The Effect of Temperature on the Activity of Rennin in Milk
Aim:
To find out what effect different temperatures have on the enzyme,
rennin, in milk.
Introduction
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]
[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.
[IMAGE]
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
The Shipping Manager’s activities required a different approach. He used coordination through formal hierarchy. The Shipping Manager assigned the Team Leader tasks that required more supervision and resources. He gave an order to the Team Leader who divided it among his Pullers. The Pullers would enter the tunnel, assemble the order from the various coolers and send it down the track to the awaiting loaders. The Loaders would remove their assigned color-coded stacks and put them in the appropriate trucks for delivery. This process did not require special training but it did require more direction from the Supervisors than the warehouse functions.
· I predict that the enzyme will work at its best at 37c because that
The Effect of Temperature on an Enzyme's Ability to Break Down Fat Aim: To investigate the effect of temperature on an enzyme’s (lipase) ability to break down fat. Hypothesis: The graph below shows the rate increasing as the enzymes get closer to their optimum temperature (around 35 degrees Celsius) from room temperature. The enzyme particles are moving quicker because the temperature increases so more collisions and reactions occur between the enzymes and the substrate molecules. After this the graph shows the rate decreasing as the enzymes are past their optimum temperature (higher than). They are getting exposed to temperatures that are too hot and so the proteins are being destroyed.
Catalysis occurs because substance S fits precisely into surface of the enzyme E, so this reaction and no others are speeded up. Diagram showing an enzyme catalsying the breakdown of its substrate into two product molecules. As can be seen from the diagram, if the enzyme changes shape, the active site (the area where the substrate reacts) would no longer be able to fit the substrate. This would mean the enzyme would lose its effect; the substrate would not break down.
needed to activate the reacting molecules. They are specific that usually act on only one type of substrate, so each of them just. perform one particular reaction. Furthermore, only a small amount of enzyme is needed every time to speed up a reaction. Enzymes are globular proteins that have a precise three-dimensional structure.
The [ES] complex can then undergo two different pathways; the complex can dissociate to [E] and [S], at a rate of k or it can shift equilibrium to the left with a rate constant of k2 to form [E] and product [P]1. In this model, the breakdown of the ES complex to yield P is the overall rate-limiting step. Three assumptions of a Michaelis-Menton plot are that a specific [ES] complex in rapid equilibrium between [E] and [S] is a necessary intermediate, the amount of substrate is more than the amount of enzyme so the [S] remains constant, and that this plot follows steady state assumptions. Steady state assumptions states that the intermediate stays the same concentration even if the starting materials and products are constantly changing.2 The rapid equilibrium between enzyme and substrate, and the enzyme-substrate complex yields a mathematical description regarded as the Michaelis-Menton
Louis Pasteur had been studying fermentation to explain why dairy and meat was going bad. He didn’t believe that it was spontaneous but rather there had to be a scientific explanation. When working with grapes and understanding that yeast was the driving agent in fermentation of grapes, he hypothesized that if you can protect grapes from fermentation, that people could be protected from infectious disease.
The three-dimensional contour limits the number of substrates that can possibly react to only those substrates that can specifically fit the enzyme surface. Enzymes have an active site, which is the specific indent caused by the amino acid on the surface that fold inwards. The active site only allows a substrate of the exact unique shape to fit; this is where the substance combines to form an enzyme- substrate complex. Forming an enzyme-substrate complex makes it possible for substrate molecules to combine to form a product. In this experiment, the product is maltose.
"The Species of the Secondary Protein Structure. Virtual Chembook - Elmhurst College. Retrieved July 25, 2008, from http://www.cd http://www.elmhurst.edu/chm/vchembook/566secprotein.html Silk Road Foundation. n.d. - n.d. - n.d.
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.
Changes in pH lead to the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place. The enzyme begins to lose. its functional shape, particularly the shape of the active site, such. that the substrate will no longer fit into it, the enzyme is said to. be denatured.
Varying Concentration of Rennin and Its Effect on the Goagulation Time of Milk Scientific Knowledge Enzymes Enzymes are large molecules, which are protein in nature. They are biological catalysts that speed up chemical reactions in the body. They operate by a "lock and key" method. The Enzyme has a certain "lock" (active site) that only a specified substrates "key" will fit into.
There is a great promise of application of ice structuring proteins in food that are frozen. Ice structuring proteins can inhibit re-crystallization during freezing storage, transport and thawing, thus preserving food texture by retarding cellular damage and minimal loss of nutrients (for fruit and vegetables like strawberries, raspberries, tomatoes) by reducing drip (Griffith and Ewart, 1995, Feeney and Yeh, 1998, Breton et al., 2000, Wang, 2000). Re-crystallization in frozen food occurs when temperature fluctuates during storage or transit, resulting in coarse texture. This technique is well suited to ice cream (Warren et al., 1992). Ice structuring proteins also find use in chilled and frozen meat, where large ice crystals may form intracellularly, resulting in drip and loss of nutrition during thawing. Since ice structuring proteins are located extracellularly in freeze-tolerant organism, these proteins can be added to food by physical means such as mixing, injection, soaking, or vacuum infiltration, or even by gene transfer (Venketesh and Dayananda, 2008).
Each protein is a large complex molecule; these molecules are made up of. of a string of amino acids. There are 20 different amino acids that occur naturally to form proteins and they all have the same basic structure. The. The 20 amino acids the body needs can be linked in.
One vital process in the human body observed in chemistry is the idea of chemical kinetics. Chemical kinetics is the study of the rate of reactions, or how fast reactions occur.1 Three factors that affect chemical kinetics are concentration, temperature, and catalysis. As the concentration of a substance increases, the rate of the reaction also increases.1 This relationship is valid because when more of a substance is added in a reaction, it increases the likelihood that the