Optimization of the enzymatic hydrolysis of<i>Moringa oleifera</i>Lam oil using molecular docking analysis for fatty acid specificity

Barbosa, Milson dos Santos; Freire, Cintia C.C.; Almeida, Lays Carvalho de; Freitas, Lisiane Santos; Souza, Ranyere Lucena de; Pereira, Ernandes Benedito; Mendes, Adriano A.; Pereira, Matheus M.; Lima, Álvaro Silva; Soares, Cleide Mara Faria

doi:10.1002/bab.1793

Cited by 40 publications

(29 citation statements)

References 60 publications

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“…Accordingly, although all of the fatty acids interact with the active site of the BCL, lauric acid has a higher preference of printing in BCL active site, once it is the only one that interacts with two amino acids that constitute the catalytic triad of lipase (Ser87 and His286) (Figure 2b). In addition to these results, the docking affinity energy values for the fatty acids in respect to the BCL structure decreases in the same order of the relative activity of BCL: lauric (−6.3 kcalˑmol −1 ) < myristic (−6.0 kcalˑmol −1 ) < palmitic (−5.9 kcalˑmol −1 ) = stearic (−5.9 kcalˑmol −1 ) 44 . The docking affinity values represent the binding pose preference for imprinted molecule relative to BCL structure.…”

Section: Resultsmentioning

confidence: 58%

“…In addition to these results, the docking affinity energy values for the fatty acids in respect to the BCL structure decreases in the same order of the relative activity of BCL: lauric (−6.3 kcalˑmol −1 ) < myristic (−6.0 kcalˑmol −1 ) < palmitic (−5.9 kcalˑmol −1 ) = stearic (−5.9 kcalˑmol −1 ). 44 The docking affinity values represent the binding pose preference for imprinted molecule relative to BCL structure. The diagram shown in Figure 2c also shows that lauric acid is docked near to amino acids that constitute the BCL lid (circled with dashed lines), resulting in a higher access of substrate to lipase active site.…”

Section: Molecular Docking Analysismentioning

confidence: 99%

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Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Brandão

Barbosa

Souza

et al. 2020

Biotechnology Progress

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Bioimprinting is an easy, sustainable and low-cost technique that promotes a printing of potential substrates on enzyme structure, inducing a more selective and stable conformation. Bioimprinting promotes conformational changes in enzymes, resulting in better catalytic performance. In this work, the effect of bioimprinting of Burkholderia cepacia lipase (BCL) and porcine pancreatic extracts (PPE) with four different fatty acids (lauric acid (C12:0), myristic acid (C14:0), palmitic acid (C16:0), and stearic acid (C18:0)) was investigated. The results demonstrated that the better bioimprinting effect was in BCL with lauric acid in esterification reaction, promoting BCL activation in which relative enzyme activity was 70 times greater than nonimprinted BCL. Bioimprinting results were influenced by the carbon chain length of fatty acids imprinted in the BCL, in which the effects were weaker with the chain increase. Molecular docking was performed to better understand the bioimprinting method. The results of these simulations showed that indeed all fatty acids were imprinted in the active site of BCL. However, lauric acid presented the highest imprinting preference in the active site of BCL, resulting in the highest relative activity. Furthermore, Fourier transform infrared (FTIR) analysis confirmed important variations in secondary structure of bioimprinting BCL with lauric acid, in which there was a reduction in the α-helix content and an increase in the β-sheet content that facilitated substrate access to the active site of BCL and led higher rigidity, resulting in high activity. Bioimprinted BCL with lauric acid showed excellent operational stability in esterification reaction, maintaining its original relative activity after five successive cycles. Thus, the results show that bioimprinting of BCL with lauric acid is a successful strategy due to its high catalytic activity and reusability.

