Quantifying Immobilized Trypsin on a Synthetic Polyurethane Surface

Department

North Carolina Agricultural and Technical State University

Document Type

Poster

Publication Date

4-17-2026

Abstract

Enzyme immobilization is the process of binding an enzyme to a surface to inhibit its free movement in a solution while preserving its catalytic properties. This process greatly increases the enzyme’s efficiency, reusability, and functional lifetime, making laboratory experiments and industrial processes more cost-effective and environmentally sustainable. However, there are challenges in quantifying the surface-bound enzyme and its retained enzymatic activity when immobilized. The aim of this study is to quantify the amount of trypsin immobilized on a synthetic polyurethane surface. Polyurethane was synthesized using polycaprolactone (PCL) and polyisocyanate. Trypsin was then immobilized onto the surface of the cast polymer. The samples were characterized using Fourier Transform Infrared Spectroscopy (FTIR) and X-ray Photoelectron Spectroscopy (XPS) elemental scans to confirm the presence of trypsin on the surface. Bicinchoninic acid (BCA) and fluorescein isothiocyanate (FITC) assays were performed to quantify the amount of protease present. Preliminary characterization confirmed the presence of trypsin on the surface. Ongoing work will focus on refining quantification methods and evaluating the stability and proteolytic activity of the immobilized enzyme over time.

This document is currently not available here.

Share

COinS