Related Experiment Video
Updated: Feb 28, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
High-level expression of recombinant thermostable β-glucosidase in Escherichia coli by regulating acetic acid
Xuejia Shi1, Jingcong Xie1, Shiyong Liao1
1College of Chemical Engineering, Nanjing Forestry University, 159 Long Pan Road, Nanjing 210037, China.
Abstract:
In the fermentation progress, fermentation parameters including the feed rate, induction temperature, and induction pH evidently regulate the accumulation of acetic acid generated by recombinant E. coli in the medium. The production of thermostable β-glucosidase (Tpebgl3) was increased by optimizing the parameters mentioned step by step. The optimal conditions were obtained with the highest enzyme expression (560.4U/mL) and the maximum DCW (65g/L) at the pre-induction specific growth rate of 0.2h-1 followed by a post-induction specific growth rate (0.18h-1); induction temperature is 39°C; the pH is 7.2; the concentration of acetic acid was maintained all along below 0.9g/L. Results show it is necessary for the synthesis of Tpebgl3 to regulate the accumulation of acetic acid at the premise of feeding to meet the normal growth of E. coli. The production of Tpebgl3 by recombinant E. coli is the highest reported to date.

