Galactose

Lactose is the disaccharide milk sugar made of glucose and galactose. In water, lactose breaks down into glucose and galactose spontaneously, but the reaction is very slow (Brennan, 2017). The enzyme β-galactosidase, commonly referred to as lactase, asks as a catalyst to hydrolyze lactose at a faster rate. This basic process of enzyme activity is worth studying as it is vital to the functioning of every cell and keeping living things alive. Lactose intolerance is a condition marked by the absence

enzyme to a specific substrate and how it can denature due to the rise in temperature. Background Information: Lactase is an enzyme that breaks down lactose. Lactose is the sugar found in milk. It is made up of two monosaccharides: glucose and galactose. Therefore it is a disaccharide that needs to break down in order to be digested. However some people are “Lactose Intolerant” or lack lactase in their bodies. This means that they cannot consume lactose-contained food or drinks or they need help

to measure the amount of CO2 produced as the yeast metabolizes. The approached used was to test the level of CO2 (mL) production, after different solutions with 1.5 mL of Saccharomyces cerevisiae and 4.5 mL and either 1M of glucose, fructose, or galactose go through cellular respiration. The higher level of CO2 produced indicates the more cellular respiration that took place. A

Spectrophotometry: Results and Relevance in the World Gretchen Riker General Biology Lab, Section 40057 (PM) Tuesday, June 2nd, 2015  Introduction: “Spectrophotometry is a method to measure how much a chemical substance absorbs light by measuring the intensity of light as a beam of light passes through sample solution” ( ChemWiki). Many chemists and biologists use the principles of spectrophotometry in everyday experiments to provide results and insight into what they are presently studying

The β-D-Galactose inhibitors were all made from β-D-Galactose pentaacetate (15), BF3 ∙ Et2O in DCM and three different alkyne containing alcohols (propargyl alcohol, 3-butyn-1-ol, and 4-pentyn-1-ol). Saturated aqueous NaHCO3 was used to neutralize the solution and after washing and drying the solvent was evaporated under reduced pressure to give the galactose inhibitors. 16 (Scheme 6) was purified by column chromatography (10% MeOH/DCM). The product, however, came too quickly off the column and

could retain it even after it has been involved in the reaction by catalysing the breakdown of lactose in glucose and galactose. Lactose was contained within the milk and as the milk met the immobilised lactase, it began to break down into glucose and galactose. The results show, as the lactose in the milk was left to the lactase for longer, the break down into glucose and galactose increased. This can be seen by the colour change. To begin with we tested the milk for glucose by dipping the clinistix

agglutination of the first couple wells, then no agglutination as the ConA concentration decreased, similar to Row A. Wells B and E that had the Galacatose additive obtained the same titer of the control ConA because ConA does not bind Galactose. Galactose doesn’t interfere with ConA from binding to the sugar residues on the red blood cells. Mannose on the other hand, is an inhibitor to ConA’s binding sites. The Mannose in solution competed with the ConA and did not allow to bind to the sugar

disorder and the exact pathophysiology has is controversial. However, it is most commonly accepted that the main factor is the accumulation of galactose-1-phosphate, gal-1P, which is due to the impairment of galactose-1-phosphate uridylytransferase, GALT. This reaction uses the GALT enzyme as a part of the Leloir pathway which enables the body to process galactose. The GLAT enzyme itself belongs to the histidine triad super family and is a member of branch III. This enzyme shows specific nucleoside monophosphate

ConA is able to agglutinate the cells that means it is biologically active. In our experiment we plated another variable by adding red blood cells and ConA and sugars to see whether the sugars interfered with ConA’s ability to bind we noticed that galactose did not interfere with the agglutination but mannose did interfere with the binding, acting as a competitive inhibitor. We know this was due to ConA’s specificity for mannose and glucose. In our experiment we had 9mLs of dilute ConA and we decreased

It catalyzes a reaction in the bacteria’s like Escherichia coli, where lactose is broken down into glucose and galactose. But, it is difficult to measure the breakdown of lactose so another substrate named as ONPG was used, which breaks itself in to ONP and galactose. It is an enzyme which helps in the process of Lac operon. There are three genes which control the synthesis of beta-galactosidase, galactoside permease, and thiogalactoside