Wait a second!
More handpicked essays just for you.
More handpicked essays just for you.
How enzymes work essay university
How enzymes work biology essay
How enzymes work biology essay
Don’t take our word for it - see why 10 million students trust us with their essay needs.
Recommended: How enzymes work essay university
Problem: Which enzymes pectinase or cellulase or a combination of pectinase and cellulase will break down the applesauce the most?
Hypothesis: If 4 combinations of apple sauce and enzymes are tested than the applesauce with pectinase will break down more because pectinase is used to speed up the extraction of fruit juice from fruit including apple and sapota.
Introduction: The students are proving for Mossa and Bogdan Apple juice inc. which enzymes Pectinase or cellulase or a combination of both will create more apple juice and which enzyme(s) will be more cost effective to use in the company's business production of Apple juice. The students did some research on Cellulase and Pectinase, they found that Pectinase is used to speed up the extraction
…show more content…
of fruit juice from fruit including apple and sapota whereas cellulase helps breaks down cellulose in the cell wall. List of materials: 100 grams of Apple sauce 15 ml of Pectinase 15 ml of Cellulase 4 plastic cups 2 stirring rods 1 graduated cylinder 1 funnel 4 filter papers 2 pipettes Procedure: The students take 25 grams of applesauce and they put in it in a plastic cup.
After that they add 5 drops of pectinase into the cup. Proceeding that the students take the stirring rod and stir until the enzymes are mixed evenly into the apple sauce then they wait for 10 minutes. The students put the mixture aside. Then the students put the funnel into the graduated cylinder and put the filter paper in a the in the funnel. The students take the mixture and carefully put it in the filter paper and the students gently squeeze the juice out of the mixture. After that the students record the amount of juice in ml. The students repeat steps 1-7 twice for 2 trials of data. The students repeat steps 1-8 but make the mixture with cellulase. After that the students make another mixture with both enzymes they put 3 drops of each enzymes in the mixture. After repeating steps 1-9 the students make another mixture without enzymes and repeat steps 1-8 as the …show more content…
control. IV: The enzymes put into the apple sauce DV: The amount of apple juice produced Control: Mixture without enzymes Data table: Enzymes Trial 1 Trial 2 Average (ml) None (Control) 19ml 14ml 16.5ml Pectinase 17ml 17ml 17ml Cellulase 14ml 14ml 14ml Pectinase and Cellulase 15ml 17ml 16ml Graph: Discussion: When the students tested the applesauce with just pectinase, there was 17 ml of apple juice filtered through the paper on average.
With the other enzyme, cellulase, on average there was 14 ml of apple juice strained from the apple sauce. The student's control consisted of no enzymes or water. The average amount of apple juice produced from the control was 16.5 ml. When the enzymes of pectinase and cellulase were combined and added to the applesauce, the average of apple juice created was 16 ml. The students data proves that pectinase withdraws the most apple juice out of all the different enzymes and combinations tested. The students found that the Pectinase is a lot cheaper to use for the company’s apple juice production. The investment over all for Pectinase is cheaper at $50 per liter whereas the Cellulase is $100 per liter and the Pectinase breaks the applesauce down more than the Cellulase. Pectinase is by far the most cost
effective. Conclusion: The enzyme of pectinase created the most amount of apple juice. The data that we collected supported our hypothesis. After this lab we could test another enzyme with pectinase and cellulase. Could another enzyme break down more apple sauce then pectinase? Does pectinase break down any other type of carbohydrate within a fruit?
In this experiment the enzyme peroxidase and the substrate hydrogen peroxide were not mixed initially, instead they were both placed in separate tubes and were incubated at a specific temperature, to prevent hydrogen peroxide from undergoing any reaction with peroxidase until they both acquire the required temperature.
