Digestive System

CHAPTER I
INTRODUCTION
A. Background
The digestive system is made up of the digestive tract a series of hollow organs joined in a long, twisting tube from the mouth to the anus and other organs that help the body break down and absorb food (see figure). Organs that make up the digestive tract are the mouth, esophagus, stomach, small intestine, large intestine also called the colon rectum, and anus. Inside these hollow organs is a lining called the mucosa. In the mouth, stomach, and small intestine, the mucosa contains tiny glands that produce juices to help digest food. The digestive tract also contains a layer of smooth muscle that helps break down food and move it along the tract.
When you eat foods—such as bread, meat, and vegetables—they are not in a form that the body can use as nourishment. Food and drink must be changed into smaller molecules of nutrients before they can be absorbed into the blood and carried to cells throughout the body. Digestion is the process by which food and drink are broken down into their smallest parts so the body can use them to build and nourish cells and to provide energy.

B. Purpose
To know the method of amylase enzyme process.
C. Benefit
1. Student able to know the factor that influence of amylase enzyme process.
2. Student able to know the amylase enzyme has role in digestives system.



CHAPTER II
PREVIEW OF LITERATURE
The processes of digestion and absorption are undertaken in the midget region of the gastrointestinal system- this is region which constitutes the first part of the intestine. By this stage, food has been broken down by mechanical (i.e. teeth and mixing) means and is known as chime. The digestive processed which occur from this stage onwards are enzymatic, and the aim is to break the major components of food-stuffs (i.e. carbohydrates, protein and lipids) down into their constituent component which can then be absorbed and utilized by the animal. (It should be remembered that there are a variety of other nutrients required by animals, e.g. minerals, vitamins and so on. A full description of the requirements and roles of these substances is beyond the scope of this book) (Kay, 1998).
Digestion involves mixing food with digestive juices, moving it through the digestive tract, and breaking down large molecules of food into smaller molecules. Digestion begins in the mouth, when you chew and swallow, and is completed in the small intestine. The large, hollow organs of the digestive tract contain a layer of muscle that enables their walls to move. The movement of organ walls can propel food and liquid through the system and also can mix the contents within each organ. Food moves from one organ to the next through muscle action called peristalsis (Anonyma, 2010).
According to the Campbell (2004), an enzyme that accelerates the hydrolysis biokatalisator in digestion, so as the enzyme catalyst must be:
a. Be effective (which is needed in very small amounts compared with
b. the amount of substrate).
c. Did not participate in the reaction process (the nature and amount does not change).
d. Be recouped by the end of the reaction.
e. Specific.
According to Kartolo (1993) that biokatalisator the enzyme is to strengthen the process of hydrolysis in digestion, because it was a catalytic enzyme should be effective (which is needed in very small amount compare with number of substrates), did not participate in the reaction process (the nature and amount does not change), to be recouped at the end of the reaction, and be specific. In addition, the enzyme has the properties of physics and chemistry as follows:
1. Solubility : well soluble in glycerol, and mixtures of water with glycerol.
slightly soluble in dilute alcohol and insoluble in absolute alcohol.
2. Precipitation: can be done with the addition of absolute alcohol.
3. Has a colloidal nature, which may be through a semi permeable membrane such as intestinal mucosal wall.
4. Sensitive to temperature: the reaction is accelerated with increasing temperature up to certain limits.
5. Influenced by pH, each enzyme has a job at a certain pH range.
• Pepsin, pH: 1-3; optimum pH: 1,2-1,8
• Trypsin, pH: 6.8 to 9; pH optimum: 8.2
6. May be susceptible to denaturation, i.e. loss of biocatalisator activity, because the occurrence of conformational changes (composition) polypeptide chains which have no primary structure, and are reversible.
In general, food in the digestive tract is divided into 4 sections, they are; Section that receives the food. This is the initial part of the digestive tract of food is also a place to enter and swallowing food, including mouth, pharynx, beaks, teeth, tongue and salivary glands. Parts that move and store food. Esophagus of animals and some other invertebrates play a role in moving the bolus by peristalsis from the mouth or pharynx space. That digests the food. In general, the process of digestion in vertebrates and some invertebrates which occur in 2 places in the stomach and the intestines. Part that absorbs the water and remove excess food. The last part of the digestive tract of food in general associated with the absorption and elimination in a way that does not change the food is digested into feces (Wiwi, 2006).
Amylase is an enzyme that breaks starch down into sugar. Amylase is present in human saliva, where it begins the chemical process of digestion. Foods that contain much starch but little sugar, such as rice and potato, taste slightly sweet as they are chewed because amylase turns some of their starch into sugar in the mouth. The pancreas also makes amylase (alpha amylase) to hydrolyze dietary starch into disaccharides and trisaccharides which are converted by other enzymes to glucose to supply the body with energy. Plants and some bacteria also produce amylase. As diastase, amylase was the first enzyme to be discovered and isolated. Specific amylase proteins are designated by different Greek letters. All amylases are glycoside hydrolyses and act on α-1,4-glycosidic bonds (Anonymb, 2010).
Cold temperature is similar to what cold blooded animals face in winter every year. The amylase cells which could not handle the cold died. Conversely the boiling presented conditions which amylase was not prepared to deal with. That the enzyme is denatured at high temperatures. Denatured amylase no longer catalyzes the hydrolysis of starch into glucose. In nature, extreme low temperatures often occur due to climate, yet extreme hot temperatures aren't prevalent. It is possible that enzymes can not withstand extreme high temperatures because they did not evolve to do so. Perhaps amylase evolved to handle low temperatures because those who did not were denatured thus never passing on their characteristics (Anonymc, 2010).
Amylase is an important metabolic enzyme. Its function is to catalyze the hydrolysis of starch into glucose. This particular enzyme, which is found in all mammals, speeds up specific digestive processes which take place along the digestive track running from the mouth to the small intestines. Amylase's essential role in digestion makes it an attractive prospect for research. Enzyme denaturation usually leaves the enzyme without its catalytic functions. There are three factors which can denature an enzyme: temperature, pH, and ion concentration (Soewolo, 2003).

