Introduction:

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

which this occurred had not been identified.

In the 19th century, when studying the fermentation of sugar to alcohol

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

"alcoholic fermentation is an act correlated with the life and organization

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

was used to refer to chemical activity produced by living organisms.

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

discovery of cell-free fermentation". Following Buchner's example, enzymes are usually

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

atomic level of detail.

Essentially an enzyme is a protein that speeds up a chemical reaction in a living organism. An

enzyme acts as catalyst for specific chemical reactions, converting a specific set of reactants into

specific products. Without enzymes, life as we know it would not exist.

Method & Procedure:

See Handout

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

would have to be extracted and their chemical composition determined.

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

can be said that the enzymes are deactivated at low temperatures.

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