Heterogeneous biocatalytic processes of vegetable oil interesterification to biodiesel

Коваленко, Г. А.; Perminova, L. V.; Беклемишев, А. Б.; Yakovleva, E. Yu.; Pykhtina, M. B.

doi:10.1134/s2070050415010109

Cited by 16 publications

(5 citation statements)

References 41 publications

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“…2). It is known that ethanol can inactivate various enzymes, including immobilized rPichia/lip [29]. Since the hydrophobicity of the original MCA in the presence of ethanol significantly decreased due to adsorption of ethanol molecules on CNTs, this adsorbent was apparently capable of exhibiting a protective effect by reducing the local concentration of C 2 H 5 OH in the lipase microenvironment.…”

Section: Resultsmentioning

confidence: 99%

Modulation of the Catalytic Properties of Immobilized Recombinant Lipase from Thermomyces lanuginosus in the Reaction of Esterification by the Selection of an Adsorbent

Коваленко

Perminova²,

Беклемишев³

et al. 2022

Appl Biochem Microbiol

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Biocatalysts with lipase activity (BLAs) were prepared by adsorptive immobilization of recombinant lipase (rPichia/lip) from thermophilic microscopic fungi Thermomyces lanuginosus produced by a genetically engineered strain of methylotrophic yeast Komagataella phafii (Pichia pastoris). Supports with different physicochemical properties were used as adsorbents: mesoporous hydrophilic silica (SiO2) and macroporous hydrophobic carbon aerogel (MCA). The enzymatic activity, substrate specificity and operational stability of BLAs were studied in the esterification of saturated fatty acids with aliphatic alcohols differing in the number of carbon atoms in the molecule from 2 to 18. Matrices of relative activities were compiled for more than 60 pairs of substrates, an acid and an alcohol, by comparing the reaction rates of the esterification under identical conditions, which allowed us to reveal differences in the specificity of adsorbed lipase depending on the chemical nature of the support. It was found that for both types of biocatalysts, rPichia/lip on SiO2 (PLSi) and rPichia/lip on MCA (PLC), the maximum reaction rate was observed under esterification of heptanoic acid (C7) with butyl alcohol (C4). Under the same conditions of the synthesis of esters (20 ± 2°C, 1 bar, a mixture of hexane and diethyl ether as an organic solvent), including the synthesis of butylheptanoate, rPichia/lip adsorbed on silica showed an order of magnitude lower activity than lipase adsorbed on carbon aerogel. The catalytic constants, equal to 3.7 s–1 and 1.1 × 102 s–1, respectively, differed by 30 times. It was found that esters of short chain fatty acids C4–C7 and ethyl alcohol C2 were synthesized 2–3 times faster using the hydrophobic PLC type than using the hydrophilic PLSi type of BLAs. At the same time, esters of high-molecular-weight acids С9, C10, С18 and alcohols С8–С16 with pronounced hydrophobicity were synthesized 1.5–2 times faster using of PLSi type BLAs. The operational stability of the biocatalysts was quite high: the prepared BLAs retained 82–99% of their initial activity after more than 30 reaction cycles, while the duration of each cycle to reach an acid conversion above 85% was several hours (4–6 h).

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Section: Resultsmentioning

confidence: 99%

Modulation of the Catalytic Properties of Immobilized Recombinant Lipase from Thermomyces lanuginosus in the Reaction of Esterification by the Selection of an Adsorbent

Коваленко

Perminova²,

Беклемишев³

et al. 2022

Appl Biochem Microbiol

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“…In reaction (III), the reaction medium consisted of 0.1 mol/L vegetable (sunflower or linseed) oil, 1.85 mol/L methyl acetate or dimethyl carbonate or 2.3 mol/L ethyl acetate, and a solvent (hexane). Transesterification products were identified by thin layer chromatography (TLC), as was described in our earlier publication [27]. The tributyrin hydrolysis and ester synthesis rates were determined by acid-base titration from the increase and decrease in the concentration of butyric acid and capric acid, respectively.…”

Section: Methodsmentioning

confidence: 99%

“…6a). Earlier [27,28], we demon strated that one of the causes of the inactivation of bio catalysts in reactions involving "oil" substrates is the dehydration of adsorbed lipase as a result of triglycer ides displacing "essential" water molecules from the microenvironment of the enzyme. For verifying this hypothetical inactivation mechanism, the biocatalysts were also examined in an esterification reaction, whose product is water.…”

