Biocatalyst engineering of Thermomyces Lanuginosus lipase adsorbed on hydrophobic supports: Modulation of enzyme properties for ethanolysis of oil in solvent-free systems

Silveira, Erick Abreu; Moreno-Pérez, Sonia; Şerban, S.; Pestana-Mamede, Rita; Tardioli, Paulo Waldir; Farinas, Cristiane S.; Castejón, Natalia; Fernández‐Lorente, Gloria; Rocha-Martín, Javier

doi:10.1016/j.jbiotec.2018.11.014

Cited by 38 publications

(31 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The mono-lipasic related derivatives TLL-LW and CALB-LW and Novozyme ® 435, were chosen as references. The operational stability of the coCL is high until the fourth cycle and seems to reflect the stability of TLL on LW; for CALB on LW and the closely related industrial biocatalyst Novozyme ® 435 the operational stability is very similar ( Figure 6) [29]. Thus, it seems that the weakest component of the coCL is TLL.…”

Section: Reuse Of Selected CLmentioning

confidence: 93%

“…In the case of the semiCL studied here, that type of differences must emerge from the different orientation on the surface and microenvironment that the lipase acquires after immobilization on the support [7,16]: It is expected that in LW the lipase adsorbs through the open lid surface [20] while in PU through the surface with the higher content of anionic residues. As the CFs for RML and TLL in their respective semiCL shown an opposite behavior with regard to additivity (Figure 3), it is clear that even when the orientation on each support type may be similar for these lipases, the exact effect in catalytic complementarity is Both RML and TLL has been characterized as sn-1,3 specific lipases [29,30]. It has been reported that this specificity can be altered depending on the immobilization support or the solvent used [29,31].…”

Section: Semi Combi-lipases (Semicl): Tll-lw/tll-pu and Rml-lw/rml-pumentioning

confidence: 97%

“…Different combinations of derivatives of the same lipase (TLL or RML) on the supports PU and LW were made and the values of %EE and CF vs. composition were determined, as seen in Figure 3. Both RML and TLL has been characterized as sn-1,3 specific lipases [29,30]. It has been reported that this specificity can be altered depending on the immobilization support or the solvent used [29,31].…”

Section: Semi Combi-lipases (Semicl): Tll-lw/tll-pu and Rml-lw/rml-pumentioning

confidence: 99%

“…Both RML and TLL has been characterized as sn-1,3 specific lipases [29,30]. It has been reported that this specificity can be altered depending on the immobilization support or the solvent used [29,31]. Other reports establish that silica support could catalyze by itself acyl migration, known as the rate-limiting step in EE production for these specific lipases [32].…”

Section: Semi Combi-lipases (Semicl): Tll-lw/tll-pu and Rml-lw/rml-pumentioning

confidence: 99%

See 3 more Smart Citations

Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production

et al. 2019

View full text Add to dashboard Cite

Most Combi-lipases (CL) are based on mixtures of different lipases immobilized on different supports. The increased CL efficiency has been attributed solely to the complementary selectivity of lipases. However, the role of the immobilization support in CL or in co-immobilized systems (coCL) and the application of kinetic models to account CL composition effects, have not been assessed. In this work, commercial lipases from Thermomyces lunuginosus (TLL), Candida antarctica (CALB) and Rhizomocur miehei (RML) and supports as Lewatit®VPOC1600 (LW) and Purolite®ECR1604 (PU), were combined to produce new CL systems for the production of fatty acid ethyl esters (EE) which are the main component of ethylic biodiesel: Co-immobilization slightly altered palm olein EE yields with regard to that of equivalent CL systems, e.g., the best coCL of TLL and CALB in LW (89.5%) and the respective CL (81.8%). The support did affect CL behavior: (i) The best coCL of TLL and RML on LW produced 80.0% EE while on PU 76.4%; (ii) CL based on mixtures of the same enzyme, but immobilized on different supports (semiCL) show complementarity: The best TLL semiCL produced 86.1% EE while its constituents (LW) and (PU) produced individually 78.2 and 70.3%, respectively. The proposed model accounts adequately the EE production properties for CL systems based on TLL, CALB and LW. This work expands the tools to obtain new CL systems for EE production.

