The Effect of Temperature on the Activity of Rennin in Milk

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The Effect of Temperature on the Activity of Rennin in Milk


To find out what effect different temperatures have on the enzyme,

rennin, in milk.


An enzyme is a biological catalyst. It speeds up a reaction by

lowering the activation energy required to start the reaction. It

speeds up a reaction, but remains unchanged unless certain limiting

factors are introduced. It is composed of polymers of amino acids. An

enzyme has an optimum pH and temperature. When an enzyme is at its

optimum conditions, the rate of reaction is the fastest. In their

globular structure, one or more polypeptide chains twist and fold,

bringing together a small number of amino acids to form the active

site, or the location on the enzyme where the substrate binds and the

reaction takes place. An enzyme has an active site, which has a unique

shape into which only a substrate of the exact same unique shape can

fit. When this substrate fits into the active site, it forms an

enzyme-substrate complex. This means that an enzyme is specific. The

bonds that hold enzymes together are quite weak and so are easily

broken by conditions that are very different when compared with their

optimum conditions. When these bonds are broken the enzyme, along with

the active site, is deformed, thus deactivating the enzyme. This is

known as a denatured enzyme. The primary structure is the sequence of

amino acids that make up a polypeptide chain. 20 different amino acids

are found in proteins. The exact order of the amino acids in a

specific protein is the primary sequence for that protein.


[IMAGE]Protein secondary structure refers to regular, repeated

patterns of folding of the protein backbone. The two most common

folding patterns are the alpha helix and the beta sheet.


In this experiment, the enzyme rennin will be used. Rennin is a

coagulating enzyme occurring in the gastric juice of the calf, forming

the active principal of rennet and able to curdle

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