Enzymatic synthesis of biolubricants from by-product of soybean oil processing catalyzed by different biocatalysts of Candida rugosa lipase

Fernandes, Keysson Vieira; Cavalcanti, Elisa D.C.; Cipolatti, Eliane Pereira; Aguieiras, Érika C.G.; Pinto, Maria do Carmo F. R.; Tavares, Felipe Mattos; Silva, Priscila R. da; Fernández-Lafuente, Roberto; Arana-Peña, Sara; Pinto, José Carlos; Assunção, Charles Lima Bessa; Silva, José André C. da; Freire, Denise Maria Guimarães

doi:10.1016/j.cattod.2020.03.060

Cited by 42 publications

(15 citation statements)

References 35 publications

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“…The immobilization yield was 100%, since the immobilization procedure was performed in organic solvent medium without free water due to the high hydrophobicity of AMP (Cesarini et al, 2014). This reduces the interaction of the aqueous phase containing the enzyme with the support, thus, immobilization in organic medium was chosen, a method that has been used by several other researchers (Bento et al, 2017;Silva et al, 2018;Da Silva et al, 2020). Complete immobilization was confirmed by method of the Bradford et al (1976).…”

Section: Obtaining the Crl-ampmentioning

confidence: 99%

“…Accurel MP 1000 (AMP) is a hydrophobic and macroporous polypropylene polymer (Cesarini et al, 2014) widely used as a support in the immobilization of lipases (Baron et al, 2011;Scherer et al, 2011;Cunha et al, 2013;Alnoch et al, 2015;Madalozzo et al, 2015;Manoel et al, 2015). Lipases immobilized on AMP are used for several purposes, such as catalysis in synthesis of biodiesel esters (Madalozzo et al, 2015;De Menezes et al, 2021), pharmacological derivatives, such as myo-inositol, a supplement that helps in hormonal disorders and fertility (Manoel et al, 2016), and catalysis of biolubricating esters from vegetable oil by-products (Fernandes et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

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Candida Rugosa Lipase Immobilized on Hydrophobic Support Accurel MP 1000 in the Synthesis of Emollient Esters

Menezes

Santo

Santos

et al. 2021

Preprint

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In the present work, Candida rugosa lipase (CRL) was immobilized by physical adsorption in organic medium on Accurel MP 1000 (AMP) with a protein load of 6.5 mg g-1 (mg protein/g support). CRL-AMP was applied with 5 and 10% of catalyst/volume of medium (m v-1) in esterification reactions of stearic acid with lauryl and cetyl alcohols producing the wax esters such as dodecanoyl octadecanoate 1 and hexadecanoyl octadecanoate 2 in a heptane medium. Six reaction cycles were studied to evaluate the stability and recyclability of the prepared biocatalyst. The specific activity (Asp) for CRL-AMP was 200 ± 20 U mg-1. Its catalytic activity was 1300 ± 100 U g-1. CRL-AMP was used in the synthesis of esters in heptane medium with a 1:1 acid:alcohol molar ratio at 45°C and 200 rpm. In synthesis 1, conversion was 62.5 ± 3.9% in 30 min at 10% m v-1 and 56.9 ± 2.8% in 54 min at 5% m v-1, while in synthesis 2, conversion was 79.0 ± 3.9% in 24 min at 10% m v-1, and 46.0 ± 2.4% in 54 min at 5% m v-1. Reuse tests after 6 consecutive cycles of reaction showed that the biocatalyst retained approximately 50% of its original activity for both reaction systems. CRL-AMP showed a high potential in the production of wax esters, since it started from low enzymatic load and high specific activities and conversions were obtained, in addition to allowing an increase in stability and recyclability of the prepared biocatalyst.

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Section: Obtaining the Crl-ampmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Candida Rugosa Lipase Immobilized on Hydrophobic Support Accurel MP 1000 in the Synthesis of Emollient Esters

Menezes

Santo

Santos

et al. 2021

Preprint

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“…They belong to the class of hydrolases (EC 3.1.1.1) and their natural function is the hydrolysis of triglycerides to fatty acids and glycerol. Nevertheless, under non-aqueous conditions, lipases are able to catalyze a broad range of reactions such as esterification, transesterification, and interesterification or acidolysis [165][166][167][168][169][170][171][172][173][174][175][176][177]. Moreover, besides this broad range of reactions, lipases are able to recognize a vast diversity of substrates, being able to catalyze even promiscuous reactions [178,179].…”

Section: Lipases As Industrial Biocatalystsmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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Section: Introductionmentioning

confidence: 99%

Candida rugosa lipase immobilized on hydrophobic support Accurel MP 1000 in the synthesis of emollient esters

et al. 2021

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Enzymatic synthesis of biolubricants from by-product of soybean oil processing catalyzed by different biocatalysts of Candida rugosa lipase

Cited by 42 publications

References 35 publications

Candida Rugosa Lipase Immobilized on Hydrophobic Support Accurel MP 1000 in the Synthesis of Emollient Esters

Candida Rugosa Lipase Immobilized on Hydrophobic Support Accurel MP 1000 in the Synthesis of Emollient Esters

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

Candida rugosa lipase immobilized on hydrophobic support Accurel MP 1000 in the synthesis of emollient esters

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