Application Of Cellulases On Juice Recovery

The use of multiple test tubes and Parafilm was used for each experiment. Catechol, potato juice, pH 7 phosphate buffer, and stock potato extract 1:1 will be used to conduct the following experiments: temperature effect on enzyme activity, the effect of pH on enzyme action, the effect of enzyme concentration, and the effect of substrate concentration on enzyme activity. For the temperature effect on enzyme activity, three test tube were filled with three ml of pH 7 phosphate buffer and each test tube was labels 1.5 degrees Celsius, 20 °C, and 60 °C. The first test tube was placed in an ice-water bath, the second test tube was left at room temperature, and the third test tube was placed in approximately 60°C of warm water. After filling the test tubes with three ml of the

The role of an enzyme is to catalyse reactions within a cell. The enzyme present in a potato (Solanum Tuberosum) is catechol oxidase. In this experiment, the enzyme activity was tested under different temperature and pH conditions. The objective of this experiment was to determine the ideal conditions under which catechol oxidase catalyses reactions. In order to do this, catechol was catalyzed by catechol oxidase into benzoquinone at diverse temperatures and pH values. The enzyme was exposed to its new environment for 5 minutes before the absorbance of the catechol oxidase was measured at 420 nm using a spectrophotometer. The use of a spectrophotometer was crucial for the collection of data in this experiment. When exposed to hot and cold temperatures, some enzymes were found to denature causing the activity to decrease. Similarly, when the pH was too high or low, then the catechol oxidase enzyme experienced a significant decrease in activity. It can be concluded after completing this experiment that the optimal pH for catechol oxidase is 7 and that the prime temperature is 20º C. Due to the fact that the catechol oxidase was only tested under several different temperatures and pH values, it is always possible to get a more precise result by decreasing the increments between the test values. However, our experiment was able to produce accurate results as to the

The purpose of this lab was to study the effect of varying the substrate concentration of Hydrogen peroxide (H2O2) on the rate of peeled potato catalase enzyme activity, on the decomposition of H2O2. This experiment was carried out by diluting the 6% H2O2 with distilled water to decrease the concentration, and then placed in a test tube. A small piece of filler paper disc was coated with the enzyme before it was submerged to the bottom of the substrate hydrogen peroxide solution. The stop timer was started immediately when the filter paper disc touched the bottom and the timer was stopped when the filter paper reached the surface. The results of the experiment showed a linear correlation between concentration of the substrate and the rate of enzyme activity. Overall, as the concentration of H2O2 was decreased, the rate of reaction had decreased.

Yeast is a fungus that can generate glucose into energy without using any oxygen molecules. We tested the fermenting ability of yeast from two different carbon sources: glucose and aspartame. We hypothesized that yeast is unable to use the carbon sources of aspartame. To do this, we decided to use both carbon sources in the same concentration. Each carbon source was mixed with the same amount of yeast solution. The experiment group of 5.5 mM aspartame solution was compared with the control group of 5.5mM glucose solution. We recorded the rate of fermentation for glucose and aspartame in the Vernier Lab Quest. The fermentation rate of aspartame is a negative number, and glucose is a positive number. Our results show that yeast was unable to ferment aspartame as yeast fermented glucose. The results indicate that aspartame has no effect on yeast fermentation rate because yeast do not catabolize aspartame because it does not have the appropriate enzymes to break it down.

Experimental Design Since the independent variable we are manipulating is the pH of the solution and the dependent variable is the decomposition reaction rate, we will investigate our hypothesis using five different concentrations of hydrochloric acid solution with the catalase enzyme from a potato. Each acid concentration will provide a different pH level, with the most acidic being the lowest on the pH scale and the least acidic being closer to the baseline of 7. To obtain the five

The selected isolate Gur1 (6 mm disc) was grown on basal salt media supplemented with 2% carboxymethyl cellulose (CMC) at 28º C until substantial growth was recorded (Hankin and Anagnostaksis 1975). The Petri plates were flooded with congo red solution (0.1%), and after 5 min congo red solution was discarded. The plates were then washed with 1M NaCl solution, and allowed to stand for 15-20 min. The clear zone was observed around the colony when the enzyme had utilized by

In the documentation provided by you the items you desire are identified as part of an observance in a recommended service. As with all religious accommodations these items are provided to inmates when donations are received for the specific observance. To date no donated items have been received from your organization which would enable you to observe as your religious organization so states.

When testing how different temperatures affect the enzyme function of the yeast mixture, it was found that the higher the temperature, the more CO2 was produced by the enzymes after seventy-five minutes, as shown in Figure 1. According to Figure 1, when the temperature was 37° C the CO2 produced was slightly over 4 milliliters, whereas at a temperature of 20° C there were slightly over 2.7 milliliters produced at the seventy-five minute mark. This showed that the optimal temperature range for this particular enzyme was to be at or above 37° C.

