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Enzyme immobilization: an update

  • Review
  • Published:
Journal of Chemical Biology

Abstract

Compared to free enzymes in solution, immobilized enzymes are more robust and more resistant to environmental changes. More importantly, the heterogeneity of the immo-bilized enzyme systems allows an easy recovery of both enzymes and products, multiple re-use of enzymes, continuous operation of enzymatic processes, rapid termination of reactions, and greater variety of bioreactor designs. This paper is a review of the recent literatures on enzyme immobilization by various techniques, the need for immobilization and different applications in industry, covering the last two decades. The most recent papers, patents, and reviews on immobilization strategies and application are reviewed.

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Abbreviations

ALG:

Alginate

AuNPs:

Gold nanoparticles

CLEAs:

Cross-linked enzyme aggregates

CLECs:

Cross-linked enzyme crystals

CLIO:

Cross-linked iron oxide

CS:

Chitosan

DEAE:

Dimethylaminoethyl

EDC:

1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide

FDA:

Food and Drug Association

HPLC:

High-performance liquid chromatography

IMAC:

Immobilized metal affinity chromatography

K d :

Dissociation constant

K M :

Michaelis constant

LC–MS:

Liquid chromatography–mass spectrometry

LCST:

Low critical solution temperature

MIONs:

Monocrystalline iron oxide nanoparticles

NHS:

N-Hydroxysuccinimide

Ni-NTA:

Nickel nitrilotriacetic acid

PLA:

Poly(lactic acid)

PLGA:

Poly(lactic-co-glycolic acid)

polyNIPAM:

Poly-N-isopropylacrylamide

PVA:

Polyvinyl alcohol

T m :

Transition temperature

USPIO:

Ultrasmall superparamagnetic iron oxide

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Acknowledgments

We would like to thank the financial support by Hormozgan Science and Technology Park.

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Authors and Affiliations

  1. Department of Biology, Faculty of Science, University of Hormozgan, Bandarabbas, Iran

    Ahmad Abolpour Homaei

  2. Reyhaneh Sariri, Department of Microbiology, Lahijan Branch, Islamic Azad University, Lahijan, Iran

    Reyhaneh Sariri

  3. Department of Comparative Biomedicine and Food Science, University of Padua, Padua, Italy

    Fabio Vianello

  4. Department of Molecular Sciences and Nanosystems, University of Venice, Venice, Italy

    Roberto Stevanato

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  1. Ahmad Abolpour Homaei
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  2. Reyhaneh Sariri
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  3. Fabio Vianello
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  4. Roberto Stevanato
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Correspondence to Ahmad Abolpour Homaei, Reyhaneh Sariri or Roberto Stevanato.

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Homaei, A.A., Sariri, R., Vianello, F. et al. Enzyme immobilization: an update. J Chem Biol 6, 185–205 (2013). https://doi.org/10.1007/s12154-013-0102-9

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  • DOI: https://doi.org/10.1007/s12154-013-0102-9

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