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Literature summary for 3.1.3.8 extracted from

  • Zhao, Q.; Liu, H.; Zhang, Y.; Zhang, Y.
    Engineering of protease-resistant phytase from Penicillium sp.: High thermal stability, low optimal temperature and pH (2010), J. Biosci. Bioeng., 110, 638-645.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene phyA, protease-resistance phytase gene, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Pichia pastoris strain GS115 with secretion to culture supernatant Penicillium sp.

Protein Variants

Protein Variants Comment Organism
L151S the mutation enhances the activity in the range of 37-70°C and pH 2.5-7.0 by facilitating the interaction between the substrate and the catalytic centre Penicillium sp.
additional information replacements of G56E, L65F, Q144H, and L151S improved the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures Penicillium sp.
N354D the substitution influences the pH profile by weakening the bondage with the side chain of D353, which causes a pKa shift of the catalytic centre Penicillium sp.
T11A/G56E/L65F/Q144H/L151S mutagenesis by Mn2+-dITP random mutation method, the mutant shows improved thermal stability and optimal temperature and pH compared to the wild-type enzyme, the mutant shows high resistance to pepsin Penicillium sp.
T11A/H37Y/G56E/L65F/Q144H/L151S/N354D mutagenesis by Mn2+-dITP random mutation method, the mutant shows improved thermal stability and optimal temperature and pH compared to the wild-type enzyme, the mutant shows high resistance to pepsin Penicillium sp.

Organism

Organism UniProt Comment Textmining
Penicillium sp. A2TEY6 gene phyA; protease-resistance phytase gene phyA
-

Purification (Commentary)

Purification (Comment) Organism
secreted recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 culture supernatant Penicillium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
32.76
-
wild-type enzyme, pH 5.5-6.0, 37°C Penicillium sp.
133.3
-
mutant T11A/G56E/L65F/Q144H/L151S, pH 5.5-6.0, 37°C Penicillium sp.
136.6
-
mutant T11A/H37Y/G56E/L65F/Q144H/L151S/N354D, pH 4.8, 37°C Penicillium sp.
145.9
-
mutant T11A/G56E/L65F/Q144H/L151S, pH 5.5-6.0, 50°C Penicillium sp.
150.4
-
mutant T11A/H37Y/G56E/L65F/Q144H/L151S/N354D, pH 4.8, 50°C Penicillium sp.

Synonyms

Synonyms Comment Organism
protease-resistant phytase
-
Penicillium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37 55 broad optimum, mutant T11A/G56E/L65F/Q144H/L151S Penicillium sp.
37 50 broad optimum, mutant T11A/H37Y/G56E/L65F/Q144H/L151S/N354D Penicillium sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 60 temperature profiles of wild-type and mutant enzymes, overview Penicillium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37 60 temperature profiles of wild-type and mutant enzymes, overview Penicillium sp.
100
-
5 min, mutant T11A/G56E/L65F/Q144H/L151S retains 72,81% of initial activity, and mutant T11A/H37Y/G56E/L65F/Q144H/L151S/N354D retains 92.43% of initial activity Penicillium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.8
-
mutant T11A/H37Y/G56E/L65F/Q144H/L151S/N354D Penicillium sp.
5.5 6 wild-type enzyme and mutant T11A/G56E/L65F/Q144H/L151S Penicillium sp.

pH Range

pH Minimum pH Maximum Comment Organism
3.5 9 pH profiles of wild-type and mutant enzymes, no activity of mutant enzymes above pH 7.5, overview Penicillium sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.5 9 pH profiles of wild-type and mutant enzymes, no activity of mutant enzymes above pH 7.5, overview Penicillium sp.

General Information

General Information Comment Organism
additional information replacements of G56E, L65F, Q144H, and L151S improve the thermal stability of the protein by increasing new hydrogen bonds among the adjacent secondary structures Penicillium sp.