Catalysis

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  • Kinetics Of Chymotrypsin Catalysis

    CHYMOTRYPSIN CATALYSIS Sarkis Hamalian ABSTRACT To examine the enzyme kinetics of chymotrypsin during the catalysis of the synthetic substrate p-nitrophenyl acetate (NPA). Initially, observe the magnitude of the initial burst with regards to the enzyme concentration. Secondly, the analysis of the steady state deacylation rate with regards to the pH of the reaction mixture. Chymotrypsin catalysis is a process that proceeds with two steps, an initial fast step involving the covalent modification of the enzyme to the substrate and the subsequent slower deacylation step which returns the enzyme to its free state (rate determining step). These steps are highly dependent on enzyme concentration and the pH of the environment in which the reaction…

    Words: 2319 - Pages: 10
  • Fatty Acid Synthesis: The Catalysis Process Of Biosynthesis

    It is also called anabolism or biogenesis. It is a enzyme-catalyzed method in which substrates are transformed into complex products. In this process simple compounds change or convert into other compounds or they join together to form macromolecules. Example: In this process gluneogenesis is responsible for the production of glucose from non carbohydrate originator. Actually biosynthesis is an enzyme-catalyzed process in which substrates are converted into complex compounds. 1. Biosynthesis…

    Words: 860 - Pages: 4
  • Haldane Reaction Lab Report

    HALDANE RELATIONSHIP AND ONE-WAY ENZYMES  INTRODUCTION: Most of the enzyme catalyzed biological reactions are reversible in nature. However, an enzyme may prefer to catalyze the reaction more efficiently in one direction over the other under given physiological concentrations of substrate or product (substrate in the reverse direction). An enzyme favouring a virtual unidirectional catalysis of an overall reversible reaction can’t escape the laws of thermodynamics. As a catalyst doesn’t change…

    Words: 2701 - Pages: 11
  • Functions Of Alkaline Phosphatase

    human body. Its main function is the cleaving of phosphate groups from mostly organic molecules, including proteins, nucleotides and even alkaloids, which makes it a hydrolase enzyme (Ellis, 2016). In biochemistry, a hydrolase enzyme is an enzyme that speeds up the hydrolysis of complex biomolecules like proteins, starch and fats (Horak, 2014). The addition and elimination of phosphate groups is an important process in biochemistry, as many enzymes are catalysed or have their activity controlled…

    Words: 1035 - Pages: 5
  • Friedel-Crafts Synthesis Of Glyoxylates

    between 4,7-dihydro-1H-indole 5 and α-amidosulfone 8 under identical reaction conditions, followed by oxidation with p-benzoquinone (Scheme 6). Finally, this method was successfully applied for the gram scale synthesis of 2- and 3-indolyl glycines 11 and 12 (Scheme 7). Scheme 5. Reactions were performed with 2 (0.18 mmol), 3 (0.15 equiv.), and (R)-1 (10 mol%) in toluene (3.0 mL) at 70 °C. The yield was determined after chromatographic purification, and the % ee was determined by HPLC…

    Words: 843 - Pages: 4
  • Catalytic Effect And Specificity Of Enzymes Essay

    In addition to few chemical reactions can be reacted in our body spontaneously, the majority of reactions are catalyzed by specific enzymes. An enzyme can identify their unique substrate from thousands of reactants. According to the differences on the degree of specificity of enzyme catalysis, we divide its specificity into three categories: absolute specificity , relative specificity and stereospecificity. If a kind of enzyme can only catalyzed one substrate, it was subjected to absolute…

    Words: 1001 - Pages: 4
  • Lab Report On The Effect Of Amylase Concentration On Starch

    Introduction An enzyme is a protein that functions as a catalyst, it speeds up chemical reactions (Freeman et al. 2017 p. 90). Enzymes are often large globular proteins and are able to hold substrates in specific orientations so they are able to react, the location where the substrate binds with the enzyme and reacts is called the active site and is the location where the catalysis occurs (Freeman et al. 2017). Enzymes activity is often related to the optimal environment for them in respect to…

    Words: 1959 - Pages: 8
  • The Importance Of Enzyme Kinetics

    of the enzyme, thus denaturing the enzyme and rendering it useless. PH levels also have an effect on enzymatic activity since high and low pH values can lead to a loss of enzymatic activity while an optimum pH value is one where the enzyme is most active4. The presence of inhibitors effect enzymatic activity by either blocking off the active site of an enzyme or by changing the shape of the active site. Competitive inhibitors compete with the substrates for the active site of an enzyme and once…

    Words: 751 - Pages: 4
  • Horseradish Peroxidase Lab Report

    The experiment conducted was to observe the enzyme catalysis of Horseradish Peroxidase with different determining factors. In this experiment the horseradish peroxidase enzyme should have an optimal temperature of 35°C, should have an optimal pH of 6, and should catalyze rapidly with the substrate and enzyme concentration. We were able to observe that the enzyme reacts best with its optimal temperature of 35° C and optimal pH of 6. Moreover, when there’s a high the substrate concentration and a…

    Words: 1134 - Pages: 5
  • Alkaline Phosphatase Synthesis

    Alkaline phosphatase catalyzes the hydrolysis and transphosphorylation of phosphomonoesters (1). A kinetic reaction scheme of AP is presented in Figure 2. Figure 2: Kinetic reaction scheme of alkaline phosphatase (11). Under the hydrolysis reaction, free phosphate and an alcohol molecule are released from the active site. The rate-determining step of this reaction is pH dependent. Transphosphorylation has similar initiate steps as hydrolysis. However, phosphate cannot exit the active site,…

    Words: 2173 - Pages: 9
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