Document Detail


Design and Implementation of Two-Dimensional Polymer Adsorption Models: Evaluating the Stability of Candida antarctica Lipase B/Solid-Support Interfaces by QCM-D.
MedLine Citation:
PMID:  23286367     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
A two-dimensional model of a solid-supported enzyme catalyst bead is fabricated on a quartz crystal microbalance with dissipation monitoring (QCM-D) sensor to measure in situ interfacial stability and mechanical properties of Candida antarctica Lipase B (CAL B) under varied conditions relating to ring-opening polymerization. The model was fabricated using a dual photochemical approach, where poly(methyl methacrylate) (PMMA) thin films were crosslinked by a photoactive benzophenone monolayer and blended crosslinking agent. This process produces two dimensional, homogenous, rigid PMMA layers, which mimic commercial acrylic resins in a QCM-D experiment. Adsorption of CAL B to PMMA in QCM-D under varied buffer ionic strengths produces a viscoelastic enzyme surface that becomes more rigid as ionic strength increases. The rigid CAL B/PMMA interface demonstrates up to 20 % desorption of enzyme with increasing trace water content. Increased polycaprolactone (PCL) binding at the enzyme surface was also observed, indicating greater PCL affinity for a more hydrated enzyme surface. The enzyme layer destabilized with increasing temperature, yielding near complete reversible catalyst desorption in the model.
Authors:
Sara V Orski; Santanu Kundu; Richard A Gross; Kathryn L Beers
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-4
Journal Detail:
Title:  Biomacromolecules     Volume:  -     ISSN:  1526-4602     ISO Abbreviation:  Biomacromolecules     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-4     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100892849     Medline TA:  Biomacromolecules     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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