[Thermal stability improvement for phenylalanine hydroxylase by site-directed mutagenesis].

doi:10.13345/j.cjb.160022

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Article

[Thermal stability improvement for phenylalanine hydroxylase by site-directed mutagenesis].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology - 25 Sept 2016

Ye Shuangshuang, Zhou Li, Zhou Zhemin

Abstract excerpt

In proteins of thermophilic bacteria, Gly is tend to be replaced by Ala and Lys is tend to be replaced by Arg to adapt the high temperature. In order to improve the thermal stability of phenylalanine hydroxylase (PAH) from Chromobacterium violaceum, all the Gly on PAH were mutated to Ala and Lys to Arg. Positive mutant enzymes with improved thermal stability were selected, followed by combined mutation and...

Topics

Bacterial Proteins
Chromobacterium
Enzyme Stability
Hot Temperature
Kinetics
Mutagenesis, Site-Directed
Mutation
Phenylalanine Hydroxylase
Protein Engineering

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PMID: 29022325
DOI: 10.13345/j.cjb.160022

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