| North Carolina State University Undergraduate Symposium |
2012- 21st Annual NC State Undergraduate Research Symposium |
| Close Details |
| Session Time : 4/10/12 12:15 PM - 4/10/12 1:30 PM |
| Content Area : Chemical & Biomolecular Engineering |
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Poster Appointment: , - |
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Student Presenters :
Brittany Nicole Glatz Chemical Engineering |
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Mentors and/or Co-Authors : Saad Khan Chemical and Biomolecular Engineering Christina Tang Chemical & Biomolecular Eng |
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Abstract Title : Increasing the Catalytic Activity of Immobilized Enzymes |
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Abstract : Enzymes are highly efficient selective biological catalysts, and hyperthermophilic enzymes are of particular interest due to their ability to function at elevated temperatures common to industrial processes. For our work, we are using the hyperthermophilic enzyme, α-galactosidase from Thermotoga maritima as a model system. The following method for enzyme immobilization is proposed: produce enzyme-loaded poly(vinyl alcohol) (PVA) nanofibers by electrospinning a solution containing enzyme, then chemically crosslinking the resulting fibers to render them water insoluble to immobilize the enzyme. Initial work indicates that the enzyme loses significant catalytic activity upon immobilization. The aim is to maximize the retained activity of the immobilized enzyme. One approach is to incorporate a small molecule known to prevent dehydration of the enzyme such as trehalose. Another approach is substrate-induced stabilization which involves electrospinning the enzyme solution with a known substrate, such as raffinose. The hypothesis is that this will help to maintain its active conformation and protect the active site during immobilization. The first step in these approaches is to determine how these additives affect the electrospinning of PVA. Solution dynamics and electrospinnability of these systems were explored. It was found that the addition of raffinose or trehalose did not affect the PVA entanglement required to electrospin. Based on these results, it was determined that the addition of trehalose or raffinose does not affect the electrospinnability of PVA. The next step will be to incorporate the enzyme into the PVA/trehalose or PVA/raffinose system and determine if the performance of the immobilized enzyme is improved. |