids are the main hydrolysis products. These results provide an alternative route for the transformation of WFO into high added-value products, which could help to reduce the environmental impact of these wastes.

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“…These results are partially in agreement with the concept that asserts that the effect of organic solvents on enzyme activity depends on their polarity. Polar organic solvents interact with the aqueous environment and thus remove the water molecules involved in the enzyme's structure, which leads to destruction of dehydrated enzyme . Furthermore, according to previous studies, organic solvents with a lower dielectric constant than water increase the strength of hydrophobic interactions, which is indispensible for preservation of the protein tertiary structure .…”

Section: Experimental Studiesmentioning

confidence: 99%

Study of the effect of F17A mutation on characteristics of Bacillus thermocatenulatus lipase expressed in Pichia pastoris using in silico and experimental methods

Karimi

Karkhane

Yakhchali

et al. 2014

Biotech and App Biochem

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Bacillus thermocatenulatus lipase 2 (BTL2), a thermoalkalophilic lipase, is the best studied enzyme for its particular properties, which make it useful in different industries. Displacement of conserved phenylalanine 17 (Phe-17) residue in the active site of BTL2 has a critical role in oxyanion hole formation, which is important for enzyme activity. In this study, to facilitate oxyanion hole formation, Phe-17 was substituted with Alanine residue (F17A). The best structures of the opened form of the native and mutated lipases were garnered based on the crystal structures of 2W22. To evaluate catalytic activity, both lipases were docked to a set of ligands using Hex 6.3 software. Following in silico study, both native and mutant btl2 genes were cloned and expressed in Pichia pastoris. Based on the results obtained, the mutation increased lipase lipolytic activity against most of the applied substrates, especially for tributyrin and tricaprylin, by 1.9 and 2.15 fold, respectively. However, optimum temperature and pH were the same for both lipases (60 °C and pH 8.0). As previously reported, it is believed that F17A mutation simplifies oxyanion hole formation and declines steric hindrance in the enzyme active site, which might ultimately lead to more efficient accessibility of substrates.

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Solvent condition in triolein hydrolysis by Rhizopus delemar lipase using an AOT reverse micellar system

Cited by 18 publications

References 29 publications

Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system

Higher order structure of Mucor miehei lipase and micelle size in cetyltrimethylammonium bromide reverse micellar system

Waste Frying Oil Hydrolysis in a Reverse Micellar System

Study of the effect of F17A mutation on characteristics of Bacillus thermocatenulatus lipase expressed in Pichia pastoris using in silico and experimental methods

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