Immobilization of lipase B from <i>Candida antarctica</i> on epoxy‐functionalized silica: characterization and improving biocatalytic parameters

Souza, Stefânia P. de; Almeida, Rayza A. D. de; Leão, Raquel A. C.; Bassut, Jonathan; Souza, Rodrigo O. M. A. de; Itabaiana, Ivaldo

doi:10.1002/jctb.5327

Cited by 31 publications

(33 citation statements)

References 52 publications

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“…The immobilization of an enzyme may produce different adverse effects on the enzyme activity because the enzyme molecule may become distorted, mainly when some multi-interactions between the enzyme and the support occur. Also, the active center may become blocked by the immobilization itself [14]. Finally, immobilization may promote diffusion problems of the substrate.…”

Section: Introductionmentioning

confidence: 99%

Regioselective Acylation of Levoglucosan Catalyzed by Candida Antarctica (CaLB) Lipase Immobilized on Epoxy Resin

et al. 2019

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Every year, a large amount of residual agroindustrial waste has been generated and only around 10% is in fact reused. The development of new strategies for biomass valorization is important to add value to these commodities, since biomass is an excellent alternative feedstock to obtain chemicals of interest from renewable resources. The major compound of pyrolytic treatment of lignocellulosic biomass is levoglucosan (1,6-anhydroglucopyranose), an anhydro-sugar that can be transformed into glucose and is greatly valued in the most diverse industrial sectors as a surfactant, emulsifier, or even a lubricant. In this work, levoglucosan was acylated by lipase-catalyzed transesterification in acetonitrile with great conversions and selectivities with different acyl donors such as ethyl esters of lauric, palmitic, stearic, and oleic acids prepared in situ in an integrated strategy mediated by commercial lipases Novozym435 (N435), PSIM, and the home-made biocatalyst CaLB_epoxy. As a result, all biocatalyst generated mostly monoesters, with N435 being more selective to produce lauric esters (99% at 50°C) and PSIM to produce oleic esters (97% at 55 °C) while CaLB_epoxy was more selective to produce oleic esters of levoglucosan (83% at 55°C). This is the first report in the literature on the production of high selectivity levoglucosan esters.

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Section: Introductionmentioning

confidence: 99%

Regioselective Acylation of Levoglucosan Catalyzed by Candida Antarctica (CaLB) Lipase Immobilized on Epoxy Resin

et al. 2019

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“…CALB is an excellent biocatalyst for many types of reactions, such as hydrolysis, esterification, and transesterification. This enzyme has high selectivity and specificity . However, as with other enzymes, CALB is susceptible to inactivation (inhibition or denaturation) by physical–chemical actions, such as extreme temperature changes, pH changes, mechanical shock, or interaction with other substances .…”

Section: Introductionmentioning

confidence: 99%

“…This enzyme has high selectivity and specificity. 11,12 However, as with other enzymes, CALB is susceptible to inactivation (inhibition or denaturation) by physical-chemical actions, such as extreme temperature changes, pH changes, mechanical shock, or interaction with other substances. 13,14 One alternative for avoiding or reducing such inactivation is to immobilize enzymes, 15,16 which enables enzyme recovery and reuse.…”

Section: Introductionmentioning

confidence: 99%

Activation of Candida antarctica lipase B in pressurized fluids for the synthesis of esters

Nyari

Zabot

Zamadei

et al. 2017

J of Chemical Tech & Biotech

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BACKGROUND The objective of this work was to evaluate the activation of Candida antarctica lipase B (CALB) in pressurized CO2 or liquefied petroleum gas (LPG) and, thereafter, to evaluate the synthesis of esters using activated CALB as a biocatalyst. Before activation, CALB was immobilized in polyurethane. For the esterification reactions, mechanical or ultrasonic agitations were studied. The stability of CALB after reuse cycles was also evaluated. RESULTS Before activation, the enzymatic activity of immobilized CALB was 789 U g‐1. After activation in pressurized CO2 and LPG, the activities increased to 2486 U g‐1 and 1413 U g‐1, respectively. Consequently, the residual activities of CALB after activation in pressurized CO2 and LPG were 315% and 179%, respectively. For the best condition of reaction under ultrasonic agitation, oleic acid conversion was 51.2% when using non‐activated CALB. Otherwise, oleic acid conversions were 66.5% and 77.1% when using CALB activated in LPG and CO2, respectively. This biocatalyst maintained more than 80% of its residual activity when reused for up to 13 cycles. CONCLUSION Activation of CALB in pressurized CO2 provided enzymatic activities 1.76 times higher than activation in pressurized LPG did. Immobilized CALB had good performance as a stable biocatalyst for esterification reactions under ultrasonic agitation. © 2017 Society of Chemical Industry

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“…The immobilization of pepsin has been performed using different methods and insoluble polymeric supports, including silica gel, agarose bead, chitosan bead and porous and cellular materials. The use of immobilized enzymes allows reduction in operational costs, once it is possible to recover the enzyme from the reaction medium more efficiently by filtration, thus enabling the reuse of the enzyme and a more efficient control of large‐scale processes …”

Section: Introductionmentioning

confidence: 99%

“…The use of immobilized enzymes allows reduction in operational costs, once it is possible to recover the enzyme from the reaction medium more efficiently by filtration, thus enabling the reuse of the enzyme and a more efficient control of large-scale processes. 9 However, to achieve better process efficiency, the immobilization should ensure enzymatic stability over long periods, preventing enzyme leaching, making it reusable and allowing the free diffusion of substrates and reaction products. 10 Several methods have been used for enzyme immobilization, including adsorption and covalent bonding.…”

Section: Introductionmentioning

confidence: 99%

Pepsin immobilization on biochar by adsorption and covalent binding, and its application for hydrolysis of bovine casein

Santos

Brito

Evaldo

et al. 2019

J of Chemical Tech & Biotech

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BACKGROUND The objective of this research was to compare the efficiency of pepsin immobilization by adsorption and covalent binding on biochar obtained from pupunha palm processing residue, and to use the immobilized enzyme in the hydrolysis of bovine casein. RESULTS The surface modification of biochar with glutaraldehyde was effective, as shown by Fourier transform infrared analyses and the texture properties of the carbons. Both activated and functionalized biochar showed high immobilization efficiency (>95%) and high enzyme‐support binding capacity (>96 mg g–1). During the activity assays, the functionalized carbon showed a higher casein hydrolysis rate when compared to the enzyme immobilized by adsorption, with values of 39.17 U and 32.67 U, respectively, and c. 95% of the activity of the free enzyme, after 60 min. CONCLUSION The functionalization of the biochar led to a surface modification of biochar by the insertion of amine‐aldehyde groups, which was responsible for the formation of strong interactions between the support material and the enzyme, thus providing a greater proteolytic activity when compared to immobilization by adsorption. The immobilized enzymes were able to maintain their proteolytic activity for more than seven cycles of reuse. © 2019 Society of Chemical Industry

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Immobilization of lipase B from Candida antarctica on epoxy‐functionalized silica: characterization and improving biocatalytic parameters

Cited by 31 publications

References 52 publications

Regioselective Acylation of Levoglucosan Catalyzed by Candida Antarctica (CaLB) Lipase Immobilized on Epoxy Resin

Regioselective Acylation of Levoglucosan Catalyzed by Candida Antarctica (CaLB) Lipase Immobilized on Epoxy Resin

Activation of Candida antarctica lipase B in pressurized fluids for the synthesis of esters

Pepsin immobilization on biochar by adsorption and covalent binding, and its application for hydrolysis of bovine casein

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