442405 Hyrdogel Encapsulation to Enhance Enzyme Stability and Functionality

Monday, November 9, 2015
Exhibit Hall 1 (Salt Palace Convention Center)
Jordan Chapman, Department of Chemical Engineering, West Virginia University, Morgantown, WV

Hydrogel Encapsulation to Preserve Enzyme Functionality

Jordan Chapman and Cerasela Zoica Dinu,

Department of Chemical Engineering, West Virginia University, Morgantown, WV

            Enzymes are highly specific biocatalysts that have applications in fields as diverse as drug delivery and alternative fuel production. However, for such applications to be viable the enzymes need to preserve their activity and functionality on a variety of temperature and pH changes. Herein, we are studying the effects of enzyme encapsulation on preserving enzyme functionality at interfaces to help reduce the inhibitory effects of temperature and pH and thus increase its shelf-life and reusability. Using soybean peroxidase (SBP) as a model enzyme, we ensured its encapsulation in hydrogel beads composed of alginate gel and calcium crosslinks. To minimize enzyme leaching and temporal loss of activity, we used scaffolds of nanomaterials of carbon known to provide nanointerfaces with stabilizing effects. The activity and stability of the immobilized and encapsulated SBP was optimized relative to the activity of the free SBP in a variety of environments (e.g., different temperature and solvents). By studying and understanding the benefits that enzyme encapsulation can offer this research could be extended to applications in pharmaceuticals, fragrances, or specialty chemicals, where defining the environment that allows for minimum operational changes is imperious necessary.   

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