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Article

Assembly of mutations for improving thermostability of Escherichia coli AppA2 phytase.

Applied microbiology and biotechnology - 1 Jul 2008

Kim Moon-Soo, Weaver Jeremy D, Lei Xin Gen

Abstract excerpt

We previously identified a number of mutations in Escherichia coli AppA2 phytase for enhancing its thermostability. The objective of the present study was to determine if these mutations (K46E, K65E, G103S, D112N, D144N, S209G, V227A, and G344D) could be sequentially added to further improve the thermostability of AppA2. Compared with the wild-type enzyme, two variants (D144N/V227A and D144N/V227A/G344D) out of...

Topics

6-Phytase
Acid Phosphatase
Escherichia coli
Escherichia coli Proteins
Hot Temperature
Hydrogen-Ion Concentration
Hydrolysis
Kinetics
Models, Molecular
Multienzyme Complexes
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Conformation

Protein Engineering

Source

Identifiers

PMID: 18443782
DOI: 10.1007/s00253-008-1478-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-18443782-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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