Michaelis–Menten kinetics

Optimum pH determination Enzymatic activity is effected by different environmental conditions; these environmental factors have a direct impact on whether the enzyme will catalyse the reaction tested or if the environment does not permit enzyme activity. One environmental factor that effects enzymatic activity is pH. All enzymes have an optimal environment where the enzyme is most efficient, this environment can even contribute to the function of the enzyme. For LDH the optimal pH would be a pH that

Introduction Aim: To determine the kinetic parameters (Km and Vmax) of the alkaline phosphatase enzyme. Theory and principles The enzyme is the most important molecule that is involved in the day-to-day functioning of the cell. Enzymes act as biological catalysts, they facilitate slow reactions by lowering the energy required to activate the reaction. Enzymes do not undergo a permanent change and therefore remain unchanged at the end of the reaction. Enzymes are highly selective and will only

Michaelis – Menten and Lineweaver – Burke kinetics of polyphenol oxidase . Effect of substrate concentration concentration on the rate of reaction” Introduction Enzymes catalyse biological reactions ,increasing the rate of chemical reactions Enzymes have an affect on the structure of chemical transformation (stryer et al , 2011 ) Enzyme substances bind at the active cite which contains amino acid chains. Without catalysis reactions the process would take place slowly to produce products , enzymes

Hui Tzu(Erin) Wang ID:0720052 Effect of an Increasing Substrate Concentration on Enzyme Activity Rate Abstract The reaction rate of an enzyme can be affected by many factors, and the purpose of this experiment was to find out how an increasing substrate concentration influences the rate of an enzyme activity; we obtained data from recording the absorbance of the samples which contain the same amount of potato juice (enzyme oxidase) and different

Introduction (5 marks) Enzymes are globular shaped proteins that are found throughout the body, with their main function being to act as biological catalysts. An enzyme can act to speed up or regulate the rate of the reaction, in order to maintain an efficient rate of biological reactions. Enzymes, whilst having an important role in the reaction of many chemicals within the body, are not consumed in the reaction, and so are able to catalyze many reactions in their life cycle. Enzymes are able

concentration versus time profiles and explains several mechanisms (such as first-pass metabolism) in an in vivo system. The main advantages of PBPK models over other models are: (1) they account for substrate concentrations at the enzyme site, Michaelis-Menten constants, and potential saturation of metabolism and (2) they accommodate any potential regional differences in intestinal availability because of the heterogeneous expression of drug-metabolizing enzymes along the small intestine. Therefore

Conclusion 5. References 1. Introduction 1.1. Aim To determine the kinetic parameters known as Vmax and Km of Alkaline Phosphatase. This will be done by determining and investigating the optimum pH and

Describe an experiment (assay) that could be used to determine the kinetic parameters of your enzyme. To determine the kinetic parameters of Beta-lactamase, one must be able to perform an experiment that could be converted into a Michaelis-Menten plot. This means that the assay must study the relationship between the velocity of an enzyme-catalyzed reaction is and the substrate concentration, where velocity

allowed the determination and calculation of different kinetic parameters for alkaline phosphatase. First, it was necessary to generate a standard curve for PNP presenting the absorbance as a function of the concentration of PNP since the remaining of the experiment is based on measuring absorbance values of PNP. This standard curve is then a good tool to convert those absorbance values into PNP concentration values that can be used to study the kinetics of the alkaline phosphatase enzyme. Once the standard

peroxide more quickly. 3) Adding less enzyme caused the reaction to proceed more slowly than when more enzyme was utilized. 4) It is likely that the rate of reaction would increase as substrate is added. It will probably follow classical michaelis-menten kinetics. See the attached picture for an example of this scheme for the rates (the picture of the hyperbola is the rate vs. the substrate concentration). 5) Hydrogen peroxide can be safely broken down into water