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Literature summary for 3.4.23.29 extracted from

  • Kawai, M.; Terada, O.
    Studies on the milk-clotting enzymes produced by basidiomycetes. Part IV. Comparisons of some properties of crystalline acid proteinases produced by the parent and mutant strains of Irpex lacteus Fr (1976), Agric. Biol. Chem., 40, 1463-1469.
No PubMed abstract available
Search for more literature for 3.4.23.29

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme from Fr. KY 2901 and mutant enzymes produced by irradiation with UV-light Irpex lacteus

Inhibitors

Inhibitors Comment Organism Structure
Fe3+
-
 Irpex lacteus
sodium lauryl sulfate
-
 Irpex lacteus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
 Polyporus tulipiferae, 3U-39, gel filtration Irpex lacteus
33500
-
 Polyporus tulipiferae 2U-148, gel filtration Irpex lacteus
34000
-
 Polyporus tulipiferae KY 2901 and U-212, gel filtration Irpex lacteus

Organism

Organism UniProt Comment Textmining
Irpex lacteus
-
 formerly Irpex lacteus
-
Irpex lacteus
-
 Fr. KY 2901 and mutant enzymes U-212, 2U-148 and 3U-39 produced by irradiation with UV-light
-

Purification (Commentary)

Purification (Comment) Organism
-
 Irpex lacteus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information milk clotting activity Irpex lacteus ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 pH 4.5, 15 min, stable up to Irpex lacteus
60
-
 pH 4.5, 15 min, complete inactivation Irpex lacteus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5
-
-
 Irpex lacteus

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 6 stable Irpex lacteus