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Literature summary for 3.4.21.25 extracted from

  • Gagaoua, M.; Ziane, F.; Nait Rabah, S.; Boucherba, N.; Ait Kaki El-Hadef El-Okki, A.; Bouanane-Darenfed, A.; Hafid, K.
    Three phase partitioning, a scalable method for the purification and recovery of cucumisin, a milk-clotting enzyme, from the juice of Cucumis melo var. reticulatus (2017), Int. J. Biol. Macromol., 102, 515-525 .
    View publication on PubMed
Search for more literature for 3.4.21.25

Application

Application Comment Organism
food industry milk-clotting enzyme for cheese-making Cucumis melo

Inhibitors

Inhibitors Comment Organism Structure
Cd2+ about 8% residual activity at 5 mM Cucumis melo
Co2+ about 15% residual activity at 5 mM Cucumis melo
EDTA 68% residual activity at 2 mM Cucumis melo
EGTA 72% residual activity at 2 mM Cucumis melo
Fe2+ about 55% residual activity at 5 mM Cucumis melo
additional information not inhibited by iodoacetamide and pepstatin Cucumis melo
phenylmethylsulfonyl fluoride 7.04% residual activity at 0.5 mM Cucumis melo
Zn2+ about 10% residual activity at 5 mM Cucumis melo

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the enzyme activity is 2.35fold increased at 5 mM Ca2+. 2.5-10 mM Ca2+ increase the half-life of the enzyme at 35-55°C Cucumis melo
Mg2+ about 180% activity at 5 mM MgSO4 Cucumis melo
Mn2+ about 160% activity at 5 mM MnSO4 Cucumis melo
additional information not influenced by Na+ and K+ Cucumis melo

Organism

Organism UniProt Comment Textmining
Cucumis melo
-
 Cucumis melo var. reticulatus
-

Purification (Commentary)

Purification (Comment) Organism
60% ammonium sulfate precipitation with 1.0:1.25 ratio of crude extract:t-butanol at pH and temperature of 8.0 and 20°C Cucumis melo

Source Tissue

Source Tissue Comment Organism Textmining
fruit juice
-
 Cucumis melo
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.71
-
 crude extract, at pH 8.0 and 20°C Cucumis melo
3.26
-
 after 4.61fold purification, at pH 8.0 and 20°C Cucumis melo

Storage Stability

Storage Stability Organism
-20°C, 10 days, 1.3% loss of milk-clotting activity Cucumis melo
25°C, 10 days, 37% loss of milk-clotting activity Cucumis melo
25°C, 3 weeks, 95.4% loss of milk-clotting activity Cucumis melo
4°C, 10 days, 85.4% loss of milk-clotting activity Cucumis melo
4°C, 3 weeks, 20% loss of milk-clotting activity Cucumis melo

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bovine casein + H2O
-
 Cucumis melo L-tyrosine + ?
-
 ?
bovine skimmed milk powder + H2O
-
 Cucumis melo ?
-
 ?

Subunits

Subunits Comment Organism
? x * 68400, SDS-PAGE Cucumis melo

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60 70
-
 Cucumis melo

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 80 about 70% activity 40°C, about 85% activity 50°C, 100% activity at 60-70°C, about 60% activity 80°C Cucumis melo

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 50 the enzyme remains stable for 2 h at 20-50°C. After 2 h at 60, 70, 80, and 90°C, the enzyme shows about 80%, 68%, 15% and 5% residual activity, respectively. The enzyme shows half-lives of 123, 104, 87, 64 and 32 min at 35°C, 40°C, 45°C, 50°C, and 55°C, respectively Cucumis melo

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Cucumis melo

pH Range

pH Minimum pH Maximum Comment Organism
7 11 the enzyme retains more than 80% proteolytic activity in the range of pH 7.0-11.0 Cucumis melo

pI Value

Organism Comment pI Value Maximum pI Value
Cucumis melo isoelectric focusing
-
 8.7