Surface modification of multiwalled carbon nanotubes (MWCNTs) could enhance the features of the nanomaterial as carrier for enzyme immobilization. In this strategy, magnetic MWCNTs were fabricated by incorporating them with cobalt and functionalization was carried out by aminated polydopamine. The surface modified MWCNTs were then used as a carrier for the immobilization of Candida rugosa lipase (CRL) via covalent binding using glutaraldehyde. The immobilized CRL maintained high activity, which was 3-folds of free CRL. The immobilized CRL exhibited excellent thermal resistance as validated by TGA and DTA technique and was found to be active in a broad range of pH and temperatures in comparison to free CRL. Systematic characterization via FT-IR spectroscopy, CD spectroscopy, SEM, TEM and confocal laser scanning microscopy confirmed the presence of CRL on the modified MWCNTs. Immobilized CRL presented an exquisite recycling performance as after ten consecutive reuses it retained around 84% of its initial hydrolytic activity and further showed high yield enzymatic synthesis of ethyl butyrate and isoamyl acetate having characteristic pineapple and banana flavour demonstrating 78% and 75% ester yield, respectively. The present work provides a novel perspective for lipase catalyzed biotechnological applications by adding a magnetic gain to intrinsic features of MWCNTs.
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http://dx.doi.org/10.1016/j.ijbiomac.2019.08.086 | DOI Listing |
J Biotechnol
January 2025
Department of Chemistry, Sapienza University of Rome, P.le A. Moro 5, 00185 Rome, Italy. Electronic address:
This study explores the immobilization of lipase from Candida rugosa (CRL) on hemp tea waste to catalyze the esterification of oleic acid with primary aliphatic C2-C12 alcohols. in a solvent-free system. The immobilization method employed was adsorption, chosen for its simplicity, low cost, and ability to preserve enzyme activity.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Key Laboratory of Chem-Biosensing of Anhui Province, Key Laboratory of Functional Molecular Solids of Anhui Province, College of Chemistry and Materials Science, Anhui Normal University, Wuhu 241000, Anhui, China. Electronic address:
Adsorption and biodegradation are two important means to remove the pollutants from the environment, but how to combine them and improve the catalytic performance and stability of free enzyme are facing great challenges. Herein, lipase from Candida rugosa (CRL) was immobilized into bimetallic ZnCo-MOF by biomineralization, which not only significantly improved the catalytic activity and stability of CRL but also endowed it with excellent reusability. Furthermore, CRL@ZnCo-MOF established a synergetic system of combined adsorption and enzymatic degradation for the sustainable removal of dibutyl phthalate (DBP) in actual water environment.
View Article and Find Full Text PDFEnviron Pollut
December 2024
Anhui Provincial Key Laboratory of Molecular Enzymology and Mechanism of Major Diseases and Key Laboratory of Biomedicine in Gene Diseases and Health of Anhui Higher Education Institutes, College of Life Sciences, Anhui Normal University, Wuhu, 241000, Anhui, China. Electronic address:
Phthalate esters (PAEs) are broadly utilized as plasticizers in industrial products, posing a significant threat to ecological security and human health. Lipase is a kind of green biocatalyst with the ability to degrade PAEs, but its application is limited due to its low stability and poor reusability. Herein, lipase from Candida rugosa (CRL) was immobilized into an organic ligand replacement MOFs (MAF-507) and cysteine modification and glutaraldehyde cross-linking were simultaneously performed to synthesize immobilized lipase (Cys-CRL@GA@MAF-507) using a one-pot method.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Department of Chemistry, Selcuk University, 42075 Konya, Turkey. Electronic address:
Considering the selective pharmacological activity of chiral drugs, it is important to develop new chiral materials to synthesize them. In this work, two new chiral MOFs (UiO-66@Np and UiO-66@Ib) were prepared by the covalent attachment of the chiral compounds (S-naproxen and S-ibuprofen) to the amine-functionalized Zr-MOF (UiO-66-NH). Then, Candida rugosa lipase (CRL) was immobilized on these chiral MOFs to fabricate two new biocomposites (UiO-66@Np@CRL and UiO-66@Ib@CRL) as effective biocatalysts, which enable significant enhancement in the catalytic activity and enantioselectivity of lipase.
View Article and Find Full Text PDFBioprocess Biosyst Eng
January 2025
Department of Chemistry, Sapienza University of Rome, P.Le A. Moro 5, 00185, Rome, Italy.
For the first time is reported the comparison of solid biocatalysts derived from Candida rugosa lipase (CRL) immobilized on different lignocellulosic wastes (rice husk, brewer's spent grain, hemp tea waste, green tea waste, vine bark, and spent coffee grounds) focusing on the characterization of these materials and their impact on the lipase-support interaction. The wastes were subjected to meticulous characterization by ATR-FTIR, BET, and SEM analysis, besides lignin content and hydrophobicity determination. Investigating parameters influencing immobilization performance revealed the importance of morphology, textural properties, and hydrophobic interactions revealed the importance of morphology, textural properties and especially hydrophobic interactions which resulted in positive correlations between surface hydrophobicity and lipase immobilization efficiency.
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