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 Experiment Videos

Alpha-chymotrypsin catalysis in imidazolium-based ionic liquids.

J A Laszlo1, D L Compton

  • 1New Crops and Processing Research, USDA-ARS, National Center for Agricultural Utilization Research, 1815 N. University St., Peoria, IL 61604 USA.

Biotechnology and Bioengineering
|September 6, 2001
PubMed
Summary

Alpha-chymotrypsin enzyme activity in ionic liquids was investigated. Moderate activity was observed with sufficient water, with higher rates in 1-octyl-3-methylimidazolium hexafluorophosphate, especially when combined with supercritical carbon dioxide.

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

Modeling the response of normally achieving and at-risk first grade children to word reading instruction.

Annals of dyslexia·2010
Same author

Are RAN- and phonological awareness-deficits additive in children with reading disabilities?

Dyslexia (Chichester, England)·2002
Same author

Brain-derived neurotrophic factor transgenic mice exhibit passive avoidance deficits, increased seizure severity and in vitro hyperexcitability in the hippocampus and entorhinal cortex.

Neuroscience·1999
Same author

Receptor tyrosine kinase specific for the skeletal muscle lineage: expression in embryonic muscle, at the neuromuscular junction, and after injury.

Neuron·1995
Same author

Differential role of the low affinity neurotrophin receptor (p75) in retrograde axonal transport of the neurotrophins.

Neuron·1995
Same author

Identification of full-length and truncated forms of Ehk-3, a novel member of the Eph receptor tyrosine kinase family.

Oncogene·1995

Area of Science:

  • Biocatalysis
  • Enzyme Engineering
  • Green Chemistry

Background:

  • Ionic liquids (ILs) offer unique solvent properties for enzymatic reactions.
  • Understanding enzyme behavior in ILs is crucial for developing novel biocatalytic processes.
  • Supercritical carbon dioxide (SC-CO2) is a tunable, environmentally friendly co-solvent.

Purpose of the Study:

  • To examine the transesterification activity of alpha-chymotrypsin in ILs ([bmim][PF(6)] and [omim][PF(6)]) and with SC-CO2.
  • To determine if established trends in enzyme activity (solvent polarity, water, support) apply to IL environments.
  • To evaluate the impact of IL structure and water content on enzyme performance.

Main Methods:

  • Investigated alpha-chymotrypsin-catalyzed transesterification of N-acetyl-L-phenylalanine ethyl ester with 1-propanol.

Related Experiment Videos

  • Utilized ionic liquids 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim][PF(6)]) and 1-octyl-3-methylimidazolium hexafluorophosphate ([omim][PF(6)]).
  • Combined ILs with supercritical carbon dioxide (SC-CO2) and varied water concentrations.

    • Main Results:

    • Enzyme showed no activity at very low water concentrations in ILs.
    • Moderate transesterification rates were achieved with >=0.25% water (v/v) in ILs.
    • Enzyme activity was significantly higher in [omim][PF(6)] compared to [bmim][PF(6)].
    • No added water was required for activity when ILs were combined with SC-CO2.
    • Enzyme support complexation (PEG, KCl) did not enhance activity in ILs as it did in organic solvents.

    Conclusions:

    • Ionic liquids ([bmim][PF(6)], [omim][PF(6)]) create a polar environment affecting enzyme activity.
    • Water content is critical for alpha-chymotrypsin activity in these ILs.
    • [omim][PF(6)] is a more favorable medium than [bmim][PF(6)] for this enzymatic reaction.
    • Combining ILs with SC-CO2 optimizes enzyme activity by modifying the polar environment without needing added water.