Disulfide bond engineering of AppA phytase for increased thermostability requires co-expression of protein disulfide isomerase in Pichia pastoris

Disulfide bond engineering of AppA phytase for increased thermostability requires co-expression of protein disulfide isomerase in Pichia pastoris

Background: Phytases are widely used commercially as dietary supplements for swine and poultry to increase the digestibility of phytic acid. Enzyme development has focused on increasing thermostability to withstand the high temperatures during industrial steam pelleting. Increasing thermostability o...

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Bibliographic Details
Main Authors: Blinco, J.-A (Author), Chen, X. (Author), Luangthongkam, P. (Author), Luna-Flores, C.H (Author), Mahler, S. (Author), Navone, L. (Author), Speight, R. (Author), Vogl, T. (Author), von Hellens, J. (Author)
Format: Article
Language:English
Published: BioMed Central Ltd 2021
Subjects:
biochemistry
Chaperone
Cobalt compounds
coliform bacterium
Covalent bonds
Dietary supplements
Disulfide bond
Enzymatic properties
enzyme activity
Enzyme development
Enzymes
Escherichia coli
Folding
gene expression
incubation
Industrial processs
Parallel development
pH
phosphatase
Phytase
Pichia pastoris
Production bottlenecks
protein
Protein disulfide isomerases
Protein engineering
Recombinant proteins
Stability
Statistical differences
Sulfur compounds
temperature anomaly
Thermostability
yeast
Yeast
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