Covalent immobilization of lipase onto aminopropyl-functionalized hydroxyapatite-encapsulated-γ-Fe2O3 nanoparticles: A magnetic biocatalyst for interesterification of soybean oil

Xie, Wenlei; Zang, Xuezhen

doi:10.1016/j.foodchem.2017.01.082

Cited by 176 publications

(60 citation statements)

References 26 publications

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“…[1][2][3][4][5][6] Although their physiological function is the hydrolysis of fats and oils, they have exhibited broad substrate specificity in vitro. Thus, lipases have been used in triglyceride modifications 7 (via transesterification, 8,9 interesterification, 10,11 or acidolysis 12,13 ), resolution of racemic mixtures, [14][15][16] regioselective reactions, [17][18][19] and so forth. In fact, lipases have been one of the most used examples as promiscuous reaction catalysts, 20 being able to catalyze reactions very far from the physiological function, like peroxidation, 21,22 C-C bond formation, [23][24][25] racemase, 26 and so forth.…”

Section: Introductionmentioning

confidence: 99%

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

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Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl‐agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p‐nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl‐CALA was less stable than octyl‐CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl‐CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl‐CALA permitted some stabilization. While octyl‐CALA was more active vs. pNPB, octyl‐CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 35: e2735, 2019

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Section: Introductionmentioning

confidence: 99%

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Arana-Peña

Lokha

Fernández‐Lafuente

2018

Biotechnology Progress

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“…Another important means to promote the implementation of lipases in commercial scale is its usage in immobilized form, which provides enzyme reusability, recyclability, operational stability and thus leading to reduced cost of production. 290 Like any other enzyme, the techniques employed for lipase immobilization include carrier bonding, cross-linking and entrapment. Further, depending upon the type of interactions between enzymes and carriers, irreversible and reversible types of immobilization techniques can be used.…”

Section: Improved Lipasesmentioning

confidence: 99%

Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

302

148

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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

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“…Moreover, the magnetic feature facilitated separation from the reaction media and enabled repeated usage of the enzyme. Magnetic nanoparticles can also be designed in a form of core-shell structure by conjugation with other materials such as hydroxyapatite (Xie W. and Zang X., 2016), silica (Shahrestani H. et al, 2016) and polypyrrol (Yang Z. et al, 2014) for the development of novel composites support for enzyme immobilisation.…”

Section: Biomolecule-hybrid Nanoparticle Conjugatesmentioning

confidence: 99%

Nanoparticles Carrying Biological Molecules: Recent Advances and Applications

Saallah

Lenggoro

2018

KONA

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In the past few decades, enormous advances have been achieved in the field of particle technology and the trend has been shifted from macro to micro and recently to the nanoscale. Integration of nanotechnology and biotechnology has paved the way to the development of biological nanoparticles, derived from biomolecules, and biomolecule-nanoparticle conjugates for numerous applications. This review provides an overview of various types of biological nanoparticles and the methods of their fabrication with primary emphasis on the drying methods, particularly on the newly emerging technique, the electrospraying. Recent advances in the integration of biomolecules with nanoparticles in the past five years to present are also discussed. Finally, the application of the biomolecule-nanoparticle conjugates in various fields including medicals and pharmaceuticals, biosensors and bioelectronics, foods, and agricultures are also highlighted.

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Covalent immobilization of lipase onto aminopropyl-functionalized hydroxyapatite-encapsulated-γ-Fe2O3 nanoparticles: A magnetic biocatalyst for interesterification of soybean oil

Cited by 176 publications

References 26 publications

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Recent advances on sources and industrial applications of lipases

Nanoparticles Carrying Biological Molecules: Recent Advances and Applications

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