Enzyme and Protein - Research Paper Example

 Enzyme/protein Among the three categories of nutrients groups are carbohydrates, vitamins and proteins (Clore & Gronenborn, 1993). Carbohydrates are termed as energy giving foods while vitamins assist in protection of the body against diseases. The third group - proteins refers to complex molecules that help your body perform a wide variety of biological functions. Each protein type serves a specific function. Proteins are composed of building blocks known as amino acids. Proteins contain varying amounts of these primary amino acids which provides biological organisms with the necessary elements for cell function. Proteins are categorized into five main groups according to their functions. These groups include structural, Hormonal, storage, Enzyme and Immunoglobulin proteins. The largest group of proteins is the structural proteins (Neurath, 1975). Structural proteins serve as essential components to your body's construction. Common examples of structural proteins are Keratin and collagen. Keratin forms the structure of the skin, nails, hair and teeth. While, collagen serves as a connective structure for tendons, bones, muscles, cartilage and skin in particular. Storage proteins house critical elements that your cells need in order to accumulate particular body components. Hemoglobin, for instance stores oxygen in the red blood cells. Ferritin is another storage protein that houses the crucial element iron, which helps the body make healthy red blood cells. Hormonal proteins facilitate the transfer of impulse and sense. Enzyme proteins are used within plants and animals as catalysts for various processes to take place. Immunoglobulin proteins aid in protection of the body against diseases and balance of nutrients within various living organisms. My research paper will basically discuss Enzyme Proteins. The enzyme proteins are further categorized into six groups. These groups include oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. Oxidoreductases catalyze oxidation or reduction reactions (Oberhauser, 2013). They are very vital for many metabolic processes, particularly in aerobic and anaerobic respiration. Oxidoreductases can be found in glycolysis, the TCA cycle and oxidative phosphorylation Transferases are enzymes that catalyze the movement of a functional group from one molecule to another. Examples of these functional groups include phosphate, methyl and glycosyl groups. Lyases catalyze lysis reactions that generate a double bond. These are a type of elimination reaction but are not hydrolytic or oxidative. They are often referred to as Synthase enzymes (Neurath, 1963). Isomerases enzymes catalyze structural changes within a molecule. Ligases are responsible for the catalysis of ligation; the joining of two substrates. The last group known as Hydrolase enzymes catalyzes hydrolysis. Hydrolysis refers to the breaking of single bonds through the addition of water. Common examples of Hydrolase enzymes are proteases also referred to as peptidases, which cleave peptide bonds between amino acids in order to breakdown proteins. Nucleases cleave phosphodiester bonds between nucleotide subunits in nucleic acids. Lipases, which is also an Hydrolase enzyme break down lipids into fatty acids and glycerol by cleaving ester bonds Narrowing our research paper into Lipases, living things, human beings in particular are not able to get nourishment from the foods they eat without the enzyme lipase. Lipases are complex proteins, called enzymes, which break down fats into fatty acids (Clore & Gronenborn, 1993). The protein lipase can be found in the Gly-X-Ser-X-Gly sequence, which contains prokaryotic and eukaryotic lipases. There are various sources of lipase, ranging from human to plants. In human beings, lipase is produced in pancreas and the tongue. Other sources of lipase are plants. Eleven significant plant sources: avocado, walnut, pinenut, coconut, lupin, lentils, chickpea, mung-bean, oats, castor beans and eggplant have been proved as sources of lipases. Oats, which are most abundant, have been used in the commercial significance of lipase to manufacture treatment of patients with pancreatic insufficiency, especially those who have cystic fibrosis. Fungi and bacteria also secret lipases that facilitate nutrients absorption from external medium. Researches by various scientists also indicate that gene C. albicans also contain lipases. C. albicans contain lipase gene (LIP) family. Lipases genes may also be found in Candida krusei, Candida parapsilosis and Candida tropicalis. LIP is a gene that encodes the lipase, example of such genes being the LIP1 transcript. The hormone-sensitive lipase gene is transcribed from at least five alternative exons in mouse adipose tissues. When the Mouse HSL (Hormone sensitive lipase) for 8.2kb is sequenced upstream of the translation start codon and the steady - state HSL mRNA levels in the mouse adipose tissue studied, five distinctive extremities will be observed. These extremities correspond to the distinct exons in the genomic DNA. Exon A will be located approximately 7Kb 5" to the HSL translation start site (Oberhauser, 2013). Exon B, C, and D will be found clustered 1.5 to 2 Kb upstream. The previously described exon 1 is immediately upstream and contiguous with the HSL translation start site. The deduced amino acid sequence encoded by the lipases is Asn-X-Ser / Thr sequons and is encoded by a cDNA. All the food consumed by human body goes through the small intestines for absorption. Breakdown of the food is thereby essential for effective absorption. Lipases are generally produced in the pancreas, but the enzymes also form in the mouth and stomach to aid in the breaking down process before food reaches the stomach. The metabolic function of the enzyme lipase is basically to break down or digest fat to fatty acids and glycerol. This depends on the conditions of the surrounding media. A healthy amount of lipases in the blood stream range from 0 to 160 units per liter (U/L). However, if the amount increases, there may be serious pancreatic damage and resultant ill health. Generally, healthy people produce enough lipases in the pancreas to digest foods for absorption (Neurath, 1975). People whose pancreas produce too little lipases suffer cystic fibrosis, Crohn's disease or celiac disease. This disease damages the lining of the small intestine. Such victims often do not have enough enzymes to get the nutrition from the foods they eat and may suffer from malnutrition. In other functions, LPL encodes lipoprotein lipase, which is expressed