Computational and experimental analysis on the preferential selectivity of lipases for triglycerides in Licuri oil

Rodrigues, César de Almeida; Barbosa, Milson dos Santos; Santos, Jefferson Cleriston Barros dos; Lisboa, Milena Chagas; Souza, Ranyere Lucena de; Pereira, Matheus M.; Lima, Álvaro Silva; Soares, Cleide Mara Faria

doi:10.1007/s00449-021-02590-y

Cited by 6 publications

(4 citation statements)

References 45 publications

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“…The maximum percentage of conversion into fatty acids of licuri oil is in accordance with the work presented by Rodrigues et al, where the conversion reached 50.9 � 0.7 % in the hydrolysis of licuri oil catalyzed by Burkholderia cepacia lipase. [22] Qiao et al investigated the enzyme content in hydrolysis reaction of soybean with four ChemCatChem different lipases and found that the best conversion rates occurred at 3 % to 5 % of enzyme (per oil mass), in agreement with the results obtained in this work. [23] Therefore these results also demonstrate that the conversion of fatty acids via hydrolysis reaction can be limited especially by the mass load offered for the reaction, since for different lipases this was a unique condition, however, conditioned to reaction times related to the catalytic capacity of each enzyme.…”

Section: Hydrolysis Of Licuri Oilsupporting

confidence: 85%

“…For the reactions with free enzyme, the percentage of fatty acids conversion showed an increase from 34.1±2.6 to 49.5±2.7 (from 3 to 5 wt%, of biocatalyst per gram of oil), remaining stable up to 15 wt% (Figure 1). The maximum percentage of conversion into fatty acids of licuri oil is in accordance with the work presented by Rodrigues et al ., where the conversion reached 50.9±0.7 % in the hydrolysis of licuri oil catalyzed by Burkholderia cepacia lipase [22] . Qiao et al .…”

Section: Resultsmentioning

confidence: 99%

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Strategies to Reuse of Biocatalysts in the Hydrolysis and Esterification Reactions of Licuri (Syagrus coronata (Mart.) Becc.) Oil

et al. 2022

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The industrial limitations for the use of enzymes are mainly related to their catalytic capacity and their high cost. Herein, it is proposed to evaluate the productive capacity of Burkholderia cepacia lipase (free enzyme and cross‐linked enzyme aggregates – CLEAs) for the hydrolysis and esterification reactions of licuri (Syagrus coronata (Mart.) Becc.) oil, also addressing different strategies to optimize the processes for the reuse of this valuable biocatalyst. For hydrolysis reactions, it was obtained an increase of 178 % in fatty acids productivity using CLEAS compared to free enzymes. By submitting the system to liquid‐liquid separation, it was possible to reuse the free enzymes, which maintained a relative conversion of approximately 75 % of the initial cycle. For the esterification reaction, CLEAs showed a productivity increase of 50 times with lauric acid and 15 times with palmitic acid; in addition to being recovered and reused for 5 cycles, with little loss of efficiency, showing good resistance to the organic environment.

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Section: Hydrolysis Of Licuri Oilsupporting

confidence: 85%

Section: Resultsmentioning

confidence: 99%

Strategies to Reuse of Biocatalysts in the Hydrolysis and Esterification Reactions of Licuri (Syagrus coronata (Mart.) Becc.) Oil

et al. 2022

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“…However, none of the tested ligands can interact with the active site of porcine pancreas lipase, showing that its low catalytic performance. The validity of molecular simulations was also demonstrated by Rodrigues et al [82], Cai et al [81] and Jo et al [71].…”

