3.4.23.4: chymosin
This is an abbreviated version!
For detailed information about chymosin, go to the full flat file.
Word Map on EC 3.4.23.4
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3.4.23.4
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milk
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casein
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cheese
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pepsin
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calf
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coagulation
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kappa-caseins
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rennet
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milk-clotting
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clot
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proteinases
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angiotensin
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hypertension
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aldosterone
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beta-caseins
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micelle
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whey
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pepsinogen
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renin
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ripening
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plasmin
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zymogen
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curd
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camel
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skim
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mucor
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cheddar
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pepstatin
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abomasum
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gelation
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cardunculus
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preruminant
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cynara
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progastricsins
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miehei
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fundic
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beta-cn
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food industry
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pusillus
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gastricsins
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urea-page
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s1-casein
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beta-lactoglobulin
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parasitica
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hypokalemia
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glycomacropeptide
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cheese-making
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rhizomucor
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3.4.23.1
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synthesis
- 3.4.23.4
- milk
- casein
-
cheese
- pepsin
-
calf
-
coagulation
- kappa-caseins
- rennet
-
milk-clotting
- clot
- proteinases
- angiotensin
- hypertension
- aldosterone
- beta-caseins
-
micelle
- whey
- pepsinogen
- renin
-
ripening
- plasmin
- zymogen
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curd
- camel
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skim
- mucor
-
cheddar
- pepstatin
- abomasum
-
gelation
- cardunculus
-
preruminant
-
cynara
- progastricsins
- miehei
-
fundic
-
beta-cn
- food industry
- pusillus
- gastricsins
-
urea-page
-
s1-casein
- beta-lactoglobulin
- parasitica
- hypokalemia
- glycomacropeptide
-
cheese-making
- rhizomucor
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3.4.23.1
- synthesis
Reaction
Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single Ser-Phe105-/-Met-Ala bond in kappa-chain of casein =
Synonyms
CHY-MAX, CHY-MAX 200, chymase, chymosin, chymosin A, chymosin B, CYM, EC 3.4.4.3, More, Preprorennin, prochymosin, rCH, rennin
ECTree
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Temperature Stability
Temperature Stability on EC 3.4.23.4 - chymosin
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0 - 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
25
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most stable at pH 5.0, denaturation can be fitted to the two-state irreversible model
25 - 50
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transgenic chymosin loses activity slightly faster than abomasal enzyme and recombinant enzyme
35 - 55
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the enzyme activity remains stable after 30 min at 35-55°C and drops to about 20% after 30 min at 60°C
4 - 70
after 1 h at 4, 10, 20, 30, 40, 50 and 60°C, the enzyme shows about 99%, 80%, 70%, 60%, 60%, 55% and 40% residual activity, respectively. The enzyme is inactive after 1 h at 70°C
40
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the enzyme is stable until 40°C for 30 min while losing 40 and 80% of its activity after incubation at 45 and 50°C for 30 min, respectively
40 - 55
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no residual clotting activities at temperatures higher than 55°C
50 - 60
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chymosin is stable up to 50°C and a relative milk-clotting activity of 50% is recorded when the temperature is raised to 60°C
55
56
60
60 - 100
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incubation at 60°C for 2 min 30 s decreases the mil clotting activity of the enzyme. A 2 min heating at 80 and 100°C totally inactivates the enzyme
75
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it is not possible to coagulate milk with chymosin at 75°C due to its loss of activity
additional information
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the enzyme undergoes irreversible, highly scan-rate-dependent thermal denaturation under all the experimental conditions investigated (pH 2-12, 20-50°C). Between pH 3.0 and 7.0, only one endotherm characterizes the thermal denaturation of the enzyme. Upon reaching pH 7.5, the denaturation is characterized by two endotherms
55
stable up to 55°C, more thermostable than cattle chymosin and equally stable as buffalo chymosin
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chymosin-mediated hydrolysis of alphas1 casein is slower in cheeses treated at 56°C
56
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chymosin-mediated hydrolysis of alphas1 casein is slower in cheeses treated at 56°C
60
the recombinant enzyme retains 42% of relative milk clotting activity at 60°C