CHAPTER III
EXPERIMENT METHOD
A. Place and Time
Day/ date : Wednesday/ 7th April 2010
Time : 08.20 am until 10.50 am
Place : the 2nd floor of Biology laboratory, Mathematics and Science Faculty, State University of Makassar
B. Tools and Materials
1. Tools
a. Activity I (Influence of temperature to the amylase work)
1) 4 of reaction tube
2) Rack of reaction tube
3) Petri dish
4) Drop pipette
5) Bunsen burner
b. Activity II (Influence of pH to the amylase work)
1) 4 of reaction tube
2) Rack of reaction tube
3) Drop pipette
4) Bunsen burner
c. Activity III (Influence of substrate concentration to amylase work)
1) 12 of reaction tube
2) 3 of rack of reaction tube
3) Drop pipette
4) Bunsen burner


2. Materials
a. Activity I (Influence of temperature to the amylase work)
1) Salivary amylase preparation
2) Iodine lughole or reagent iodine solution
3) Matches
4) Paper
5) Aquadest
b. Activity II (Influence of pH to the amylase work)
1) Salivary amylase preparation
2) Buffer solution pH 4, pH 7, pH 9
3) Starch 1 %
4) Iodine lughole or reagent iodine solution
5) Matches
6) Aquadest
7) Paper
c. Activity III (Influence of substrate concentration to amylase work)
1) 12 of Reaction tube
2) Starch 5 %, 1 %, and 0.5 %
3) NaCl solution; 2%, 4%, 6%, and 8%
C. Work Procedure
1. Activity I (Influence of temperature to the amylase work)
a. Gave serial numbers for the fourth test tube and pour the preparation of amylase in the tubes 1, 2, 3 and 4.
b. Entered the amylase preparation 3 ml for each tube.
c. Placed the tube in a water bath 1 to 4° C, the tube 2 into the water bath 37° C, and tube 3 at 70° C water bath and the tube 4 at 25° C water bath as a control.
d. Added 5 ml of starch in each tube.
e. Shake for 5 minutes and place on rack tube.
f. Took a little sample of each mixture and place it on the Petri dish.
g. Added 2 drops of iodine reagent.
h. Took note of the result by giving a positive sign (+) for positive reaction to the color blue and the sign is negative (-) for negative reactions in red.


