Optimization of flavor ester synthesis catalysed by Aspergillus niger lipase

Veríssimo, Lizzy Ayra Alcântara; Soares, Wanescy Caroliny Leite; Mól, Paula Chequer Gouveia; Minim, Valéria Paula Rodrigues; Silva, Maria do Carmo Hespanhol da; Minim, Luís Antônio

doi:10.5897/ajmr2015.7367

Cited by 5 publications

(3 citation statements)

References 30 publications

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“…On the other hand, their activity was similar to the one showed by Thc_Cut1 (~18%). These data are also confirmed by previous publications using these enzymes as the catalysts, where poor esterification yield (<40%) with butyric acid and 1-butanol were obtained in absence of water after 24 h reaction using AnL, as reported by Verissìmo et al (2015) [33]. Regarding TLL, Gumel et al (2016) reported low conversion yield achieved in a continuous flow microreactor for methyl butanoate synthesis [30].…”

Section: Thermomyces Lanuginosus Lipase (Tll) and Aspergillus Niger Lipase (Anl) 3d Surface Responsessupporting

confidence: 87%

“…On the other hand, Aspergillus niger is among the most wellknown lipase producers and its enzyme is suitable for many uses in industrial applications [31,32]. Besides this, AnL synthesis activity in esterification reactions has not been extensively investigated [33]. Our results on temperature optimum were consistent with others previously published, indicating that, in polycondensation reactions, Thc_Cut1 is more efficient at 50 • C than at 70 • C, with C 4 monomer conversion rates in 24 h of~80% and~37%, respectively [6,23].…”

Section: Thermomyces Lanuginosus Lipase (Tll) and Aspergillus Niger Lipase (Anl) 3d Surface Responsesmentioning

confidence: 99%

“…On the other hand, Aspergillus niger is among the most well-known lipase producers and its enzyme is suitable for many uses in industrial applications [31,32]. Besides this, AnL synthesis activity in esterification reactions has not been extensively investigated [33].…”

Section: Thermomyces Lanuginosus Lipase (Tll) and Aspergillus Niger Lipase (Anl) 3d Surface Responsesmentioning

confidence: 99%

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Biocatalyzed Synthesis of Flavor Esters and Polyesters: A Design of Experiments (DoE) Approach

Fabbri

Bertolini

Guebitz

et al. 2021

IJMS

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In the present work, different hydrolases were adsorbed onto polypropylene beads to investigate their activity both in short-esters and polyesters synthesis. The software MODDE® Pro 13 (Sartorius) was used to develop a full-factorial design of experiments (DoE) to analyse the thermostability and selectivity of the immobilized enzyme towards alcohols and acids with different chain lengths in short-esters synthesis reactions. The temperature optima of Candida antarctica lipase B (CaLB), Humicola insolens cutinase (HiC), and Thermobifida cellulosilytica cutinase 1 (Thc_Cut1) were 85 °C, 70 °C, and 50 °C. CaLB and HiC preferred long-chain alcohols and acids as substrate in contrast to Thc_Cut1, which was more active on short-chain monomers. Polymerization of different esters as building blocks was carried out to confirm the applicability of the obtained model on larger macromolecules. The selectivity of both CaLB and HiC was investigated and best results were obtained for dimethyl sebacate (DMSe), leading to polyesters with a Mw of 18 kDa and 6 kDa. For the polymerization of dimethyl adipate (DMA) with BDO and ODO, higher molecular masses were obtained when using CaLB onto polypropylene beads (CaLB_PP) as compared with CaLB immobilized on macroporous acrylic resin beads (i.e., Novozym 435). Namely, for BDO the Mn were 7500 and 4300 Da and for ODO 8100 and 5000 Da for CaLB_PP and for the commercial enzymes, respectively. Thc_Cut1 led to polymers with lower molecular masses, with Mn < 1 kDa. This enzyme showed a temperature optimum of 50 °C with 63% of DMA and BDO when compared to 54% and 27%, at 70 °C and at 85 °C, respectively.

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Section: Thermomyces Lanuginosus Lipase (Tll) and Aspergillus Niger Lipase (Anl) 3d Surface Responsessupporting

confidence: 87%

Section: Thermomyces Lanuginosus Lipase (Tll) and Aspergillus Niger Lipase (Anl) 3d Surface Responsesmentioning

confidence: 99%

Section: Thermomyces Lanuginosus Lipase (Tll) and Aspergillus Niger Lipase (Anl) 3d Surface Responsesmentioning

confidence: 99%

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Biocatalyzed Synthesis of Flavor Esters and Polyesters: A Design of Experiments (DoE) Approach

Fabbri

Bertolini

Guebitz

et al. 2021

IJMS

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Ternary Blended Chitosan/Chitin/ $$\hbox {FE}_{3}\hbox {O}_{4}$$ FE 3 O 4 Nanosupport for Lipase Activation and Stabilization

et al. 2019

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Facile modulation of enantioselectivity of thermophilic Geobacillus zalihae lipase by regulating hydrophobicity of its Q114 oxyanion

Wahab

Basri

Rahman

et al. 2016

Enzyme and Microbial Technology

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Site-directed mutagenesis of the oxyanion-containing amino acid Q114 in the recombinant thermophilic T1 lipase previously isolated from Geobacillus zalihae was performed to elucidate its role in the enzyme's enantioselectivity and reactivity. Substitution of Q114 with a hydrophobic methionine to yield mutant Q114M increased enantioselectivity (3.2-fold) and marginally improved reactivity (1.4-fold) of the lipase in catalysing esterification of ibuprofen with oleyl alcohol. The improved catalytic efficiency of Q114L was concomitant with reduced flexibility in the active site while the decreased enantioselectivity of Q114L could be directly attributed to diminished electrostatic repulsion of the substrate carboxylate ion that rendered partial loss in steric hindrance and thus enantioselectivity. The highest E-values for both Q114L (E-value 14.6) and Q114M (E-value 48.5) mutant lipases were attained at 50°C, after 12-16h, with a molar ratio of oleyl alcohol to ibuprofen of 1.5:1 and at 2.0% (w/v) enzyme load without addition of molecular sieves. Pertinently, site-directed mutagenesis on the Q114 oxyanion of T1 resulted in improved enantioselectivity and such approach may be applicable to other lipases of the same family. We demonstrated that electrostatic repulsion phenomena could affect flexibility/rigidity of the enzyme-substrate complex, aspects vital for enzyme activity and enantioselectivity of T1.

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Optimization of flavor ester synthesis catalysed by Aspergillus niger lipase

Cited by 5 publications

References 30 publications

Biocatalyzed Synthesis of Flavor Esters and Polyesters: A Design of Experiments (DoE) Approach

Biocatalyzed Synthesis of Flavor Esters and Polyesters: A Design of Experiments (DoE) Approach

Ternary Blended Chitosan/Chitin/ $$\hbox {FE}_{3}\hbox {O}_{4}$$ FE 3 O 4 Nanosupport for Lipase Activation and Stabilization

Facile modulation of enantioselectivity of thermophilic Geobacillus zalihae lipase by regulating hydrophobicity of its Q114 oxyanion

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