in endothelial cells found within the heart, muscles, and the adipose tissue. This lipase acts as homodimer, with dual functions - triglyceride hydrolases and the ligand factor for receptor - immediate lipoprotein uptake. Severe mutations that may cause LPL deficiency resulting into hyperlipoproteinemia, while less extreme mutations in the LPL are likely to cause many disorders of lipoprotein metabolism. However, the uses of lipases have also taken an industrial aspect. Researches have managed to discover other uses of lipase outside the body. The production of fatty acids by the hydrolysis of natural oils and fats is a very important component in the economic exploitation of these naturally produced renewable raw materials. Lipase has been used to extract oil from oil products such as corn, rapeseed, sunflower, palm, coconut, olives and rice bran, and a wide range of animal fats such as tallow’s. A large number of high-value products require fatty acids in their manufactures. These include coatings, adhesives, specially lubricating oils, shampoos and other personal care products. Oils and fats are part of a group of compounds known as fatty esters or triglycerides, and their hydrolysis essentially involves reactions by use of lipases with water to produce valuable the required free fatty acids and glycerol (Neurath, 1975). Dairy industry uses lipases to change, or modify, the fatty acids in types of cheeses. Some household cleaners and detergents also contain lipases which are used to digest grease left in skillets, pans, sinks and also remove dirt in clothes. Lipases are also used for obesity medications. Researches are also underway, trying to figure out various ways in which the lipases can help break down other molecules. The regulation of lipases is done transcriptionally and post-transcriptionally. The circadian clock may be important in the control of Lpl mRNA levels in peripheral tissues. LPL isozymes are regulated differently depending on the tissue. Insulin is known to activate LPL in adipocytes and its placement in the capillary endothelium (Neurath & In Hill, 1975). Contrary, insulin has been shown to decrease expression of muscle LPL. Instead muscle and myocardial LPL is activated by glucagon and adrenaline. This can be evident during fasting, where LPL activity increases in muscle tissue and decreases in adipose tissue, whereas after a meal, the opposite occurs. Due to this, dietary macronutrients differentially consistently, affect adipose and muscle LPL activity. After about 16 days feeding on a high-carbohydrate or a high-fat diet, LPL activity increased significantly in both tissues 6 hours after a meal of either of the two composition, but there is a significantly greater rise in adipose tissue LPL in response to the high-carbohydrate diet compared to the high-fat diet (Dietrich & Vénien-Bryan, 2005). There is significantly no difference between the two diets' effects on or insulin sensitivity, or on fasting LPL activity in either tissue. The LPL concentration displayed on endothelial cell surface cannot be regulated by endothelial cells. This is because hey neither synthesizes nor degrades LPL. Instead, this regulation occurs by managing the flux of LPL arriving at the lipolytic site and being released into circulation attached to lipoproteins (Whitford, 2005). A greater percentage of people, including scholars and scientists only see the positive impacts of the lipase in the human body - its ability to break down fats to fatty acids and amino - acids for absorption in the body. However, the lipases have diverse health impacts to the human body. Production of inadequate lipases more so in the human body leads to malabsorption resulting to pancreatic exocrine insufficiency. Severe cases of malabsorption lead to steatorrhea in later years. In cases of little production of lipase, patients suffer not only from nutritional deficiencies but also from increased nutrient delivery to distal intestinal sites, causing symptoms by profound alteration of upper gastrointestinal secretory and motor functions. Such patients are recommended to take 25,000 to 40,000 units of lipase per meal using pH-sensitive pancreatin microspheres, with dosage increases, compliance checks, and differential diagnosis in case of treatment failure. A prove of the above information can be done through a simple experiment to test whether the lipase can break down fats into fatty acids and fat (Whitford, 2005). When lipase from pancreatic juice is put in substrate within a test tube, the lipid substrate is broken down into Glycerol and fatty acid, which is evident by the Phenol Red color change in the substrate. In conclusion, lipase is a very essential element in the field of biochemistry, whose use ranges from human health to industrial and commercial use. Lipase assists in digestion and absorption of various foods within the human body. The lipase product in some plants also makes them economically essential, where they are used to manufacture various digestive products such as detergents and household cleaners. However, little or excess production of the enzyme lipase in the human body can be unhealthy. This case can however be maintained by manufacture of lipase control products to stabilize the lipase level within the body. References Whitford, D. (2005). Proteins: Structure and function. Hoboken, NJ: Wiley & Sons. L'Italien, J. J. & Symposium of American Protein Chemists on Modern Methods in Protein Chemistry. (1987). Proteins: Structure and function. New York: Plenum Press. Neurath, H. (1963). The proteins: composition, structure, and function. New York, NY: Academic Press. Hoffmann, R., University of Maryland at College Park, Educational Film Center (Annandale, Va.) & Intellimation, Inc. (1989). Proteins: Structure and function. Santa Barbara, California: Intellimation. Neurath, H., & In Hill, R. L. (1975). The proteins. New York, NY: Academic Press. (1986). Proteins. New York, NY: John Wiley & Sons. Neurath, H. (1975). The proteins. New York, NY: Academic Press. Quality and Utilization of Agricultural Products National Program (U.S.) & United States. (2009). Bio-industrial uses of sorghum proteins ... annual report. Washington, D.C.: U.S. Dept. of Agriculture, Agricultural Research Service. Oberhauser, A. F. (2013). Single-molecule studies of proteins. New York, NY: Springer. Dietrich, J. & Vénien-Bryan, C. (2005). Strategies for two-dimensional crystallization of proteins using lipid monolayers. London: Imperial College Press. Clore, G. M. & Gronenborn, A. M. (1993). NMR of proteins. Boca Raton, FL: CRC Press. Read More