Section: Substrate Specificity Of Lipasementioning

confidence: 60%

Progress and perspectives of enzymatic preparation of human milk fat substitutes

Liu

Dai

Liu

2022

Biotechnol Biofuels

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Human milk fat substitutes (HMFS) with triacylglycerol profiles highly similar to those of human milk fat (HMF) play a crucial role in ensuring the supply in infant nutrition. The synthesis of HMFS as the source of lipids in infant formula has been drawing increasing interest in recent years, since the rate of breastfeeding is getting lower. Due to the mild reaction conditions and the exceptionally high selectivity of enzymes, lipase-mediated HMFS preparation is preferred over chemical catalysis especially for the production of lipids with desired nutritional and functional properties. In this article, recent researches regarding enzymatic production of HMFS are reviewed and specific attention is paid to different enzymatic synthetic route, such as one-step strategy, two-step catalysis and multi-step processes. The key factors influencing enzymatic preparation of HMFS including the specificities of lipase, acyl migration as well as solvent and water activity are presented. This review also highlights the challenges and opportunities for further development of HMFS through enzyme-mediated acylation reactions.

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“…the study of molecular dynamics in relation to biocatalysis can promote an optimization of experimental time in the bench, as these studies can predict the behavior of the biocatalyst against the substrate of interest (Barbosa et al, 2019;Brandão et al, 2020;Santana et al, 2020;Rodrigues et al, 2021). The study of tunnels to access and transport of ligands using experimental techniques in silico is not too investigated, not so well understood, and not yet widely used, as these analyses present a broad challenge, since most methods used to verify tunnels are based on molecular dynamics simulation practices (Stourac et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

In Silico Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters

Azevedo

Silva

Lima

et al. 2022

Front. Bioeng. Biotechnol.

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Motivation: α-Tocopherol is a molecule obtained primarily from plant sources that are important for the pharmaceutical and cosmetics industry. However, this component has some limitations such as sensitivity to oxygen, presence of light, and high temperatures. For this molecule to become more widely used, it is important to carry out a structural modification so that there is better stability and thus it can carry out its activities. To carry out this structural modification, some modifications are carried out, including the application of biotransformation using enzymes as biocatalysts. Thus, the application of a computational tool that helps in understanding the transport mechanisms of molecules in the tunnels present in the enzymatic structures is of fundamental importance because it promotes a computational screening facilitating bench applications.Objective: The aim of this work was to perform a computational analysis of the biotransformation of α-tocopherol into tocopherol esters, observing the tunnels present in the enzymatic structures as well as the energies which correspond to the transport of molecules.Method: To carry out this work, 9 lipases from different organisms were selected; their structures were analyzed by identifying the tunnels (quantity, conformation, and possibility of transport) and later the calculations of substrate transport for the biotransformation reaction in the identified tunnels were carried out. Additionally, the transport of the product obtained in the reaction through the tunnels was also carried out.Results: In this work, the quantity of existing tunnels in the morphological conformational characteristics in the lipases was verified. Thus, the enzymes with fewer tunnels were RML (3 tunnels), LBC and RNL (4 tunnels), PBLL (5 tunnels), CALB (6 tunnels), HLG (7 tunnels), and LCR and LTL (8 tunnels) and followed by the enzyme LPP with the largest number of tunnels (39 tunnels). However, the enzyme that was most likely to transport substrates in terms of α-tocopherol biotransformation (in relation to the Emax and Ea energies of ligands and products) was CALB, as it obtains conformational and transport characteristics of molecules with a particularity. The most conditions of transport analysis were α-tocopherol tunnel 3 (Emax: −4.6 kcal/mol; Ea: 1.1 kcal/mol), vinyl acetate tunnel 1 (Emax: −2.4 kcal/mol; Ea: 0.1 kcal/mol), and tocopherol acetate tunnel 2 (Emax: −3.7 kcal/mol; Ea: 2 kcal/mol).

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Computational and experimental analysis on the preferential selectivity of lipases for triglycerides in Licuri oil

Cited by 6 publications

References 45 publications

Strategies to Reuse of Biocatalysts in the Hydrolysis and Esterification Reactions of Licuri (Syagrus coronata (Mart.) Becc.) Oil

Strategies to Reuse of Biocatalysts in the Hydrolysis and Esterification Reactions of Licuri (Syagrus coronata (Mart.) Becc.) Oil

Progress and perspectives of enzymatic preparation of human milk fat substitutes

In Silico Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters

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