In Situ Calb Enzyme Immobilization in Mesoporous Material Type MCM-48 Synthesis Using Ionic Solid [C14MI]Cl as Structure-Directing Agent

Battiston, Catia Santin Zanchett; Ficanha, A. M. M.; Oro, Carolina Elisa Demaman; Dallago, Rogério Marcos; Mignoni, Marcelo Luís

doi:10.1007/s12010-021-03648-z

Cited by 6 publications

(3 citation statements)

References 29 publications

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“…The synthesis of the ionic solids [C 16 MI]Cl (1-hexadecyl-3-methylimidazolium chloride) and [C 14 MI]Cl (1tetradecyl-3-methylimidazolium chloride) and use in the immobilization of CALB in MCM-48 was performed as previously described by (Battiston et al 2022).…”

Section: Synthesis Of Mcm-48 Mesoporous Materials and In Situ Immobil...mentioning

confidence: 99%

“…However, the esteri cation of geraniol can overcome this de ciency, altering olfactory characteristics and biological properties (Bahadori et Regarding the choice of lipase for the present study, Candida antarctica type B (CALB) stands out in terms of the e ciency of its applications and is well established for biocatalysis purposes. Our research group successfully immobilized CALB on the MCM-48 structure using the ionic solids [C 16 MI]Cl (1hexadecyl-3-methylimidazolium chloride) (Battiston et al 2017) and [C 14 MI]Cl (1-tetradecyl-3methylimidazolium chloride) (Battiston et al 2022) structure-directing agents. However, no studies were found in the literature regarding the use of CALB immobilized on MCM-type supports in the synthesis of geranyl acetate and geranyl butyrate.…”

Section: Introductionmentioning

confidence: 99%

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In Situ Immobilization of CAL B Enzyme in Mesoporous Materials of the MCM-48 Type Using Different Ionic Solids: Synthesis and Application in Sterification Reactions

Battiston,

Oro,

Ficanha

et al. 2024

Preprint

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The ionic solids [C16MI]Cl and [C14MI]Cl were used as structure directors on MCM-48 mesoporous support with immobilized CALB lipase for the synthesis of esters from geraniol. Significant results were obtained in the synthesis of geranyl acetate and geranyl butyrate. Enzyme concentration, temperature and molar ratio of substrates were parameters that affect the synthesis yield. The highest temperature (60°C) and highest enzyme concentration (13%) conditions showed the best ester conversion results. For both esters, the ionic liquid [C16MI]Cl showed better conversion results and reached a value above 38% of conversion. Furthermore, the support tested in the present study for application in ester synthesis is cost-effective. In addition, the enzymatic route to obtain the esters presents mild reaction conditions and the results show potential for application in industrial applications.

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Section: Synthesis Of Mcm-48 Mesoporous Materials and In Situ Immobil...mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

In Situ Immobilization of CAL B Enzyme in Mesoporous Materials of the MCM-48 Type Using Different Ionic Solids: Synthesis and Application in Sterification Reactions

Battiston,

Oro,

Ficanha

et al. 2024

Preprint

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show abstract

“…Despite these challenges, the remarkable catalytic capabilities offered by enzymes for numerous applications have spurred extensive research aimed at addressing these issues [6][7][8][9]. One successful and straightforward strategy to overcome these limitations is the immobilization of enzymes onto a support [8, [10][11][12][13][14][15]. The advantages of immobilized enzymes over their free counterparts include the preservation of activity and stability at various temperatures, pH levels, and even in the presence of organic solvents [16][17][18][19][20][21][22][23][24][25][26].…”

Section: Introductionmentioning

confidence: 99%

Enhancing Enzyme Stability and Functionality: Covalent Immobilization of Trypsin on Magnetic Gum Arabic Modified Fe3O4 Nanoparticles

BEHSHAD,

Pazhang,

Najavand

et al. 2023

Preprint

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This study aimed to fabricate gum Arabic (GA)–coated Fe3O4 nanoparticles bearing numerous active aldehyde groups on their surface, followed by an assessment of their capability as a magnetic support for the covalent immobilization of the trypsin enzyme for the first time. FT-IR, XRD, TGA, and SEM results demonstrated the successful synthesis of GA-coated Fe3O4 nanoparticles, along with the covalent immobilization of the enzyme onto the support. Immobilization enhanced the relative enzymatic activity across a range of aqueous solution pH levels (ranging from 4 to 11) and temperatures (ranging from 20 to 80°C) without altering the optimum pH and temperature for trypsin activity. Kinetic studies using Michaelis-Menten plots revealed changes in kinetic parameters, including a lower Vmax and higher Km for immobilized trypsin compared to the free enzyme. The immobilization onto magnetic gum Arabic nanoparticles resulted in an improved stability of trypsin in the presence of various solvents, maintaining a stability order comparable to that of the free enzyme due to the stabilizing effect of the support. The reusability results showed that the immobilized enzyme can retain over 93% of its activity for up to 15 cycles.

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Immobilization of Lipase from Candida antarctica B (CALB) by Sol–Gel Technique Using Rice Husk Ash as Silic Source and Ionic Liquid as Additive

Vesoloski

Todero

Macieski

et al. 2022

Appl Biochem Biotechnol

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In Situ Calb Enzyme Immobilization in Mesoporous Material Type MCM-48 Synthesis Using Ionic Solid [C14MI]Cl as Structure-Directing Agent

Cited by 6 publications

References 29 publications

In Situ Immobilization of CAL B Enzyme in Mesoporous Materials of the MCM-48 Type Using Different Ionic Solids: Synthesis and Application in Sterification Reactions

In Situ Immobilization of CAL B Enzyme in Mesoporous Materials of the MCM-48 Type Using Different Ionic Solids: Synthesis and Application in Sterification Reactions

Enhancing Enzyme Stability and Functionality: Covalent Immobilization of Trypsin on Magnetic Gum Arabic Modified Fe3O4 Nanoparticles

Immobilization of Lipase from Candida antarctica B (CALB) by Sol–Gel Technique Using Rice Husk Ash as Silic Source and Ionic Liquid as Additive

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