Related Experiment Video
Updated: Mar 22, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
[Characterization of β-1, 4-mannanase from Bacillus pumilus and heterologous expression in Lactobacillus casei]
Objective:
Lactobacillus casei is widely used in food production and feed industry. The aim of this study was to construct the recombinant expression mannanase Lb. casei.
Methods:
The mature peptide gene of β-1,4-mannanase from Bacillus pumilus was cloned into expression vectors pELX1 and pELSH, then electroporated into Lb. casei, establishing an intracellular and a secretion expression mannanase Lb. casei respectively.
Results:
After incubation, the specific activity of β-1,4-mannanase was 23 U/mg whole cell protein for intracellular expression and 8.8 U/mL for secretion expression in supernatant.
Conclusion:
Mannanase gene expression in Lb. casei provides application prospect and deserves further study.
More Related Videos
12:23Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
08:06The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
Published on: February 1, 2018