Literature Review On Lipase

Enzymes react differently under different conditions and concentrations, being the most productive at the enzymes specific optimum condition and concentration. The enzyme sucrase, extracted from yeast, breaks down the complex sugar sucrose into the simple sugar glucose. Testing for sucrase’s optimum environment, multiple reactions were ran using varying amounts and concentrations of sucrose and sucrase at different pHs and temperatures. The product was then treated with Benedicts solution to visually observe what amount of glucose was present after the reaction was ran; negative results being little to no glucose present and positive results being

I predict that at temperatures above 70°C the enzyme lipase will become denatured and at temperatures below 10°C the enzyme will become inactive. Since lipase operates within the human body I’d also predict that its optimum temperature would be around human body temperature which is approximately 37°C. I predict that before the optimum temperature the rates will gradually increase and preceding the optimum there will be a drastic decrease in rate until the enzyme is denatured.

Enzymes are proteins which can catalyse chemical reactions without changing themselves. The enzyme lipase breaks down the fat in dairy products such as full-cream milk for people who are lactose intolerant. Lipase acts on its specific substrate, lipids produces fatty acids. If enzyme concentration increases, random collisions between the substrates and active sites of enzyme increase due to the increasing amount of active sites which allow more collisions to happen, so the rate of breakdown of lipids to simpler substances will increase. During the experiment, sodium carbonate solution and pH indicator phenolphthalein will be added ahead of

According to kim et al. (2014), A 59-years-old man with account of alcohol addiction offered to an emergency room having dyspnea supplementary with diarrhea, malaise, a 40 pound weight loss and nausea for 4 months. He was hypoxic in ambulation. A CT of chest revealed borderline mediastinal lymphadenopathy. Lipase was raised to 1000. He was discharged numerous days once conservative treatment for recognized viral gastroenteritis, acute bronchitis, and pancreatitis. He improved to some extent but after three weeks, he returned to ER with persistent signs and a new-fangled bullous skin rash of his right ankle was found to be an eosinophillic vasculitis on skin biopsy. Moreover, He had a

60 µM of Lysozyme (10 mg/ml) was added to 6 ml of the solution. 60 µM of 0.1 M Deoxyribonuclease I, 25 mg/ml (10,000 U/ml) was added after and incubated for two minutes. It was followed by addition of Ethylenediaminetetraacetic acid (EDTA) and incubated for 10 minutes. 60 µM of 1M Magnesium sulfate were added, carefully mixed and incubated for 20 minutes. The centrifugation technique was completed with Sorvall RC 5C Plus (code 3.19.5.06) with Rotar Sorvall SM-24, Autoclovable 121 C at 12,000g speed, at 4oC for twenty minutes. The Enzyme Stage 1 (0.3 ml) was extracted for additional analysis. The dialysis procedure was performed using Dialysis tubing Seamless-cellulose, width 25mm, diameter 15.9mm, 4.8 nm pore diameter, that retained materials with 12,000 or higher MW. The length of the tubing was cut and was approximately 14 centimeters, soaked in water, and after was filled with the retentate and left in a beaker covered with plastic wrap. The dialysate was the 10mM Tris-HCL, pH 7.4 and 10mM Magnesium sulfate. The buffer was replaced few times within the

In this experiment, the results identify the different temperatures that the lactase enzymes were most effective and ineffective at. At 0°, 1% of glucose was present in the milk meaning that the lacteeze enzymes were effective at the temperature but the reaction time of the enzymes were slower. At 40°, the milk contained the maximum amount of glucose at 2% or more. This indicates that at this temperature, the lacteeze enzymes work the most effective and they have the most amount of collisions which increases the reaction time and breaks down the lactose quicker. At 100°, there was no glucose present in the milk. This meant that all the lactase enzymes were denatured in the hot temperature and none of the lactose sugars were broken down.

BglA was remain active even in the existence of 600 mM glucose. However, BglA activity was gradually repressed with the increase of glucose concentration, and Ki value for glucose was found to be 1200 mM as shown in figure 4b. Organic solvents have proven an obvious constrain for the BglA activity, enzyme was completely inactive by adding 40% (v/v) methanol, ethanol, n-butanol and isopropanol whereas, 40% (v/v) acetone, ethyl acetate and acetonitrile strongly repressed BglA activity up to 18%, 38%, 50%, respectively.

