Effect of Fold-Promoting Mutation and Signal Peptide Screening on Recombinant Glucan 1,4-Alpha-maltohydrolase Secretion in Pichia pastoris
Contact us if these videos are not relevant.
Contact us if these videos are not relevant.
View abstract on PubMed
Summary
This summary is machine-generated.This study enhances glucan 1,4-alpha-maltohydrolase (GMH) production using Pichia pastoris. Rational design and fermentation optimization significantly boosted enzyme secretion for improved bread quality and storage.
Area Of Science
- Biotechnology
- Enzymology
- Industrial Microbiology
Background
- Glucan 1,4-alpha-maltohydrolase (GMH) is crucial for delaying bread staling and enhancing cold-storage durability.
- Efficient production of GMH is essential for its industrial application in baking.
Purpose Of The Study
- To characterize and optimize the secretory production of a newly cloned Thgmh enzyme.
- To enhance the maltogenic activity and secretion yield of GMH using Pichia pastoris.
Main Methods
- Computational assisted rational design for improved peptide folding.
- Signal peptide screening and gene dosage increment for enhanced secretion.
- Fed-batch fermentation in a 5-L bioreactor for large-scale production.
Main Results
- Rational design increased maltogenic activity 1.6-fold.
- Further optimization improved secretion by approximately 6.4-fold.
- Achieved 6130 U mL⁻¹ extracellular maltogenic activity via fed-batch fermentation.
Conclusions
- A highly promising Pichia pastoris strain for GMH production was successfully developed.
- The optimized strain provides a valuable reference for the secretory production of other industrial enzymes.
Contact us if these videos are not relevant.
Contact us if these videos are not relevant.
