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Literature summary for 3.4.23.4 extracted from

  • Wang, N.; Wang, K.Y.; Li, G.; Guo, W.; Liu, D.
    Expression and characterization of camel chymosin in Pichia pastoris (2015), Protein Expr. Purif., 111, 75-81.
    View publication on PubMed
Search for more literature for 3.4.23.4

Activating Compound

Activating Compound Comment Organism Structure
additional information when subjected to a low pH, recombinant prochymosin is converted into mature and active chymosin Camelus dromedarius

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris strain GS115 Camelus dromedarius

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ maximum milk clotting activity is detected with 20-40 mM Ca2+ Camelus dromedarius

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 x * 40000, active chymosin, SDS-PAGE Camelus dromedarius
42000
-
 x * 42000, deglycosylated recombinant enzyme, SDS-PAGE Camelus dromedarius
45000
-
 x * 45000, glycosylated recombinant enzyme, SDS-PAGE Camelus dromedarius

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
kappa-casein + H2O Camelus dromedarius
-
 ?
-
 ?
additional information Camelus dromedarius does not cleave alpha-casein and beta-casein ?
-
 ?

Organism

Organism UniProt Comment Textmining
Camelus dromedarius Q9GK11
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Camelus dromedarius

Storage Stability

Storage Stability Organism
0-20°C, at pH 5.5, 8 h, no loss of activity Camelus dromedarius
40°C, at pH 5.5, 8 h, 37.5% residual activity Camelus dromedarius
50°C, at pH 5.5, complete loss of activity Camelus dromedarius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
kappa-casein + H2O
-
 Camelus dromedarius ?
-
 ?
additional information does not cleave alpha-casein and beta-casein Camelus dromedarius ?
-
 ?
skim milk + H2O
-
 Camelus dromedarius ?
-
 ?

Subunits

Subunits Comment Organism
? x * 40000, active chymosin, SDS-PAGE Camelus dromedarius
? x * 42000, deglycosylated recombinant enzyme, SDS-PAGE Camelus dromedarius
? x * 45000, glycosylated recombinant enzyme, SDS-PAGE Camelus dromedarius

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45 55 optimum for milk clotting activity Camelus dromedarius

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
35 60 relative activity of 50% is observed at temperatures of 35°C and 60°C. Chymosin activity completely ceases below 20°C or above 70°C Camelus dromedarius

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
 50 after 8 h of incubation, between 0 and 20°C the enzyme shows 100% activity, while at 30°C and 40°C 70% and 35% is retained, respectively. The enzyme is inactive after 8 h at 50°C Camelus dromedarius

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 optimum for milk clotting activity Camelus dromedarius

pH Range

pH Minimum pH Maximum Comment Organism
5.1 6.7 at pH 5.1, the relative clotting activity decreases to 50% and further declines to 17% and 10% at pH 5.6 and pH 6.7, respectively Camelus dromedarius

pH Stability

pH Stability pH Stability Maximum Comment Organism
2.5 6.5 the recombinant enzyme is highly active and stable over a wide pH range (from 2.5 to 6.0) at 20°C for 8 h. Relative clotting activity declines when the recombinant chymosin is kept at a pH value above 6.0. No detectable clotting activity at pH 6.5 Camelus dromedarius