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As early as the late 1700s and early 1800s, the digestion of meat by stomach secretions and the
conversion of starch to sugars by plant extracts and saliva were known. However, the mechanism by
by yeast, Louis Pasteur came to the conclusion that this fermentation was
catalysed by a vital force contained within the yeast cells called "ferments",
which were thought to function only within living organisms. He wrote that
cells."
In 1878, German physiologist Wilhelm Kühne first used the term enzyme, which
comes from Greek ενζυμον, "in leaven", to describe this process. The word enzyme
was used later to refer to nonliving substances such as pepsin, and the word ferment
In 1897, Eduard Buchner began to study the ability of yeast extracts that lacked any
living yeast cells to ferment sugar. In a series of experiments at the University of Berlin, he
found that the sugar was fermented even when there were no living yeast cells in the
mixture. He named the enzyme that brought about the fermentation of sucrose "zymase". In
1907, he received the Nobel Prize in Chemistry "for his biochemical research and his
named according to the reaction they carry out. Typically, to generate the name of an enzyme, the
suffix -ase is added to the name of its substrate or the type of reaction.
Having shown that enzymes could function outside a living cell, the next step was to determine
their biochemical nature. Many early workers noted that enzymatic activity was associated with
proteins, but several scientists argued that proteins were merely carriers for the true enzymes and that
proteins per se were incapable of catalysis. However, in 1926, James B. Sumner showed that the
enzyme urease was a pure protein and crystallized it; Sumner did likewise for the enzyme catalase in
1937. The conclusion that pure proteins can be enzymes was definitively proved by John Howard
Northrop and Wendell Meredith Stanley, who worked on the digestive enzymes pepsin (1930), trypsin
and chymotrypsin. These three scientists were awarded the 1946 Nobel Prize in Chemistry.
This discovery that enzymes could be crystallized eventually allowed their structures to be solved
by x-ray crystallography. This was first done for lysozyme, an enzyme found in tears, saliva and egg
whites that digests the coating of some bacteria; the structure was solved by a group led by David
Chilton Phillips and published in 1965. This high- resolution structure of lysozyme marked the
beginning of the field of structural biology and the effort to understand how enzymes work at an
enzyme acts as catalyst for specific chemical reactions, converting a specific set of reactants into
Results:
Test Tube Number Test Tube Contents Observation of Reaction Flame test; Oxygen or
Hydrogen
1 Liver + Hydrogen Peroxide Began to fizz and turn Oxygen
white, splint lit
2 Yeast + Hydrogen Peroxide Yeast turned white and NR
fizz formed
3 Potato + Hydrogen
Peroxide Fizz formed + white mousse NR
formed at top.
4 Charcoal + Hydrogen Peroxide Became grey, fizz Oxygen (lit)
formed, charcoal was
bouncy
5 Hydrogen Peroxide + 0.1g of NR NR
Sand
6 Hydrogen Peroxide + 0.1g of Turned black and bubbles NR
Manganese Dioxide formed
7 Hydrogen Peroxide (old) + old NR (Hydrogen Peroxide NR
Liver and new Liver already broken down)
8 Hydrogen Peroxide (old) with Fizzed rapidly Oxygen (lit)
old Liver and new Hydrogen
Peroxide
9 Heated Liver + Hydrogen When heated, liver NR
Peroxide shrivelled and turned
brown.
Discussion:
Charcoal could not be an enzyme because it is an element and it has been produced by very
high temperatures that would destroy enzymes. Manganese dioxide is a catalyst because it speeds the
rate of a chemical reaction and is not used up in the reaction. It lowers the activation energy necessary
for the reaction to take place. It is an inorganic compound. It is not an enzyme. Enzymes are proteins
that are produced by living organisms. Enzymes can act as catalysts, they can speed or slow a reaction
in the body.
There seems no fundamental reason why yeast and liver should not have different enzymes
which catalyse the decomposition of hydrogen peroxide. To be certain on this point, the enzymes
The temperature is directly linked to the enzyme activity. Greater the temperature, greater the
kinetic energy and greater the enzyme activity. Increase in temperature results in more energetic
collusion and increase internal energy of molecules in the system. It also increases number of collisions
per unit time of the system. At low temperatures the rate of enzyme reaction is very slow. The
molecules have low kinetic energy and collisions between them are less frequent and even if they do
collide the molecules do not posses the minimum activation energy required for the reaction to occur. It
Work Cited:
− http://en.wikipedia.org/wiki/Louis_Pasteur
− http://en.wikipedia.org/wiki/Wilhelm_Kühne
− http://en.wikipedia.org/wiki/Eduard_Buchner
− http://en.wikipedia.org/wiki/Nobel_Prize_in_Chemistry
− http://en.wikipedia.org/wiki/Zymase
− http://en.wikipedia.org/wiki/James_B._Sumner
− http://www.yourdictionary.com/urease
− http://en.wikipedia.org/wiki/John_Howard_Northrop
− http://en.wikipedia.org/wiki/Wendell_Meredith_Stanley
− http://en.wikipedia.org/wiki/X-ray_crystallography
− http://en.wikipedia.org/wiki/David_Chilton_Phillips