Directed evolution of an acid Yersinia mollaretii phytase for broadened activity at neutral pH

Applied Microbiology and Biotechnology
Georgette KörferUlrich Schwaneberg

Abstract

Phytases are phosphohydrolases that initiate the sequential hydrolysis of phosphate from phytate, which is the main storage form of phosphorous in numerous plant seeds, especially in cereals and grains. Phytate is indigestible for most monogastric animals, such as poultry, swine, fish, and humans; therefore, microbial phytases have been widely used in plant (specially soy)-based animal feeding to improve nutrition by enhanced phosphorus, mineral, and trace element absorption, and reducing phosphorus pollution by animal waste. Most phytases used as animal feed additives have an acid pH optimum (pH 2.5 and 5.5 for Aspergillus and pH 4.5 for E. coli phytases) and show a sharp decrease in performance at neutral pH, correlating with intestinal digestion. Directed evolution of phytases has been previously reported to improve enzyme thermostability, pH, or specific activity. In this manuscript, we report a directed evolution campaign of the highly active bacterial phytase from Yersinia mollaretii (YmPh) towards a broadened pH activity spectrum. Directed evolution identified the key positions T44 and K45 for increased YmPh activity at neutral pH. Both positions are located in the active site loop of the phytase and have a synergistic e...Continue Reading

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Citations

Sep 25, 2019·Biotechnology and Bioengineering·Sarah DedischUlrich Schwaneberg
Jun 30, 2019·Applied Microbiology and Biotechnology·Kevin R HerrmannUlrich Schwaneberg
Jan 2, 2021·Current Opinion in Chemical Biology·Serena Gargiulo, Patrice Soumillion
Dec 7, 2021·Critical Reviews in Biotechnology·Shu-Fang LiYu-Guo Zheng

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Datasets Mentioned

BETA
JF911533.1

Methods Mentioned

BETA
PCR
Electrophoresis
Protein Assay
X-ray
size exclusion chromatography

Software Mentioned

Ed
YASARA Structure
AMol
Clone Manager
ERRAT
KnowVolution
YASARA
Verify 3D
Sci
BLAST

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