2. Activity II (Influence of pH to the amylase work)
a. Give the serial number into four test tubes and place on rack tube.
b. 3 ml of amylase preparations entered in each tube.
c. Added 3 ml of pH 4 buffer solution into the tubes 1, 3 ml of pH 7 buffer solution into the tube 2, 3 ml of buffer solution of pH 9 to the tube 3, and 3 ml of distilled water into the tube 4.
d. Shook and place it into the water bath temperature to 37 C for 10 minutes.
e. Added 1% starch solution into each tube.
f. Stir and let the bath for 5 minutes.
g. Grabbed sample at the time of 5 minutes, 15 minutes, and 30 minutes.
h. Starch hydrolysis test it by adding 2 drops of iodine reagent. Record the result.


3. Activity III (Influence of substrate concentration to amylase work)
a. Give the number on the 12 test tubes and place on rack tube.
b. Entered 1% starch solution into each tube 1-5 1 ml, 2 ml, 3 ml, 5 ml, 10 ml.
c. Then entered 5% starch solution into each tube 6-10 each 1 ml, 2 ml, 3 ml, 5 ml, 10 ml.
d. 5 ml of distilled water enter the tube 11 and 5 ml of alcohol on the tube 12.
e. Shook tube and heated in the Bunsen burner for 10 minutes at 37 C.
f. Saw the changes.



CHAPTER IV
OBSERVATION RESULT AND DISCUSSION
A. Observation Result
1. Activity I (Influence of temperature to the amylase work)
No. Tube Temperature Note Reaction
1. 1 4°C White- dark blue- dark blue, sediment +
2. 2 37°C White- dark blue – purple, black sediment +
3. 3 70°C White- dark blue- orange -
4. 4 25°C White – dark blue – black greenish, sediment +

2. Activity II (Influence of pH to the amylase work)
No. Tube First 5 minutes 10 minutes 30 minutes
1. 1 Pure Pure Turbid More turbid
2. 2 Pure Pure Turbid More turbid
3. 3 Pure Pure Turbid Turbid
4. 4 Pure Pure Pure Turbid


3. Activity III (Influence of substrate concentration to amylase work)
No. Tube/ Substrate Condition Changes
5 min 10 min 15 min 20 min 30 min
1. Starch 1% Pure Pure Less Turbid
2. 2 Turbid Turbid Turbid
3. 3 Turbid Turbid So Turbid
4. 4 Turbid Turbid Turbid
5. 5 Turbid Turbid Turbid
6. Starch 5% Pure Pure Less Turbid
7. 7 Turbid Pure Turbid
8. 8 Turbid Turbid Turbid
9. 9 Turbid Turbid Turbid
10. 10 Turbid Turbid Turbid
11. Aquadest Pure Turbid Turbid
12. Alcohol Pure Pure Turbid

