SYNTHETIC EXPLOITATION OF ENZYMES: BIOCATALYSIS IN ORGANIC SOLVENTS: FUNDAMENTALS ENZYMES IN ORGANIC SYNTHESIS 1. Enzymes catalyze a broad spectrum of reactions with high turnover numbers. Rate enhancements approach 1012 fold. 2. Enzymes may accept a wide range of substrates. 3. Enzymes are highly regio and stereoselective. 4. Enzyme reactions take place under mild conditions; this minimizes problems of isomerization and racemization. 5. Enzymatic processes are less hazardous and polluting
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point for the enzyme (catalase) to substrate (H2O2(aq)) concentration ratio. Thus‚ to truly understand this‚ the trial time period should be extended insofar that a declination in the rate of the reaction can be observed with multiple trials. If the trends of the independent trials coincide with one another‚ then it is plausible that a saturation point may have been a factor of the linear-like trend. This case will be further discussed in one of the five major factors that influence enzyme activity:
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Identification of the Marker Enzymes Present in Different Fractions of a Chicken Liver Cell Priscilla Mariel M. Cadiz Biology Department‚ De La Salle University‚ 2401 Taft Ave‚ Manila‚ Philippines *Email: cadizpriscillamariel@yahoo.com Cell Fractionation allows the organelles to be studied in more depth and detailed. It is an important technique in Cell Biology because it enables to obtain precise information about the different structure and functions of the organelles. Certain organelles
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precipitate. Enzymes Enzymes are protein molecules that act as biological catalysts. An enzyme catalyses a specific reaction. They have an active site… Substrate ENZYME Products. Maltose is broken down by the enzyme maltase to glucose and glucose. The reactions enzymes catalyse can be anabolic or catabolic - Anabolic meaning building‚ catabolic meaning breaking down. They do not die. They are simply denatured. They are affected by temperature‚ pH and concentration of enzyme and/or substrate
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designed to test the reaction of the enzyme amylase at various temperatures. There were two different kinds of amylase being tested‚ one was fungal amylase also known as aspergillus oryzae and human amylase. The changes in temperature effect the rate at which an enzyme and a substrate collide. When the temperature is too high the active site changes shape or denatures‚ once this occurs it stops substrates from attaching themselves to their corresponding enzyme. When the temperature is too low it decreases
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Natural enzymes are proteins that catalyze biological reactions by lowering the activation energy of the reaction without being altered during the process. The enzyme used in this experiment was the β-galactosidase purified from E. coli. This enzyme hydrolyzes lactose and turns it into galactose and glucose. Since it is difficult to assay the activity of β-galactosidase‚ we will be using the artificial substrate‚ o-nitrophenyl-β-galactoside (ONPG) instead of lactose. ONPG is an analog of lactose
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the Catalytic Properties of the Enzyme Peroxidase Extracted from a Turnip Under the Conditions of Temperature‚ pH‚ Boiling and Competitive Inhibitors By Robin Caserta BIO 101 September 30‚ 2013 ABSTRACT The enzyme‚ peroxidase‚ extracted from a turnip was tested for its efficiency in binding to its substrate and its stability under several conditions. To do this‚ we tested effects on peroxidase activity‚ first‚ with different amounts of the enzyme‚ next at temperatures of 4oC‚ Room
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carbohydrates begin in the mouth‚ where an enzyme‚ salivary amylase (α-amylase;ptyalin) starts to breaking the polysaccharides (starch) into short polysaccharides (dextrin). Dextrin is a partial degradation of starch‚ shorter chains of maltose units. Salivary amylase is inactivated by stomach acid in the stomach and to a small extent‚ it continues breaking down starch (but there’s no enzymatic activities on carbohydrates in the stomach). An intestinal enzyme‚ pancreatic amylase‚ continues the activity
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Amylase 1. List the substrate and the subunit product of amylase. _starch & maltose respectively__ 2. What effect did boiling and freezing have on enzyme activity? Why? How well did the results compare with your prediction?__Boiling caused amylase to be denatured‚ thus inactivating the enzyme. Freezing has no effect. The function of an enzyme is directly related to its environment‚ like temperature.__ 3. At what pH was the amylase most active? Describe the significance of this result. __ pH
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steeping is a risky process and may result in the degradation of cotton cellulose while rot steeping‚ hot caustic soda treatment and hot washing with detergents are less efficient for the removal of the starch sizes. * Enzymatic desizing : Enzymes are solubilizing bio catalysts‚ mainly proteins‚ thermo labile (readily changed or desized by heat) and highly specific in their action. A
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