It may limit the application of the PS cyclization as a chemical ligation method for peptides with N-terminal aromatic residue and peptides with aldehyde residue at C-terminal(40). 7. Pictet-spengler reaction for protein chemical modification= proteins are having aldehyde and ketone groups in their structures. So proteins are taken as a substrate and the pictet-spengler reaction is performed for making modification in the chemical nature of the proteins. P. agarwal and co-workers work for protein chemical modification by conducting a pictet-spengler reaction between aldehydes and alkoxyamines.
KINETICS OF MULTISUBSTRATE REACTIONS Introduction Enzyme kinetics is the study of rate of biochemical reactions that are catalyzed by enzymes. In enzyme kinetics, the reaction rate is measured and the their effect is measured or investigated. Studying an enzyme kinetics in this way we can check the catalytic activity of enzyme, its major role in metabolism, and how its activity is determined. Enzymes are protein in nature and binds to substrates. These substrate molecules bind to active site of enzyme and changed into products through a number of steps known as enzymatic reactions.
1.Introduction: An enzyme is a large protein that acts as a biological catalyst which changes the rate of a reaction. It provides an active site which is an environment where a reaction can take place this is made up of amino acids. The structure and shape of the substrate, the structure and shape of an enzyme and the substance upon which the enzyme works all have to match exactly. This enables the substrate to bind, but it can 't do this if the shapes of the two are different. The Aim of Enzyme Catalase Experiment is making a series of experiments involving the enzyme Catalase which has been performed in order to determine some of the enzyme 's properties.
Enzyme assays are performed to serve two different purposes: (i) To identify a special enzyme by proving its presence or absence in a distinct specimen. (ii) To determine the amount of the enzyme in the sample by monitoring the disappearance of substrate or appearance of product. Enzymes speed up reaction rate by decreasing the activation energy required to start the reaction. Activation energy is the energy required to break certain bonds in the substrate so that other bonds can form. The formation of these new bonds results in the formation of the product by measuring the changes in absorbance due to the substrate (starch) being changed into product by the amylase enzyme.
Usually, the microbial enzymes have various potential uses in industries and medicine. The microbial enzymes are also more reliable than plant and animal enzymes as they are more stable and active. Also the microorganisms demonstrate an alternative source of enzymes because they can be cultured in large quantities in a short time by fermentation and owing to their biochemical diversity and susceptibility to gene manipulation. Industries are looking for new microbial strains in order to produce different enzymes to fulfil the current enzyme
The product of the glycolysis is pyruvate. In a further reaction, which is catalyzed by the enzyme complex pyruvate dehydrogenase, acetyl-CoA is formed out of pyruvate, which can be introduced into the citric acid cycle or Krebs Cycle. In an eight-step reaction sequence, the acetyl group of acetyl-CoA is oxidized into two molecules of CO2. These reactions are catalyzed by eight different enzymes. Instead of producing high amounts of ATP, eight electrons were removed from the acetyl group and transferred to the co-enzymes NAD+ and FAD, which are reduced to NADH and FADH2.
Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.
Catalase and Temperature Introduction Background: Enzymes are catalysts which help reactions inside of organisms such as cells. Many different types of enzymes are used to catalyze different types of reactions. Enzymes are able to catalyze reactions that normally wouldn’t be possible under the specific circumstances in the cell such as the pressure or temperature of the cell. The way an enzyme works is it binds with the active site of a substrate and creates an enzyme substrate complex. The enzyme then breaks apart the bonds in a substrate and then leaves unchanged after the reaction.
The Cu1+ then react to bicinchoninic acid assay forming a purple water soluble complex. Moreover, the total volume of protein concentration can be measured by the colorimetric technique which will change the colour of sample solution from green to purple in proportion to protein concentration. SDS-PAGE electrophoresis Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE electrophoresis) is probably the most common analytical technique widely used to separate biological molecules, usually a nucleic acid or protein based on their electrophoretic mobility. The motility is a function of conformation, the length of their peptide chain and charge of the molecule. Depending on their size, small biomolecules move faster and more easily fit through the pores in the gel than larger ones.