The purpose of this study is to analyze the activity of the enzyme, catalase, through our understanding
These labels indicated the lactose solution that was be placed into the mini-microfuge tubes. The varying lactose ph solutions were obtained. The four miniature pipets were then used, (one per solution,) to add 1mL of the solution to the corresponding mini-microfuge tubes. When this step is completed there were two mini-microfuge tubes that matched the paper towel. Then, once all of the solutions contained their respective lactose solutions, 0.5mL of the lactase enzyme suspension was added to the first mini-microfuge tube labeled LPH4 on the paper towel, and 4 on the microfuge tube. As soon as the lactase enzyme suspension was added to the mini-microfuge tube, the timer was started in stopwatch mode (increasing.) When the timer reached 7 minutes and 30 seconds, the glucose test strip was dipped into the created solution in the mini-microfuge tube for 2 seconds (keep timer going, as the timer is also needed for the glucose strip. Once the two seconds had elapsed, the test strip was immediately removed, and the excess solution was wiped gently on the side of the mini-microfuge tube. The timer was continued for 30 addition seconds. Once the timer reached 7:32 (the extra two seconds accounting for the glucose dip), the test strip was then compared the glucose test strip color chart that is found on the side of the glucose test strip
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
Materials used in the experiment included 5-7 g of the potato tissue, 50ml of 2.0M phosphate buffer coffee filter and guaiacol dye.
What effect will varying concentrations of pectinase, 0%, 1%, 1.5%, 2%, 2.5% and 3%, have on the rate of reaction, volume(cm3) and clarity of juice produced, of the apple (Malus domestica) variety of New Zealand Rose incubated at a temperature of 45C for 20 minutes?
2nd step heat the mixture: Make sure the agarose dissolves. Wait until it boils and when you are going to transfer the mixture, wear gloves to avoid getting burnt. Transfer the mixture into a removable gel tray.
In this experiment I will be finding out which fruit juice contains the most vitamin C. I will be using a method similar to titration but I will be using a syringe instead of a burette.
In this lab, the hydrogen peroxide will act as the substrate to the beef liver catalase solution. The rate at which oxygen gas is evolved will be measured to determine the rate at which the enzyme is working. This lab utilizes various elements such as varying temperature, state and concentration to demonstrate how changes can affect the rate of activity. The change in catalase concentration should affect the enzyme rate by increasing as the concentrat...
Pectinases (also known as polyglacturonase) is the collective term for a row of enzymes that are able to break down or to transform pectin. They include pectolyase, pectozyme and polyglacturonase. These enzymes are ubiquitous part of the fruit juice and wine-making industries. Pectinases form the gel which stabilizes the cell walls of the plant cells. Other molecules, like cellulose, are embedded in it. Some fruits form Pectinases during natural gestation. Pectic substance is a generic name used for the compounds that are acted upon by the Pectinolytic enzymes. They are high molecular weight, negatively charged, acidic, complex glycosidic macromolecules (polysaccharides) that are present in the plant kingdom. They are present as the major components of middle lamella between the cells in the form of calcium pectate and magnesium pectate. These substances are a group of complex colloidal polymeric materials, composed largely of a backbone of anhydrogalacturonic acid units.
Garbage enzymes were produced based on the formulation of three parts of fruit peels, one part of brown sugar and ten parts of water were mixed together (The Star, 2009) and fermented in 5L plastic bottle at room temperature for three months.
Fruits and their juices are important sources of mineral nutrients in human nutrition (Pennington and Fisher, 2010; Ribeiro et al., 2009; Wall, 2006). The worldwide consumption of fruit juices has been increasing requiring more and better production efficiency, sustained by technological development (AIJN, 2010). In general, the 100% fruit juice products are obtained by two different types of processing. Pure juices are produced directly by fruit extraction, usually by squeezed fruit, as raw material, obtained without dilution and without the addition of sugars (Bates et al. 2001). Juices from concentrate are produced by adding an adequate amount of water to concentrate previously obtained by partial dehydration of the fruit juices (Ashurst, 2005; Keshani et al., 2010; Mobhammer et al., 2006). The addition of sugars, up to 150 g/L is allowed in Portugal, but only if clearly stated on the product label. These products are manufactured in varieties containing only one fruit or mixtures of two or more fruits; they are pasteurized and presented to the market in two states of preservation: refrigeration with three months shelf life and at room temperature with twelve month shelf life.