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Section: Resultsmentioning

confidence: 58%

Section: Molecular Docking Analysismentioning

confidence: 99%

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Brandão

Barbosa

Souza

et al. 2020

Biotechnology Progress

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“…Characterization of the heterogeneous biocatalysts prepared in this study and their performance in ester synthesis. These lipase preparations had different purity, enzyme concentration, and stabilizing agents in their formulations, as well as different features, including molecular mass, molecular diameter and activity [48]. However, as shown in Table 1, similar immobilized protein loading (around 20-22 mg/g of support) has been obtained for CRL, PFL and TLL.…”

Section: Immobilization Of Different Lipases On Octyl-siomentioning

confidence: 95%

Sustainable Enzymatic Synthesis of a Solketal Ester—Process Optimization and Evaluation of Its Antimicrobial Activity

et al. 2020

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The present study aims the enzymatic synthesis of solketal palmitate by esterification between solketal and palmitic acid using heptane as solvent. Lipases from Thermomyces lanuginosus (TLL), Candida rugosa type VII (CRL), and Pseudomonas fluorescens (PFL) were immobilized via interfacial activation on rice husk silica functionalized with triethoxy(octyl)silane (Octyl–SiO2) and used as biocatalysts. A loading of 20–22 mg of lipase/g of support was immobilized independently of the studied enzyme. TLL–Octyl–SiO2 was the most active biocatalyst in oil hydrolysis (656.0 ± 23.9 U/g) and ester synthesis (productivity of 6.8 mmol/min.gbiocat), and it has been chosen for further ester synthesis optimization. The effect of some important parameters such as biocatalyst concentration, reaction temperature and acid:alcohol molar ratio on the reaction has been evaluated using a central composite rotatable design at fixed mechanical stirring (240 rpm) and reaction time (15 min). Subsequently, the effect of reactants concentration and molecular sieve concentration has also been examined. Under optimal conditions (56 °C, acid:alcohol molar ratio of 1:3 with a palmitic acid concentration of 1 M, and 20% wt. of TLL–Octyl–SiO2 per volume of reaction mixture), 83% acid conversion was obtained after 150 min of reaction. The biocatalyst retained 87% of its initial activity after seven successive reaction batches. The product was identified by nuclear magnetic resonance analysis. Antimicrobial activity studies showed that the synthesized ester demonstrated antifungal activity against Candida albicans and Candida parapsilosis, with minimum inhibitory concentration (MIC) between 200 and 400 µg/mL, and bacteriostatic/fungistatic action—minimum microbicial concentration (MMC) > 400 µg/mL.

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“…The CS oil hydrolysis step produces free fatty acids that can be used in industrial processes. As also, lipase‐catalyzed selective hydrolysis is a promising method to enrich PUFA in the form of acylglycerols due to its simple and mild reaction conditions, which can prevent quality deterioration of PUFA‐rich oil (Barbosa et al, 2019; Chen et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Potential Use of Crude Coffee Silverskin Oil in Integrated Bioprocess for Fatty Acids Production

Mota

Barbosa

Schneider

et al. 2021

J Americ Oil Chem Soc

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Oil from coffee silverskin (CS) is a potential source of fatty acids with promising applications in several industries. Thus, CS crude oil extraction processes were investigated for further enzymatic hydrolysis for fatty acids production. Firstly, Soxhlet (with 150 mL hexane for 8 hours at 70 °C) and ultrasound‐assisted (three times in sequential with 50 mL of hexane for 30 min at 30 °C) extractions were carried out to extract CS oil (3.8% and 3.1%, respectively). The fatty acid profiles obtained by both extraction methods presented a similar composition, shows palmitic (16:0: 32.6–34.4%) and linoleic acids (18:2: 31.5–36.1%) as the main. Then, CS oil extracted by Soxhlet was used as the feedstock for fatty acids production by enzymatic hydrolysis using four commercial lipases. Among the lipases studied, Candida rugosa lipase (CRL) displayed a higher hydrolytic activity (1143.70 U g−1), with a maximum hydrolysis degree of 51.94% (acid value of the CS oil increased from 13.4 to 37.5 mg KOH g−1) after 180 min of reaction. Molecular docking analysis showed that interactions between the CRL active site (Ser209 and His449) and palmitic acid, the fatty acid of highest concentration in CS oil (≈35%), lead to higher hydrolytic activity. The integrated process developed is an advance in fatty acid production and valorization of coffee industry waste, since there is still a promising approach yet to be explored that aims at the utilization of residual CS oil.

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Optimization of the enzymatic hydrolysis ofMoringa oleiferaLam oil using molecular docking analysis for fatty acid specificity

Cited by 40 publications

References 60 publications

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Sustainable Enzymatic Synthesis of a Solketal Ester—Process Optimization and Evaluation of Its Antimicrobial Activity

Potential Use of Crude Coffee Silverskin Oil in Integrated Bioprocess for Fatty Acids Production

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