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Man/Cel5B, a Bifunctional Enzyme Having the Highest Mannanase Activity in the Hyperthermic Environment
Beenish Sadaqat1, Chong Sha1, Parveen Fatemeh Rupani1
1Biofuels Institute, School of the Environment and Safety Engineering, Jiangsu University, Zhenjiang, China.
Frontiers in Bioengineering and Biotechnology
|April 2, 2021
Summary
A novel bifunctional enzyme, Man/Cel5B, from Thermotoga maritima exhibits high activity on galactomannan and carboxymethyl cellulose. This hyperthermophilic enzyme shows potential for industrial applications in food, feed, and biofuel production.
Area of Science:
- Biochemistry
- Enzymology
- Industrial Biotechnology
Background:
- Thermotoga maritima possesses genes for hyperthermophilic enzymes with industrial potential.
- Gene TM1752 was annotated as cellulase Cel5B, but its function required investigation.
Purpose of the Study:
- To clone, express, purify, and characterize the enzyme encoded by TM1752 from Thermotoga maritima.
- To identify the enzymatic activities and optimal conditions for the recombinant protein.
Main Methods:
- Gene cloning and expression in Escherichia coli.
- Enzyme purification and characterization, including activity assays and stability tests.
- Thin layer chromatography for substrate degradation analysis.
Main Results:
- The purified enzyme, Cel5B, demonstrated high specific activities on galactomannan (416 U/mg) and carboxymethyl cellulose (215 U/mg).
- The enzyme, renamed Man/Cel5B, functions optimally at 85°C and pH 5.5, showing excellent thermostability and pH stability.
- Degradation of locust bean gum yielded mannobiose, mannotriose, and mannooligosaccharides.
Conclusions:
- Cel5B is a novel bifunctional mannanase and cellulase, designated Man/Cel5B, with unique properties.
- Man/Cel5B's high activity, stability, and substrate specificity indicate significant potential for industrial applications in food, feed, and biofuel sectors.