show abstract

Section: Reuse Of Selected CLmentioning

confidence: 93%

Section: Semi Combi-lipases (Semicl): Tll-lw/tll-pu and Rml-lw/rml-pumentioning

confidence: 97%

Section: Semi Combi-lipases (Semicl): Tll-lw/tll-pu and Rml-lw/rml-pumentioning

confidence: 99%

Section: Semi Combi-lipases (Semicl): Tll-lw/tll-pu and Rml-lw/rml-pumentioning

confidence: 99%

See 2 more Smart Citations

Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production

et al. 2019

View full text Add to dashboard Cite

show abstract

“…In this scenario, Novozym ® 435 (lipase B from Candida antarctica immobilized on a macroporous resins) the most commonly used lipase in the biodiesel production (see Table 1) [22][23][24]. In general, lipases are used in a wide variety of biotransformation through several types of reactions, such as hydrolysis, esterification and transesterification [25]; therefore, they are used for laboratorial and industrial applications [26][27][28][29][30][31][32][33], such as formulation of drugs, modification of racemic alcohols, acids and esters [34]. Besides, lipases can replace synthetic processes in the industry, such as in the cleaning, hygiene, leather, pharmaceutical and food industries (aroma and flavor) [35], once enzyme exhibits a very high degree of substrate specificity and selectivity [36][37][38].…”

Section: Introductionmentioning

confidence: 99%

Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM

et al. 2020

Self Cite

View full text Add to dashboard Cite

Residual oil from babassu (Orbignya sp.), a low-cost raw material, was used in the enzymatic esterification for biodiesel production, using lipase B from Candida antarctica (Novozym® 435) and ethanol. For the first time in the literature, residual babassu oil and Novozym® 435 are being investigated to obtain biodiesel. In this communication, response surface methodology (RSM) and a central composite design (CCD) were used to optimize the esterification and study the effects of four factors (molar ratio (1:1–1:16, free fatty acids (FFAs) /alcohol), temperature (30–50 °C), biocatalyst content (0.05–0.15 g) and reaction time (2–6 h)) in the conversion into fatty acid ethyl esters. Under optimized conditions (1:18 molar ratio (FFAs/alcohol), 0.14 g of Novozym® 435, 48 °C and 4 h), the conversion into ethyl esters was 96.8%. It was found that after 10 consecutive cycles of esterification under optimal conditions, Novozym® 435 showed a maximum loss of activity of 5.8%, suggesting a very small change in the support/enzyme ratio proved by Fourier Transform Infrared (FTIR) spectroscopy and insignificant changes in the surface of Novozym® 435 proved by scanning electron microscopy (SEM) after the 10 consecutive cycles of esterification.

show abstract

Synthesis of activated carbon from hydrothermally carbonized tamarind seeds for lipase immobilization: characterization and application in aroma ester synthesis

Gonçalves

Gandolfi

Bonomo

et al. 2021

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND: This study aimed to evaluate the effect of hydrothermal carbonization on the activated carbons properties of tamarind seeds, which were used as a support in porcine pancreatic lipase (PPL) immobilization, and to evaluate the biocatalyst in the butyl butyrate synthesis. RESULTS:The activated carbon from hydrochar (ACHT) had oxygen functional groups content about 32.5% higher and a lower point of zero charge (4.42) when compared to those obtained from crude bran (ACT). Differences in textural properties were also observed, with an average pore diameter of 3.20 and 6.46 nm for ACHT and ACT, respectively. The optimal immobilization pH was 5.0, resulting in enzyme loading of 71.8 ± 1.42 mg.g 1 and 53.03 ± 0.31 mg•g −1 , and in a hydrolytic activity of 222.47 ± 2.80 U•g −1 and 257.18 ± 7.31 U•g −1 for ACT and ACHT, respectively. The addition of Triton X-100 0.025 w•v −1 to the immobilization buffer led to an increase in ∼7% of the hydrolytic activity. The PPL immobilized in pH 5.0 was used in the butyl butyrate synthesis, using a mixture of butanol (240 mmol L −1 ) and butyric acid (120 mmol L −1 ), with an esterification yield of ±83% after 4 h of reaction at 40 °C. CONCLUSION:The PPL immobilized on ACHT showed a small decrease in activity over time, with a residual esterification yield of 84% after 4 cycles of reuse. The present results suggest that the supported biocatalyst has the potential to be used in aqueous and organic media, such as hydrolytic lipid reactions and aroma synthesis mostly used in the food industry.

show abstract

Biocatalyst engineering of Thermomyces Lanuginosus lipase adsorbed on hydrophobic supports: Modulation of enzyme properties for ethanolysis of oil in solvent-free systems

Cited by 38 publications

References 53 publications

Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production

Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production

Optimization of the Production of Enzymatic Biodiesel from Residual Babassu Oil (Orbignya sp.) via RSM

Synthesis of activated carbon from hydrothermally carbonized tamarind seeds for lipase immobilization: characterization and application in aroma ester synthesis

Contact Info

Product

Resources

About