Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

[Yield of xenodiagnosis and PCR in the evaluation of specific chemotherapy of Chagas' disease in children].

Boletin chileno de parasitologia·1998
Same author

[Percutaneous suprapubic bladder lithotripsy].

Annales d'urologie·1998
Same author

Factors associated with outcome in major depression: a 6-month prospective study.

Social psychiatry and psychiatric epidemiology·1998
Same author

[Simultaneous transplantation of fetal mesencephalic cells to the striatum and globus pallidus of rats with lesions induced by 6-hydroxydopamine].

Revista de neurologia·1998
Same author

Signs of glaucoma in rhesus monkeys from a restricted gene pool.

Journal of glaucoma·1998
Same author

The Bcl-2 gene is differentially regulated by IL-2 and IL-4: role of the transcription factor NF-AT.

Oncogene·1998

Related Experiment Video

Updated: Jul 4, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
09:27

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

Cellulase immobilization on Fe3O4 and characterization.

A Garcia1, S Oh, C R Engler

  • 1Department of Agricultural Engineering, Texas A&M University, College Station, Texas 77843-2117, USA.

Biotechnology and Bioengineering
|January 15, 1989
PubMed
Summary
This summary is machine-generated.

Researchers developed a method to immobilize cellulase enzymes on iron oxide particles, significantly enhancing their stability and activity for industrial applications.

More Related Videos

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

Related Experiment Videos

Last Updated: Jul 4, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
09:27

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
11:16

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization

Published on: July 11, 2012

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy
11:34

Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Published on: December 20, 2013

Area of Science:

  • Biotechnology
  • Enzyme immobilization
  • Nanomaterials

Background:

  • Cellulase enzymes are crucial for biomass degradation.
  • Immobilization can improve enzyme stability and reusability.
  • Iron oxide nanoparticles offer a versatile platform for enzyme attachment.

Purpose of the Study:

  • To develop a procedure for immobilizing cellulase onto iron oxide nanoparticles.
  • To characterize the activity, stability, and optimal conditions of the immobilized enzyme.
  • To evaluate the efficiency of the immobilization process.

Main Methods:

  • Cellulase was attached to 45 micrometer iron oxide particles using a high-molecular-weight ligand.
  • Mass and activity balances were performed for varying enzyme loadings.
  • Enzyme activity, optimal pH, and half-life were measured and compared to free enzyme.

Main Results:

  • The highest specific activity of the immobilized enzyme was 5.9 mmol glucose/g bound protein/h.
  • Efficacy of retaining enzymatic activity was 128%.
  • The optimal pH shifted to 5.5, and the half-life extended to 272 hours from 0.77 hours.

Conclusions:

  • Successful immobilization of cellulase on iron oxide nanoparticles was achieved.
  • The immobilized enzyme exhibits significantly enhanced stability and activity compared to the free enzyme.
  • This method holds potential for improving enzymatic processes in various industries.