The metabolic pathway of L. lactis can function through aerobic and anaerobic reactions. It consists of 621 reactions and 509 metabolites and requires minimally glucose, arginine, methionine, glutamate and valine for growth. The main metabolism of L. lactis is through the anaerobic pathway, fermentation, which produces lactic acid from the available carbohydrates and is used for industrial food production. The carbon sources that L. lactis draws from include fructose, galactose, glucosamine, glucose, lactose, maltose, mannitol, mannose, ribose, sucrose and trehalose. However, the growth rate of the cell with the intake of each carbon source is different. Growth rate on glucose, mannose, galactose, sucrose, lactose and glucosamine are the same,

The Transesterification process is the reaction of a triglyceride (fat/oil) with an alcohol to form esters and glycerol (Wahab Maqbool, 2010). A triglyceride has a glycerine molecule as its base with three long chain fatty acids attached. During the esterification process, the triglyceride is reacted with alcohol in the presence of a catalyst, usually a strong alkaline like sodium hydroxide. The alcohol reacts with the fatty acids to form the mono-alkyl ester, or biodiesel and crude glycerol. In most production methanol or ethanol is the alcohol used (methanol produces methyl esters, ethanol produces ethyl esters) and is base catalyzed by either potassium or sodium

Lipoma is benign tumor of fatty tissue. Benign tumor means that lipoma isn’t cancerous and rarely harmful. Lipoma slowly develops under animal skin and is most common in older animals. Owners can notice following characteristics in lipoma: soft on touch, be just under skin, move easily if prodded with your finger, grow slowly. Lipomas are commonly located in the neck, back,stomach. In most cases, if one lipoma appears on the body more will appear in time. Although lipomas are rarely harmless it is advisable to remove them while there are small. In time they can grow bigger, and if they grow between the legs or on chest, they can cause mobility problems. In addition, if blood vessel disease occur within the tumor, that complicate later surgery.

2. Introduction: Each student was given unknown bacteria and was instructed to perform a variety of experimental tests that would help to identify their bacteria. During the process of identification, the unknown bacteria was added to many different testing medias using aseptic technique. They are as follows: lactose fermentation on eosin methylene blue (EMB), TSI (Triple Sugar Iron agar), Phenol red sucrose, the SIM test, H2S by SIM, IMViC (indole, motility, voges-proskauer, and citrate), Urease (urea broth), PDase (Phenylalanine Deaminase), Lysine Decarboxylase, and Ornithine Decarboxylase. Colonial morphology on EMB was used to

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).

Based on the results of the batch cultures, in the previous chapter, the authors decided to investigate 15 g, 25 g, and 35 g of 500 mg/g of 95% LIPC for the in vivo study. Day 0 samples confirmed that opportunistic bacteria were present. SBEC bacterial concentrations increased linearly (P = 0.008) as LIPC dose increased but concentrations were similar for 0 and 15 (Table 5.1). As the dose of LIPC increased the concentration of C. perfringens decreased linearly (P = 0.03). The remaining three opportunistic bacteria strains, C. difficile, E. coli general, and E. coli K-12, were not significant (P ≥ 0.20) across treatments. Numerically, 25 had the lowest concentration of E. coli general, and 0 had the lowest concentration of C. difficile. Although increasing the dose of LIPC decreased C. perfringens the observation that increasing the dose also increases SBEC would suggest that there may be no additional benefit of dosing LIPC above the recommended rate. However, this would also suggest that the nutraceutical reaches the cecum without being compromised in the stomach during the digestion process.

For obtaining the best performance of EMR, an appropriate operating condition should be selected. To optimize the operating condition of EMR, RSM was applied to model the apparent enzymatic membrane activity of the immobilized lipase using four parameters: substrate concentration (C), peristaltic pump flow rate (μL·min-1), reaction pH, and temperature (°C). These four variables were optimized using two 2-factor-3-level CCDs. The accuracy of the models was evaluated by the coefficient of determination (R2). The value of R2 for designs 1 and 2 were 96.69 and 97.27%, respectively. ANOVA (Table 2, The Supporting Information) shows that both the models for designs 1 and 2 were statistically good with a significance level of P 1162 μL·min-1 and certain substrate concentration, the membrane activity apparently

LCFA exert an acute inhibitory effect on acetoclastic and hydrogenotrophic methanogens, acetogens, and to the β-oxidation itself (Kim et al., 2004; Lalman and Bagley 2000, 2001, 2002; Templer et al., 2006). Moreover, LCFA degrading bacteria have a very slow growth rate (Mackie et al., 1991). As a consequence, during anaerobic digestion of lipid-rich wastes, accumulation of LCFA is most likely phenomenon and subsequently, inhibition of the biomethanation occurs. Oleic acid is the major LCFA in various kinds of industrial and domestic lipid-rich wastewaters (Pereira et al., 2002). It was also reported as the most toxic LCFA (Cirne et al., 2007). Adsorption of LCFA to the cell wall (Koster and Cramer, 1987), and binding of LCFA to cell membranes, changing their surface property with interference in transport functions (Hook et al., 2010), have been suggested as potential mechanisms underlying inhibition by LCFA. Nevertheless, Pereira et al. (2004, 2005) observed mineralization of biomass-associated LCFA up to 5 g COD-LCFA g-1 volatile solids, and concluded that LCFA inhibition is reversible which is primarily caused by physical transport