Related Experiment Video
Updated: Aug 16, 2026
Protein Engineering by Yeast Surface Display
Published on: November 29, 2024
Development and characterization of membrane surface display system using molecular chaperon, prsA, of Bacillus
June-Hyung Kim1, In-Suk Park, Byung-Gee Kim
1Institute for Molecular Biology and Genetics, School of Chemical Engineering, Seoul National University, Seoul, Republic of Korea.
Abstract:
We report a new membrane surface display system based on molecular chaperon, prsA, of Bacillus subtilis. Clostridium thermocellum cellulase, celA, was fused to C-terminal end of PrsA. Cellulase activity of B. subtilis protoplast, which expressed PrsA-CelA was 15 times higher compared to control strain. More than 85% of total cellulase activity was observed in surface displayed format and less than 15% of total cellulase activity was found in supernatant. Flow cytometric analysis of protoplast of PrsA-CelA fusion expressing bacteria provided another proof of uniform expression of fusion protein onto cytoplasmic membrane of B. subtilis. Without lysozyme treatment, only part of cellulase activity (10%) was observed in whole cell fraction.
