Congenital Sucrase-Isomlatase Deficiency CSID

B 10. A Similars and Dissimilars 1. polypeptide 2. sucrose 3. glucose 4.

1) Amylase is utilized to break down starch molecules into more simple sugars for use by the body. It performs this function by hydrolyzing glycosidic linkages in the polysaccharide chain.

Sucrase activity in the intestine is affected by sucrose content in food as most foods contain some sucrose. Adding sucrose will increase

specific enzyme (Knowles, 1991). One part of the enzyme, salivary amylase, is that alpha amylase is in the saliva of most animals because this enzyme breaks down starch (Jacobsen, Melvaer, Hensten- Pettersen, 1972). In the presence of starch, this enzyme is present in saliva, but is not present when there is no starch present (Jacobsen, Melvaer, Hensten- Pettersen, 1972). The conditions for salivary amylase to have a reaction with starch would change in temperature and enzyme concentration, as well as, monitoring the pH levels (Jacobsen, Melvaer, Hensten- Pettersen, 1972). Salivary amylase is an enzyme is human saliva that helps in digestion of specific substrates, such as starch (Hudman, Friend, Hartman, Ashton, Catron, 1957). It breaks down starch molecules by splitting maltose from the non-reducing end of a gluten molecule (Jacobsen, Melvaer, Hensten-Pettersen, 1972).

In this lab experiment the action of the enzyme Amylase was observed on starch (the substrate). Amylase changed the starch into a simpler form, the sugar maltose, which is soluble in water. Maltose then breaks down the glucose chains of starch in the pancreas and intestines. Amylase is present in human saliva, and begins to act on the starch in the food while still in the mouth. Exposure to heat or extreme PH (acid or base) will denature proteins. Enzymes, including amylase, are proteins; if denatured enzymes can no longer act as a catalyst for the reaction. In the presence of potassium iodide, starch turns a dark purple color; however maltose does not react with I2KI. The rate of fading of starch allows a quantitative measurement of reaction rate.

Starch and fiber are both made of glucose but fiber moves through the small intestine undigested since we cannot digest it due to the lack of the correct enzyme and starch is broken down into glucose.

Sakuraba H, Matsuzawa F, Aikawa S, Doi H, Kotani M, Nakada H, Fukushige T, Kanzaki T. Structural and immunocytochemical studies on alpha-N-acetylgalactosaminidase deficiency (Schindler/Kanzaki disease). J Hum Genet. 2004;49(1):1-8. Epub 2003 Dec 19. PubMed citation

Phosphorylase Deficiency is a rare inherited disease where the body is not able to break down glycogen in muscle cells. Glycogen is an important source of energy that is stored in all tissues, especially in the muscles and liver. It is also known as McArdle’s disease. People who get this disease experience fatigue and failure during activities such as jogging, swimming or even walking. It is first present in a person's teens or twenties, but they can appear anytime from infancy to adulthood and experience some symptoms. It is usually diagnosed in adulthood. The National Organization for Rare Disorders states, “The prevalence of GSD-V in the Dallas-Fort Worth, TX area has been estimated at 1:100,000 and the prevalence in Spain has been reported at 1:170,000” (NORD). The condition is caused by a recessive gene. This means that one abnormal copy of the gene is passed from each parent to the affected child. The child will then have inherited two abnormal copies of the gene. People who have

Lactase is an enzyme that breaks down lactose. Lactose is the sugar found in milk. It is made up of two monosaccharides: glucose and galactose. Therefore it is a disaccharide that needs to break down in order to be digested. However some people are “Lactose Intolerant” or lack lactase in their bodies. This means that they cannot consume lactose-contained food or drinks or they need help digesting it. People who are lactose intolerant must be very selective to make sure that they do not eat food or drinks with lactose. There are pills though, which are purchased by lactose intolerant people. This pill helps the people break down the sugar lactose into its smaller components.

This paper is to inform you on the disease Acid Maltase Deficiency. This is a disease that affects a small amount of people but can be very deadly if it is not treated or taken care of. It affects a person’s enzyme and makes them, and their muscles, weak. Acid Maltase Deficiency affects a small number of people, but it can happen to anyone. We need to do more research on this so we can figure out why exactly this happens.

The Mucopolysaccharide disease or also known as Hunter Syndrome is an inherited condition and it is a rare inborn of metabolism characterized by inadequate production of an enzyme known as iduronate sulfatase, which is needed to break down complex sugars that produced in the body. This disease usually involves males. And the severe form of the disease starts at the age of 2.

In this lab our group observed the role of pancreatic amylase in the digestion of starch and the optimum temperature and pH that affects this enzyme. Enzymes are located inside of cells that increase the rate of a chemical reaction (Cooper, 2000). Most enzymes function in a narrow range of pH between 5 through 9 (Won-Park, Zipp, 2000). The temperature for which enzymes can function is limited as well ranging from 0 degrees Celsius (melting point) to 100 degrees Celsius (boiling point)(Won-Park, Zipp, 2000). When the temperature varies in range it can affect the enzyme either by affecting the constant of the reaction rate or by thermal denturization of the particular enzyme (Won-Park, Zipp, 2000). In this lab in particular the enzyme, which was of concern, was pancreatic amylase. This type of amylase comes from and is secreted from the pancreas to digest starch to break it down into a more simple form called maltose. Maltose is a disaccharide composed of two monosaccharides of glucose. The presence of glucose in our experiment can be identified by Benedicts solution, which shows that the reducing of sugars has taken place. If positive the solution will turn into a murky reddish color, where if it is negative it will stay clear in our reaction. We can also test if no reduction of sugars takes place by an iodine test. If starch is present the test will show a dark black color (Ophardt, 2003).

In bread making for example addition of amylases can yield more sugars from the starch in flour and barley grains, another commercial which is statue of import ants is the conversion of starch to sweet glucose syrups which are used generally as sweeteners in food industry as well as in the bread-making and brewing industry. Altering the balance between amyloglucosidase and the fungi alpha amylase can produce different proportions of glucose and maltose. A higher proportion of glucose is useful for fermentation whereas higher maltose is more useful in preparation of jam and confectionary. The Amylase Enzyme breaks down starch; which is a carbohydrate.

Numerous enzymes are needed in dough to break down starch into simple sugars that yeast can digest. The process is a very complex one, and includes the enzymes alpha amylase and beta amylase. Starch occurs in two different forms, a branched form called amylopectin and an unbranched chain called amylose.

Sugars exist in solution as an equilibrium mixture of open chain and closed ring(orcyclic), strutures. sugars that can be oxidised by mild oxidising agents are called reducing sugars because oxidising agent is reduced in the reaaction. A non reducing sugar is not oxidised by oxidising agent . All common monosaccrides are reducing sugars. there are several test forr sugars which are based on composition or specific group. Hence sucrose is not a reducing agent due to bonding of oxygen with carbon to form glycosidic bonds between monosacrrides. Therefore they are not free to let go so cant be reduced , some of test includes seliwanoff 's test which distinguish between aldose and ketose sugars.Other test for sugars is benedicts test which commonly used to detect presence of