Both plots of data were hen used to find at which concentrations of NP absorption levels, and thus enzyme activity rates, were at their highest across each of the three pH solutions. Based on the results of both experiments, it was found that a pH of 5 is the optimal pH for the productivity of lactate enzyme. INTRODUCTION: Lactate enzyme is used throughout the food industry to break lactose, found in milk, down into the sugars glucose and calaboose.
A deficiency in lactate prevents the breakdown of lactose and results in what is called lactose intolerance, which can lead to digestion problems, cramps, and possibly diarrhea upon ingestion of airy products (Phillips). Through the use of lactate outside of the body, milk is separated into its more viscous and creamy form for the production of dessert products such as ice cream. Many enzymes are proteins that lower the activation energy needed to start chemical reactions that are crucial to the survival of life.
Alike to other proteins enzymes undergo changes in shape based on the surrounding environment, and thus their productivity changes as well. Many factors affect the productivity of enzyme including temperature, concentration of enzyme in a reaction, and pH (Gangland 441). In this experiment the factors of concentration and pH were tested. The tests performed were done so in order to investigate the effects of pH and concentration difference on the overall productivity of lactate enzyme by measuring light absorbency levels of enzyme while changing each of the two variables over time.
It was hypothesized that as concentration of enzyme precipitate in the form of NP was increased so would the absorption levels. It was also hypothesized that if the lactate enzyme reaction took place at a pH of 5 it would have the highest absorbency level as reactions with other pH levels loud change the enzyme’s shape and thus decrease overall absorbency (Bunkhouses). MATERIALS & METHODS: Absorbency levels of a 40% NP concentration in 5 ml were measured at wavelengths ranging from 400-600 NM by 20 NM intervals to find the optimal wavelength for testing.
Absorbency levels of a pH 5 buffer and NP solution were measured at amounts of NP ranging from O to . 40 mol. A blank was made containing 20% lactate enzyme in 5 ml. In a small beaker 15 ml of pH 5 buffer and 6 ml of enzyme were mixed. To each of 5 civets, initially 1 ml of Niacin was added. As soon as 3 ml of GNP was added to the small beaker, creating a . 05 p mole concentration of NP, a timer was started and 4 ml of solution was added to the cavetti labeled 0.
The first hypothesis stated that as the concentration increased so would the absorption level. According to Figure 1 such is the case where as the total concentration of NP increased, the absorption increased steadily in an all but linear fashion. This shows that an increased concentration of enzyme within a reaction, whether lactate or not, could mean increased activity and thus a better catalysis of reactants, such as lactose, into more usable product, such as glucose and calaboose (Phillips).
The second hypothesis stated that the maximum absorption levels from the reaction of GNP to produce NP precipitate would be highest at a pH of 5 and decrease as a solution got farther from that optimal pH value (Bunkhouses). As shown in Figure 2 the tests acted exactly as was originally predicted. Figure 2 mainly shows that lactate enzyme has a very small window of for optimal pH, centering around 5 and decreasing drastically at a pH of 6. This shows that the body’s ability to keep pH values in the digestive tract, as well as other areas, mostly constant, is crucial to the survivability of life.
If pH values are not within the optimum for an enzyme to function, it not only lowers production but also begins to unfold the proteins and thus denatures the enzyme and eventually halts the catalysis of the reaction if the pH is too far to either side of the optimum. This relates back to the rate of enzyme catalysis f lactose in the human digestive tract and how fluctuations in pH can cause issues such as lactose intolerance (Phillips). While the optimum pH range of lactate enzyme is shown to be very small, it is not the case for all enzymes.
Every protein reacts differently when introduced to new surrounding environments. In some cases proteins and thus enzymes can have a large tolerance to changes in pH; such is the case with acid phosphate, an enzyme found throughout the body as well as in blood. Acid phosphate is shown to have an optimum pH ranging anywhere from 4. 9 to 6. 0 (Gangland 444). This reiterates the profound ND necessary ability to regulate pH levels throughout the different systems of the body.
While both concentration of NP and the optimum pH ranges are discussed and tested in this lab, one major factor that was not observed in detail was time. The lactate enzyme catcalled the reaction and each experiment was set to run over the course of 8 minutes, one possible change that could be made would be to run the experiment for a longer period of time to see its effects on the rate of production of NP. In both Figure 2 and 3 the reaction was tested at a final time of 8 minutes, but in each of the tests it was observed that the absorption level as well as the concentration level of NP was still climbing.