curds casein in the stomach
Renin is an enzyme secreted by the kidneys (from specialized cells called the juxtaglomerular aparatus) whose function is to aid in the conversion of angiotensinogen into angiontensinogen II. Renin controls blood pressure by means of extracellular volume mediation and vasoconstriction
angiotensinogen
Rennin is very ineffective at 0 degrees. Its optimum temperature which it works in is body temperature (37oC). If the enzyme is heated up to 70 degrees then it will denature and have no effects at all.
its all to do with the milk proteins, caseins. the rennin makes them coagulate. you probbably never got any of that, im doing a planning task and its hard.
Rennin, also known as chymosin, is an enzyme found in the stomach lining of calves. It can be isolated from the stomachs of calves or produced using biotechnology. Rennin is used in cheese making to coagulate milk, separating it into curds and whey.
Yes, rennin is considered a biological catalyst because it acts to speed up the coagulation of milk proteins during the cheesemaking process. It primarily helps to convert milk protein (casein) into solid curds, aiding in the formation of cheese.
CI rennin?
Type your answer here.how to make rennin
rennin
When the temperature is raised to the boiling point, the enzyme rennin will denature, meaning it will lose its shape and function due to the high heat. This will render the enzyme ineffective in catalyzing reactions.
Robert Tigerstedt in 1898
No. Rennin is derived fom rennet, which comes from a cows stomach.
In the stomach
angiotensinogen
The function of rennin is to curdle milk proteins by converting the soluble protein caesinogen into the insoluble protein caesinogen. If the new born mammal is unable to produce rennin, then the soluble milk proteins would just pass through the stomach into the duodenum like water. This is bad because the milk proteins would not be able to get digested by the pepsin. However, if there is rennin, the converted insoluble milk proteins would be abe to stay in the stomach long enough for the pepsin to digest it into polypeptides.
No, optimal pH for pepsin is around 2.0 (acidic environment) while optimal pH for rennin is around 6.5-6.7 (slightly acidic to neutral environment). Each enzyme has a specific pH range at which it functions most efficiently due to its unique structure and function.
the optimal pH for rennin is around 1-2, as this closely resembles the acidic environment of the stomach where rennin is most commonly found. However rennin also works at neutral pH, although at a much lower level of reaction. This is necessary because sometimes the stomach is diluted by outside materials.
rennin