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Literature summary for 3.4.23.20 extracted from

  • Alhelli, A.; Manap, M.; Mohammed, A.; Mirhosseini, H.; Suliman, E.; Shad, Z.; Mohammed, N.; Hussin, A.
    Response surface methodology modelling of an aqueous two-phase system for purification of protease from Penicillium candidum (PCA 1/TT031) under solid state fermentation and its biochemical characterization (2016), Int. J. Mol. Sci., 17, 1872 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.20

Application

Application Comment Organism
food industry the enzyme is used in the dairy industry such as in accelerated cheese ripening Penicillium candidum

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 23% residual activity at 10 mM Penicillium candidum
EDTA 7% residual activity at 10 mM Penicillium candidum
Fe3+ complete inhibition at 10 mM Penicillium candidum
K+ 85% residual activity at 10 mM Penicillium candidum
Mg2+ 31% residual activity at 10 mM Penicillium candidum
Mn2+ 98% residual activity at 10 mM Penicillium candidum
additional information not inhibited by phenylmethylsulfonyl fluoride Penicillium candidum
SDS 33% residual activity at 10 mM Penicillium candidum
Zn2+ 92% residual activity at 10 mM Penicillium candidum

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 112% activity at 5 mM Penicillium candidum
Mn2+ 110% activity at 5 mM Penicillium candidum
Na+ 136% activity at 5 mM Penicillium candidum
Zn2+ 122% activity at 5 mM Penicillium candidum

Organism

Organism UniProt Comment Textmining
Penicillium candidum
-
-
-
Penicillium candidum PCA 1/TT031
-
-
-

Purification (Commentary)

Purification (Comment) Organism
aqueous two-phase system system using 9% (w/v) PEG 8000, 5.2% (w/v) NaCl, and 15.9% (w/v) sodium citrate Penicillium candidum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
azocasein + H2O
-
 Penicillium candidum ?
-
 ?
azocasein + H2O
-
 Penicillium candidum PCA 1/TT031 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 100000-140000, SDS-PAGE Penicillium candidum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Penicillium candidum

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4 50 the enzyme retains more than 80% of its initial activity at 4-50 °C. The activity is reduced to 52% at 60°C Penicillium candidum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Penicillium candidum

pH Range

pH Minimum pH Maximum Comment Organism
5 7 more than 77% activity between pH 5.0 and 7.0 Penicillium candidum

pH Stability

pH Stability pH Stability Maximum Comment Organism
8 9 the enzyme retains less than 35% activity after 1 h at pH 8.0-9.0 Penicillium candidum