Agroindustrial Wastes as a Support for the Immobilization of Lipase from Thermomyces lanuginosus: Synthesis of Hexyl Laurate

Lira, Regiane Késsias de Sousa; Zardini, Rochele T.; Carvalho, Marcela C. C. de; Wojcieszak, Robert; Leite, Selma Gomes Ferreira; Itabaiana, Ivaldo

doi:10.3390/biom11030445

Cited by 15 publications

(2 citation statements)

References 62 publications

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“…by using cross-linking on the magnetic particles as a support and found that it has applications in the synthesis of 2-phenylethyl butanoate (fragrance compound and flavor). Lira et al (2021) also immobilized the lipase of Thermomyces lanuginosus on agro-industrial wastes as a support and found that it has applications in the production of hexyl laurate.…”

Section: Immobilization Of Fungal Lipasementioning

confidence: 99%

Industrial applications of fungal lipases: a review

Kumar¹,

Verma²,

Dubey³

et al. 2023

Front. Microbiol.

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Fungal lipases (triacylglycerol acyl hydrolases EC 3.1.1.3) are significant industrial enzymes and have several applications in a number of industries and fields. Fungal lipases are found in several species of fungi and yeast. These enzymes are carboxylic acid esterases, categorized under the serine hydrolase family, and do not require any cofactor during the catalyzing of the reactions. It was also noticed that processes including the extraction and purification of lipases from fungi are comparatively easier and cheaper than other sources of lipases. In addition, fungal lipases have been classified into three chief classes, namely, GX, GGGX, and Y. Fungal lipases have applications not only in the hydrolysis of fats and oils (triglycerides) but are also involved in synthetic reactions such as esterification, acidolysis, alcoholysis, interesterification, and aminolysis. The production and activity of fungal lipases are highly affected by the carbon source, nitrogen source, temperature, pH, metal ions, surfactants, and moisture content. Therefore, fungal lipases have several industrial and biotechnological applications in many fields such as biodiesel production, ester synthesis, production of biodegradable biopolymers, formulations of cosmetics and personal care products, detergent manufacturing, degreasing of leather, pulp and paper production, textile industry, biosensor development, and drug formulations and as a diagnostic tool in the medical sector, biodegradation of esters, and bioremediation of wastewater. The immobilization of fungal lipases onto different carriers also helps in improving the catalytic activities and efficiencies of lipases by increasing thermal and ionic stability (in organic solvents, high pH, and temperature), being easy to recycle, and inducing the volume-specific loading of the enzyme onto the support, and thus, these features have proved to be appropriate for use as biocatalysts in different sectors.

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Section: Immobilization Of Fungal Lipasementioning

confidence: 99%

Industrial applications of fungal lipases: a review

Kumar¹,

Verma²,

Dubey³

et al. 2023

Front. Microbiol.

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“…Various value‐added materials can be produced from agricultural residues, such as industrially important enzymes (Ravindran et al, 2018). An alternative for this biomass is their use as a carrier for the immobilization of enzymes and cells (Bilal et al, 2017; Bilal & Iqbal, 2019; Dutta & Wu, 2014; Girelli et al, 2020; Li et al, 2019; Lira et al, 2021; Rodríguez‐Restrepo & Orrego, 2020). The lignocellulosic materials fulfill the specific properties (inertness, physical strength, stability, renewability, and low cost) of a support on which a biocatalyst can be fixed (Rodríguez‐Restrepo & Orrego, 2020).…”

Section: Agricultural Residual Biomass Utilizationmentioning

confidence: 99%

Immobilizing white‐rot fungi laccase: Toward bio‐derived supports as a circular economy approach in organochlorine removal

Serbent,

Magario,

Saux

2023

Biotech & Bioengineering

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Despite their high persistence in the environment, organochlorines (OC) are widely used in the pharmaceutical industry, in plastics, and in the manufacture of pesticides, among other applications. These compounds and the byproducts of their decomposition deserve attention and efficient proposals for their treatment. Among sustainable alternatives, the use of ligninolytic enzymes (LEs) from fungi stands out, as these molecules can catalyze the transformation of a wide range of pollutants. Among LEs, laccases (Lac) are known for their efficiency as biocatalysts in the conversion of organic pollutants. Their application in biotechnological processes is possible, but the enzymes are often unstable and difficult to recover after use, driving up costs. Immobilization of enzymes on a matrix (support or solid carrier) allows recovery and stabilization of this catalytic capacity. Agricultural residual biomass is a passive environmental asset. Although underestimated and still treated as an undesirable component, residual biomass can be used as a low‐cost adsorbent and as a support for the immobilization of enzymes. In this review, the adsorption capacity and immobilization of fungal Lac on supports made from residual biomass, including compounds such as biochar, for the removal of OC compounds are analyzed and compared with the use of synthetic supports. A qualitative and quantitative comparison of the reported results was made. In this context, the use of peanut shells is highlighted in view of the increasing peanut production worldwide. The linkage of methods with circular economy approaches that can be applied in practice is discussed.

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Continuous Flow Synthesis of Hexyl Laurate Using Immobilized Thermomyces Lanuginosus Lipase from Residual Babassu Mesocarp

de S. Lira,

do Nascimento,

Lima

et al. 2024

ChemPlusChem

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This work applied BM as support for immobilization of lipase TLL in packed‐bed reactor and its application for the synthesis of hexyl laurate. Initially, the percolation of a solution containing 5 mg of TLL at 25 oC generated an immobilized derivative with hydrolytic activity of 504.7 U/g and 31.7% of recovered activity. Subsequent treatment with n‐hexane, as well as the effect of temperature on the immobilization process were able to improve the activities of the final BM‐TLLF, achieving a hydrolysis activity of 7023 U/g and esterification activity of 430 U/g against 142 U/g and 113.5 U/g respectively presented by commercial TLIM. Desorption studies showed that the TL IM has 18 mg of protein per gram of support, compared to 4.92 mg presented by BM‐TLL. Both biocatalysts were applied to synthesize hexyl laurate, achieving 98% conversion at 40°C within a residence time of 2 hours. Notably, BM‐TLLF displayed exceptional recyclability, maintaining catalytic efficiency over 12 cycles. This reflects a productivity of 180 mg of product/h/U of the enzyme, surpassing 46 mg/h/U obtained for TLIM. These results demonstrate the efficacy of continuous flow technology in creating a competitive and integrated process offering an exciting alternative for the valorization of residual lignocellulosic biomass.

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Agroindustrial Wastes as a Support for the Immobilization of Lipase from Thermomyces lanuginosus: Synthesis of Hexyl Laurate

Cited by 15 publications

References 62 publications

Industrial applications of fungal lipases: a review

Industrial applications of fungal lipases: a review

Immobilizing white‐rot fungi laccase: Toward bio‐derived supports as a circular economy approach in organochlorine removal

Continuous Flow Synthesis of Hexyl Laurate Using Immobilized Thermomyces Lanuginosus Lipase from Residual Babassu Mesocarp

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