Synergistic effect in the catalytic activity of lipase Rhizomucor miehei immobilized on zeolites for the production of biodiesel

Vasconcellos, Adriano de; Paula, Alex Silva; Filho, Roberto A. Luizon; Farias, Lucas A.; Gomes, Eleni; Aranda, Donato Alexandre Gomes; Nery, José Geraldo

doi:10.1016/j.micromeso.2012.07.043

Cited by 22 publications

(8 citation statements)

References 74 publications

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“…The only two exceptions were observed for Nano-X/Cu/0.5M-TLL and Nano-X/Ni/0.5M-TLL. In the case of the Nano-X/Cu/0.5M-TLL complexes, the FAEE yield obtained from the complex was lower than yield obtained using the enzymes in their free forms, providing strong evidence that cupric cations are strong inhibitors of both enzymes, as has been reported elsewhere [33].…”

Section: A N U S C R I P Tsupporting

confidence: 72%

“…27 complex can be attributed to the toxicity of copper ions to lipases, as reported in the literature [33], [75][76][77]. This dynamic behavior was not observed for the R. miehei lipase, as the Nano-X/Mn/0.5M-RML, Nano-X/Cu/0.5M-RML, Nano-X/Co/0.5M-RML and Nano-X/Zn/0.5M-RML complexes yielded lower FAEEs contents than the R. miehei enzyme in its free form (see Fig.…”

Section: A C C E P T E D Accepted Manuscriptmentioning

confidence: 78%

“…The nanozeolite-enzyme complexes derived from T. lanuginosus lipase were designated Nano-X/Mn/0.1M-TLL, Nano-X/Mn/0.5M-TLL , Nano-X/Cu/0.1M-TLL, Nano-X/Cu/0.5M-TLL , Nano-X/Co/0.1M-TLL, Nano-X/Co/0.5M-TLL , Nano-X/Zn/0.1M-TLL, Nano-X/Zn/0.5M-TLL , Nano-X/Ni/0.1M-TLL and Nano-X/Ni/0.5M- The enzymatic hydrolytic activities of the free lipases were determined through spectrophotometric analysis according to the method developed by Winkler et al [31] and updated by other researchers [32,33]. The method consists of measuring the micromoles of 4-nitrophenol released via the hydrolysis of p-4-nitrophenyl palmitate (p-NPP).…”

Section: Lipase Immobilization On the Ion-exchanged Nanozeolitic Suppmentioning

confidence: 99%

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Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals

Vasconcellos

Laurenti

Miller

et al. 2015

Microporous and Mesoporous Materials

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Nanozeolite NaX ion exchanged with different transition metals (Mn 2+ ,Cu 2+ , Co 2+ , Zn 2+ , Ni 2+ ) was used as a solid support for the immobilization of the lipases of Thermomyces lanuginosus (TLL) and Rhizomucor miehei (RML). The nanozeolite-enzyme complexes were used as heterogeneous catalysts for the transesterification reaction of palm oil to fatty acid ethyl esters (FAEEs). The most relevant results were obtained with the Thermomyces lanuginosus enzyme immobilized on nanozeolitic supports ion exchanged with Ni 2+ . Although these zeolitic supports were able to immobilize a relatively small amount of the enzyme (43.7%) in comparison with the other nanozeolitic supports, the FAEE yields obtained with Nano-X/Ni/0.5M-TLL complexes were above 94%. These results revealed an unusual synergistic effect between the Thermomyces lanuginosus enzyme and the nickel ion-exchanged nanozeolitic support; this effect was not observed for the complexes prepared with the Rhizomucor miehei enzyme. Bioinformatics calculations were performed for both enzymes by taking into consideration the crystallographic structures of the enzymes and the zeta potential of the surface of the nanozeolitic supports. By combining calculations of the protein electrostatic potential surface and normal mode analyses in a model, we were able to propose an explanation for the synergistic effect between the lipases and the nanozeolitic supports. The synergistic effect could be explained through an allosteric mechanism describing the interaction between aspartic acid residues 102 and 158 of the Thermomyces lanuginosus lipase and the positively charged zeolitic support surface. This interaction results in the stabilization of the opening of the enzyme lid and leaves its catalytic triad permanently exposed to the reaction medium.

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Section: A N U S C R I P Tsupporting

confidence: 72%

Section: A C C E P T E D Accepted Manuscriptmentioning

confidence: 78%

Section: Lipase Immobilization On the Ion-exchanged Nanozeolitic Suppmentioning

confidence: 99%

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Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals

Vasconcellos

Laurenti

Miller

et al. 2015

Microporous and Mesoporous Materials

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“…Diferentes suportes podem ser empregados para imobilização de enzimas, dentre eles as zeólitas (VASCONCELLOS et. al, 2012).…”

Section: Introductionunclassified

Revitalização De Processadoras Automáticas Kodak M35 X-Omat Prox Processor

Cerutti¹,

Reis²,

Santos³

et al. 2019

Impactos Das Tecnologias Nas Ciências Biológicas E Da Saúde 2

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“…Other immobilization methods have been studied, as the immobilization of whole cell [29] and to improve the proprieties and efficiency of enzyme immobilization, some factors have been tested to optimize this process [30,31]. The development of supports for immobilization and the study of the properties of the derivatives and the supports have been investigated for some authors, reporting synergic effect on the enzymatic properties [32][33][34][35]. In some cases, the synergism was achieved by the addition of two distinct lipases in the reaction medium [36].…”

Section: Introductionmentioning

confidence: 99%

Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism

Quilles

Ferrarezi

Borges

et al. 2016

Bioprocess Biosyst Eng

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It is known that lipases may have their catalytic properties improved by the action of some salts or by the adsorption on hydrophobic supports. However, what we present in this work is more than that: we evaluate the combination of these two factors of hyperactivation of lipases from Acremonium-like ROG 2.1.9, a study that has not been done so far. This work proves that a synergistic effect occurs when the lipases are immobilized on hydrophobic supports at the presence of sodium chloride and are applied in triacylglycerol hydrolysis. This assay made it possible to achieve the highest hyperactivation of 500 % with the lipases immobilized on Phenyl-Sepharose and applied with 0.1 M of sodium chloride. Besides this positive effect on enzyme activity, the use of these two factors led to the thermal stability increasing of the immobilized lipases. For this derivative, the recovered activity was approximately 85 % after 6 h incubated at 55 °C and 1.0 M of the sodium chloride against 50 % of the same derivative without this salt. Furthermore, others assays were performed to prove the evidences about the synergistic effect, showing a promising method to improve the catalytic properties of the lipases from Acremonium-like ROG 2.1.9.

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Synergistic effect in the catalytic activity of lipase Rhizomucor miehei immobilized on zeolites for the production of biodiesel

Cited by 22 publications

References 74 publications

Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals

Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals

Revitalização De Processadoras Automáticas Kodak M35 X-Omat Prox Processor

Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism

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