B. Discussion
1. Activity I (Influence of temperature to the amylase work)
At the change of temperature, speed of reactions catalyzed by enzymes initially increased due to rising temperatures. Kinetic energy will increase at a complex of enzymes and substrates react. However, the increase in kinetic energy by increasing the temperature has an optimum limit. If the limit is exceeded, then the energy can be decided hydrogen bonds and hydrophobic weak-tertiary maintain secondary structure. At this temperature, the denaturation is accompanied by a decrease in enzyme activity as a catalyst will occur. The optimal temperature depends on the duration of the measurement of enzyme levels used to define it. Supposed to be at a temperature of 37°C is the temperature where the maximum enzyme activity. At this temperature the reaction should be the fastest. This occurs because the temperature is a normal human body temperature (optimum temperature of amylase enzyme salivary is 37°C). But in the experiment obtained the highest velocity of enzymatic reaction is at room temperature. This is probably because the temperature in the lab room is higher than normal room temperature (28°C) or perhaps because of incubation at 37°C imprecise or inaccurate. In the temperature interval 0°C-37°C, the enzymatic reaction velocity increases. After passing through the optimum temperature (37°C), the enzymatic reaction velocity decreases again.
2. Activity II (Influence of pH to the amylase work)
PH conditions can affect enzyme activity through the changing structures or changing the charge on the residue that functions in substrate binding or catalytic. In the curves obtained through experiments, can be seen that the enzyme salivary amylase has a pH optimum at pH 7, because at this pH is obtained a high enzyme activity (velocity of enzymatic reaction high). Generally, the enzymatic reaction velocity increases until it reaches the optimal pH and decreased after pH greater than pH optimum. At pH 8, the enzyme activity is inactive, but small (indicated by the enzymatic reaction of a small speed too). This is due, at pH less than 4, salivary amylase enzyme becomes inactive.
3. Activity III (Influence of substrate concentration to amylase work)
Enzyme activity is affected by enzyme levels. Enzyme activity and enzyme levels have a straight comparison of the relationship. This means that the greater the concentration of enzyme, the greater the faster the enzyme activity and enzyme catalyzed reactions. If the fixed substrate concentration and enzyme levels decreased, the enzyme catalyzed reaction velocity will decrease because the enzymes that are available are not enough to react with the substrate. More and more enzymes that bind to the substrate, increasing reaction speed and the more enzyme-substrate complex is formed. So any product that is formed more and more. At this time the experiment was made with a variety of enzyme solution to be able to compare the concentration of enzyme at various concentrations. Varying levels of an enzyme made by dilution with water. In the experiment results, the highest enzyme activity (the highest enzymatic reaction speed) should be obtained on the largest enzyme levels, ie when the saliva is not diluted. This caused a lot of enzymes that react with the substrate so that a high reaction speed and a lot of products produced. Declining levels of an enzyme, enzyme activity should be decreased.



CHAPTER V
CONCLUSION AND SUGGESTION
A. Conclusion
Enzymatic reaction speed will increase with increasing temperature until the optimum limit. After passing through the optimum temperature, the enzymatic reaction speed will be back down. Salivary enzyme amylase optimum temperature is 37 oC, the same as normal body temperature. Enzymatic reaction speed will increase with increasing temperature until the optimum limit. After passing through the optimum temperature, the enzymatic reaction speed will be back down. The optimum temperature of amylase enzymes contained in saliva is 37°C, the same as normal body temperature. The enzyme has maximum activity at pH optimum (optimum pH of salivary amylase enzyme is 9. The decrease or increase in pH affects enzyme activity.
B. Suggestion
1. I hope laboratory equipment can be completed, thus practicant can do observation well.
2. Assistant can give more again information about observation.
3. Practicans must do observation well.



BIBLIOGRAPHY
Anonyma. 2010. Your Digestive System and How It Works. http://digestive.niddk.nih.gov/ddiseases/pubs/yrdd/. Accessed on April 20th 2010
Anonymb. 2010. Amylase Enzyme: The Effects Of Temperature http://en.wikipedia.org/wiki/Amylase. Accessed on April 20th 2010
Anonymc. 2010. Amylase. http://www.allsands.com/science/amylaseenzymeh. Accessed on April 20th 2010
Campbell.Neil A, Reece, and Mitchell. 2004. Biologi Jilid 3 Edisi Kelima. Jakarta. Erlangga
Isnaeni, Wiwi. 2006. Fisiologi Hewan. Yogyakarta. Kanisius
Soewolo,dkk. 2003. Fisiologi Manusia. FMIPA Departemen Biologi. Universitas Negeri Malang
Suripto, Drs. 2009. Fisiologi Hewan. Bandung. Departemen Biologi Institute Teknologi Bandung.
Wulangi, S Kartolo. 1993. Prinsip-Prinsip Fisiologi Hewan. Jakarta. Departemen Pendidikan dan Kebudayaan