Section: Preparation Of Lipase Active Biocatalystsmentioning

confidence: 99%

Synthesis of nanostructured carbon on Ni catalysts supported on mesoporous silica, preparation of carbon-containing adsorbents, and preparation and study of lipase-active biocatalysts

et al. 2016

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This work continues a series of our studies on the synthesis of nanostructured carbon (NSC) by the pyrolysis of H 2 + C 3 -C 4 alkane mixtures on nickel and cobalt metal catalysts supported on chemically diverse inorganic materials (aluminosilicates, alumina, carbon) having different textural characteristics (mesoporous and macroporous supports) and shapes (granules, foamed materials, and honeycomb mono liths). Here, we consider Ni catalysts supported on granular mesoporous silica (SiO 2 ). It has been elucidated how the yield of synthesized carbon depends on the Ni/SiO 2 catalyst preparation method (homogeneous pre cipitation or impregnation) and on the composition of the impregnating solution, including the molar ratio of its components-nickel nitrate and urea. The morphology of catalytic NSC and Ni distribution in the sil ica granule have been investigated using a scanning electron microscope with an EDX analyzer. Carbon con taining composite supports (NSC/SiO 2 ) have been employed as adsorbents for immobilizing microbial lipase. The enzymatic activity and stability of the resulting biocatalysts have been estimated in transesterifi cation reactions of vegetable (sunflower and linseed) oils involving methyl or ethyl acetate, esterification, and synthesis of capric acid-isoamyl alcohol esters in nonaqueous media.

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“…Below is authors' report of the most effective rE. coli/lip lysate-based biocatalysts prepared and studied in the following reactions: (1) hydrolysis of tributyrin [16,19]; (2) interesterification of oil-fat blends [16,19,36,40]; (3) interesterification of sun flower oil with ethyl acetate [40,41]; (4) esterification of fatty acid with aliphatic alcohols [36,42]. It was found that the rates of reactions were considerably in more than 500 times higher in aqueous buffered media (hydrolysis) than in anhydrous organic solvents (esterification).…”

Section: Lipase-active Biocatalystmentioning

confidence: 99%

“…The interesterification of vegetable oil with methyl-or ethyl acetate was carried out in periodic mode in a stirred-tank reactor on a shaker at 120-150 rpm and 40 • C. The reaction medium had the following composition: 0.1 M oil, 2.3-2.5 M ethyl acetate, solvent-n-hexane. Depending on the activity of the prepared biocatalyst, the duration of one reaction cycle ranged from 5 to 144 h. The products-ethyl esters of fatty acids-were analyzed using gas (GC) and thin-layer chromatography (TLC) under the conditions described elsewhere [41].…”

Section: Interesterification Of Vegetable Oil With Ethyl Acetatementioning

confidence: 99%

Heterogeneous Biocatalysts Prepared by Immuring Enzymatic Active Components inside Silica Xerogel and Nanocarbons-In-Silica Composites

et al. 2018

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Proprietary results on preparation and studies of whole-cell and lysates-based heterogeneous biocatalysts with different enzymatic activity were reviewed. A peculiar method was developed for preparing these biocatalysts by immuring (entrapping) enzymatic active components (EAC) inside silica (SiO 2) xerogel and nanocarbons-in-silica composites. Properties of the multi-component composite biocatalysts such as enzymatic activity and operational stability were compared. The effect of the inclusion of nanocarbons such as nanotubes, nanofibers, and onion-like nanospheres with various texture, nanostructure and dispersion were thoroughly studied. With invertase-active biocatalysts, the direct correlation between an increase in the enzymatic activity of the nanocarbons-in-silica biocatalyst and efficiency of EAC adhesion on nanocarbons was observed. The steady-state invertase activity of the baker yeast lysates-based biocatalysts was determined to increase by a factor of 5-6 after inclusion of the multi-walled carbon nanotubes inside SiO 2-xerogel. With lipase-active biocatalysts, the effect of the included nanocarbons on the biocatalytic properties depended significantly on the reaction type. In interesterification of oil-fat blends, the biocatalysts without any included nanocarbons demonstrated the maximal lipase activity. In esterification of fatty acids with aliphatic alcohols, the activity of the biocatalysts increased by a factor of 1.5-2 after inclusion of the aggregated multi-walled carbon nanotubes (CNTs) inside SiO 2-xerogel. In the low-temperature synthesis of isopentyl esters of butyric (C4:0), capric (C10:0), and srearic (C18:0) fatty acids, the lipase-active composite CNTs-in-silica biocatalysts operated without loss of activity for more than thousand hours.

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Heterogeneous biocatalytic processes of vegetable oil interesterification to biodiesel

Cited by 16 publications

References 41 publications

Modulation of the Catalytic Properties of Immobilized Recombinant Lipase from Thermomyces lanuginosus in the Reaction of Esterification by the Selection of an Adsorbent

Modulation of the Catalytic Properties of Immobilized Recombinant Lipase from Thermomyces lanuginosus in the Reaction of Esterification by the Selection of an Adsorbent

Synthesis of nanostructured carbon on Ni catalysts supported on mesoporous silica, preparation of carbon-containing adsorbents, and preparation and study of lipase-active biocatalysts

Heterogeneous Biocatalysts Prepared by Immuring Enzymatic Active Components inside Silica Xerogel and Nanocarbons-In-Silica Composites

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