Immobilization of Candida rugosa lipase onto an eco-friendly support in the presence of ionic liquid

Padilla, Rebeca Yndira Cabrera; Lisboa, Milena Chagas; Pereira, Matheus M.; Figueiredo, Renan Tavares; Franceschi, Elton; Fricks, Alini Tinoco; Lima, Álvaro Silva; Silva, Daniel P.; Soares, Cleide Mara Faria

doi:10.1007/s00449-014-1322-2

Cited by 14 publications

(7 citation statements)

References 42 publications

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“…The group of signals at 1151 cm −1 , 1073 cm −1 and 1037 cm −1 are associated with the presence of C-O-C bonds in the protein structure [ 45 ]. In addition, of note are two signals below 1000 cm −1 : at 576 cm −1 a band of N-H stretching vibrations, and at 531 cm −1 a band of scissor vibrations of the C-C bonds forming the skeleton of the enzyme structure [ 46 ].…”

Section: Resultsmentioning

confidence: 99%

Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization

et al. 2015

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Innovative materials were made via the combination of chitin and lignin, and the immobilization of lipase from Aspergillus niger. Analysis by techniques including FTIR, XPS and 13C CP MAS NMR confirmed the effective immobilization of the enzyme on the surface of the composite support. The electrokinetic properties of the resulting systems were also determined. Results obtained from elemental analysis and by the Bradford method enabled the determination of optimum parameters for the immobilization process. Based on the hydrolysis reaction of para-nitrophenyl palmitate, a determination was made of the catalytic activity, thermal and pH stability, and reusability. The systems with immobilized enzymes were found to have a hydrolytic activity of 5.72 mU, and increased thermal and pH stability compared with the native lipase. The products were also shown to retain approximately 80% of their initial catalytic activity, even after 20 reaction cycles. The immobilization process, using a cheap, non-toxic matrix of natural origin, leads to systems with potential applications in wastewater remediation processes and in biosensors.

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Section: Resultsmentioning

confidence: 99%

Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization

et al. 2015

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“…The thermal stability of the immobilized biocatalysts was determined by incubating the samples at temperatures from 55 to 65 °C in water (0.1 mol L −1 phosphate buffer, pH 7.0) for 4 h. Thus, in different time periods, samples were removed, immediately cooled and used to determine activity according to Cabrera‐Padilla et al, with modifications.…”

Section: Methodsmentioning

confidence: 99%

“…Although they have some disadvantages compared with AIL (lower conductivity and stability), LIP have qualities that overcome these limitations, such as methods of synthesis and purification which are simple, good biodegradability, low toxicity, and low cost, awakening the largest industrial interest . Several research studies have confirmed that ionic liquids are suitable media for enzyme catalysis; however, most found in the literature are using aprotic ionic liquids with only some using protic ionic liquids …”

Section: Introductionmentioning

confidence: 99%

Protic ionic liquids influence on immobilization of LipaseBurkholderia cepaciaon hybrid supports

Martins

Santos

Fricks

et al. 2016

J. Chem. Technol. Biotechnol

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BACKGROUND This work aims to assess the use of protic ionic liquids (PIL), propanoate, butanoate and pentanoate of N‐methylmonoetanolamine (C3, C4 and C5), in the preparation of hybrid supports made of poly(3‐hydroxybutyrate‐co‐hydroxyvalerate) (PHBV) and silica for the immobilization of lipase of Burkholderia cepacia (BCL) by covalent binding. For immobilized biocatalysts (IBs), the performance was determined for immobilization and characterization (pH, temperature, stability thermal, operational and in solvents), with the best conditions being defined. For the supports and efficient IB, the morphological and physicochemical characterization (MEV, BET, FTIR and TGA) was evaluated. RESULTS For preparation of the hybrid support, the experiment using 3 g of PHBV presented a higher percentage of mass, around 50% recovery of the support in the granulometry used. The IBs total activity recovery yield (Ya) in hybrid supports modified with ionic liquids IB‐hybrid‐C3 (103%), IB‐hybrid‐C4 (120%) and IB‐hybrid‐C5 (133%) were above the results reported for the control (90%), with IB‐hybrid‐C5 being the most efficient, and presenting better thermal and operational stability. CONCLUSION Burkholderia cepacia lipase was immobilized successfully in a hybrid support (PHBV and silica) modified with protic ionic liquid by covalent binding, resulting in an improvement in the morphological and physicochemical characteristics, and consequently with greater Ya and good thermal and operational stability. © 2016 Society of Chemical Industry

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“…The second method is easy, cheap, and allows simple recycling of the support when the enzyme is no more active. However, there is a possibility of enzymatic desorption 38,39 . Badgujar et al 9 .…”

Section: Resultsmentioning

confidence: 99%

“…However, there is a possibility of enzymatic desorption. 38,39 Badgujar et al 9 also obtained activation of the enzyme (400%) after immobilization in PLA-CH-PVA film.…”

Section: Lipase Immobilization and Organic Reactionmentioning

confidence: 95%

Lipase immobilization on biodegradable film with sericin

Castro

Garcia

Andrade

et al. 2021

Biotech and App Biochem

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An ecofriendly and low‐cost film composed by cassava starch, polyvinyl alcohol, and sericin blend (CS–PVA–SS) was synthesized, characterized, and applied as a novel support for Botryosphaeria ribis EC‐01 lipase immobilization by enzyme–film–enzyme adsorption. Film revealed thickness between 230 and 309 μm and higher flexibility and malleability in comparison with film without SS. Based on p‐nitrophenyl palmitate hydrolysis reaction, the activity retention of immobilized lipase was 987%. For optimal conditions, the yield in ethyl oleate was 95% for immobilized enzyme. Maximum yield was obtained at 49°C, molar ratio oleic acid:ethanol of 1:3, 1.25 g lipase film or 50 U (1.03 ± 0.03 mg protein) and 30 h. Even after seven cycles of use, immobilized lipase showed 52% reduction in ester yield. Biodegradable and biorenewable film is a promising material as a support to immobilize lipases and application in biocatalysis.

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Immobilization of Candida rugosa lipase onto an eco-friendly support in the presence of ionic liquid

Cited by 14 publications

References 42 publications

Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization

Chitin-Lignin Material as a Novel Matrix for Enzyme Immobilization

Protic ionic liquids influence on immobilization of LipaseBurkholderia cepaciaon hybrid supports

Lipase immobilization on biodegradable film with sericin

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