To anaerobically break down glucose into ethanol and carbon dioxide, yeast will use the zymase enzyme which catalyses the catabolic fermentation reaction according to the induced fit model. The zymase enzyme will form weak bonds with it’s specific complementary substrate (a glucose molecule), inducing a conformational change in the shape of the enzyme and substrate. In a catabolic reaction this stresses the substrate bonds of the substrate so that they break easily, allowing the substrate to seperate into desired products; in this case ethanol and carbon dioxide. After the zymase enzyme has facilitated the reaction the weak enzyme-substrate bonds break and the enzyme can be reused. This model of enzyme substrate binding reduces the activation energy required in the reaction, allowing fermentation to occur quicker and more readily.

Bacterial tannase enzyme were purified from the 24 h old solid state culture filtrate of E. cloacae by two-step purification protocol consisting of ammonium sulfate precipitation (60%) followed by chromatography techniques, Ion exchange chromatography (DEAE) and Gel filtration chromatography (Sephadex G-100). In the final step, Ion exchange chromatography enzyme was purified 1.96 fold with 20.25% recovery and specific activity of 5.51U/mg, and then gel filtration chromatography enzyme was purified 1.45 fold with 29.97 recovery and specific activity of 4.08 U/mg (Table ). The purification of tannase from microbial source generally involves sequential chromatography techniques, mainly, ion exchange, gel filtration chromatography techniques (Qiu et al., 2011; Goncalves et al., 2011). In these steps, a considerable amount of enzyme is lost due to auto lysis and some remain physically adsorbed on the matrix. To overcome these constraints, single double step purification systems, like ion exchange, gel filtration

The enzyme catechol oxidase, extracted from masticated potato (Solanum tuberosum) lowers activation energy, as it is a catalyst. This enzyme can react with catechol to produce benzoquinone and water. Catechol oxidase is tested against a multitude of phosphate buffers, acidic, neutral and basic pH values, and chilled temperatures to hot temperatures. The purposes of these testes were to determine the optimal temperature and pHs at which catechol oxidase performs at. The method to measure results was the usage of a spectrophotometer (Vernier Spectrouis Plus). The spectrophotometer measures the absorbance levels of the pigment excreted when catechol oxidase undergoes a reaction. The high the absorbance, the more products produced and vise versa. The highest absorbance for the catechol oxidase submitted to different temperatures measured an average 0.6018 nm, when at 20 C. The highest absorbance for the catechol oxidase submitted to different pH values measured two averages of 0.658 at pH 6 and 0.6464 at pH 7. The conclusion taken from the available data explains that the optimal pH for catechol oxidase was between pH 6 and 7 and the optimal temperature was at room temperature at 20C.

Lignin is composed of non-phenolic and phenolic structures. White-rot basidiomycetes such as Phanerochaete chrysosporium, Trametes versicolor, Trametes Trogii, Pleurotus ostreatus, Lentinula edodes, Irpex lacteus, Fomes fomentarius and Cerrena maxima have been found to be the most efficient lignin-degrading microorganisms studied. It has been reported that lignin degrading fungi secreted enzymes collectively termed “ligninases” (Figure 2). These include two ligninolytic families; phenol oxidases (laccases) and peroxidases [lignin peroxidase (LiP), manganese peroxidase (MnP) and versatile peroxidase (VP)]. In delignification process, ligninolytic enzymes have been applied in different methods as fungal delignification, enzymatic delignification, laccase-mediator system (LMS), and integrated fungal fermentation (IFF) (Angel, 2002; Martin, 2002; Pérez et al., 2002; Alcalde, 2007; Hammel and Cullen, 2008; Plácido and Capareda, 2015). Lignolytic peroxydases

Pectinase is an enzyme that breaks down pectin, a polysaccharide found in plant cell walls. Commonly referred to as pectic enzymes, they include pectolyase, pectozyme and polygalacturonase. They are released when plant material is naturally fermented. (Pedrolli, 2009)

Until recent decades, unpasteurized fruit juices have been traditionally considered safe in respect to pathogenic microorganisms, due to their acidic conditions (Whitney, 2005). However, with several global foodborne illness outbreaks, various studies have determined that certain bacterial, viral and parasitic pathogens are able to withstand the acidic condition and be potentially infectious. In particular, upon consumption of various types of fruit juices, several infections caused by Escherichia coli O157:H7, Salmonella spp., and even hepatitis A were documented (Mihajlovic et al., 2013). As a consequence, FDA have set HACCP regulations which ensures a 5 log reduction of the specific pathogens present in the juice products (FDA, 2001).

2011 2nd International Conference on Biotechnology and Food Science IPCBEE vol.7 (2011) © (2011) IACSIT Press, Singapore