Lipases can lipolyze a variety of substrates, such as natural oils, synthetic triglycerides and esters of fatty acids. They are resistant to solvents and have broad spectrum biotechnological applications. Lipase conduct transesterification, hydrolysis and esterification and these are the important class of reactions for food technology applications in fats and oil, dairy, pharmaceuticals and bakery industry. Applications of lipases Applications in food industry The enzymes used in industry are mainly utilized in processing of food, primarily for the modification and processing of biomaterials. A lot of fat breaking lipases are produced on industrial scale.
Enzymes are biological catalysts made of proteins that accelerate chemical reactions by lowering their activation energy therefore increasing the activity rate of the enzyme and more substrates turned into products. The ‘Catalase’ enzyme that was used during this experiment was obtained from peroxisome found in celery which are organelles found in bacteria, plant, and animal cells. It is involved in the breaking down of certain substances and the diminish of reactive oxygen species and that includes hydrogen peroxide (H2O2) which can be a byproduct of the metabolism of oxygen. Hydrogen peroxide is toxic to the cell and so the catalase enzyme is utilised to break down H2O2 to form oxygen molecules and water free of free radicals. As with all
Cellulases are used in the textile industry, in detergents, pulp and paper industry, improving digestibility of animal feeds, in food industry, and these enzymes account for a significant share of the world enzyme market (Sukumaran, et al., 2005). Some of the applications are shown in Table 4. Cellulases were initially investigated for the bioconversion of biomass which gave way to research in the industrial applications of the enzymes in animal feed, food, textiles and detergents and in the paper industry (Sukumaran, et al., 2005). Nowadays with the shortage of fossil fuels and the arising need to find alternative source for renewable energy and fuels, there is a renewal of interest in the bioconversion of biomass using cellulases and other
• Now a days cellulases are commonly used in garments made with a variety of cellulosics such as cotton, linen, lyocell and viscose and polynosic rayon. • Catalase is used in dye house water recycling to eliminate residual hydrogen peroxide following bleaching. • Proteases are used for softening of wool as well as protect it from pilling as well as for sand washing of silk. • In the fuel ethanol application, typically amylases and amyloglucosidases leads to covert a feedstock to a substrate fermented by yeast generates ethanol. • Enzymes are also used in the production of fine chemicals and pharmaceuticals.
Introduction In class, a series of experiments were performed that pertained to the enzyme known as catalase, which converts hydrogen peroxide into oxygen. Due to peroxide being toxic to the tissues of both plants and animals, both possess the enzyme catalase, which breaks into two non-toxic compounds: water and oxygen gas. Enzymes are proteins that react to certain substrates to create a product, and continue doing so afterwards. Methods and Materials To test reactions between catalase and hydrogen peroxide, groups of three to four people were formed. A scale of zero to five was used to describe the reactions, with zero being no reaction at all, one being a slow reaction, and five being a very fast reaction.
isolating the gluten from the starch in the wheat flour. This enzyme is also used in coffee-bean mucilage (Wong and Saddler, 1993). The main desirable properties for xylanases for use in the food industry are high stability and optimum activity at an acid pH. With the advances in the techniques of molecular biology, other uses of xylanases are being discovered. Recently, a recombinant yeast of wine was constructed with the gene for xylanase of Aspergillus nidulans, xlnA, resulting in a wine with a more pronounced aroma than is conventional (Ganga et al., 1999).
Bubbles are produced continuously from the time the tablet enters the water until the time when the reaction between sodium bicarbonate and citric acid ceases. The disappearance of bubbles can be used as a qualitative indicator for the completion of the chemical reaction and the production of the sodium citrate solution. The chemicals in the final solution are sodium bicarbonate, and citric acid, to make a sodium citrate solution. The solute is the Alka-Seltzer tablet and the solvent is the
In plants, catalase is found predominantly in peroxisomes (and also in glyoxysomes) where it functions chiefly to remove the H2O2 formed during photorespiration (or during β-oxidation of fatty acids in glyoxsomes) (Bowler et al., 1992). In spite of its restricted location it may play a significant role in defense against oxidative stress since H2O2 can readily diffuse across membranes. Some of these enzymes have broad substrate specificity while others can only function with one. Catalase is an enzyme related to the cellular control. Catalase catalyses the dismutation of hydrogen peroxide into water and oxygen (Redinbaugh et al.,
o For all three trails the H202 solution in water increase by 10˚C in terms of before and after yeast is added. o The third trial has the same trend of increase as the first two but begins and ends with a 1˚C higher than the previous trials. Data processing: Number of moles for the hydrogen peroxide (H202) 34.02 = Mr Mass = 20g x 0.03 = 0.6 0.6÷34.02 = 0.017 moles Conclusion: What was learned in this lab is temperature rises when a hydrogen peroxide solution in water is activated by yeast. The hypothesis is supported by the data. Referring to what was stated, the Hydrogen peroxide solution did change based yeast that activated the solution, many were similar in temperature.
The acid-catalysed dehydration of a secondary and primary alcohol revealed that the E1 mechanism undergoes and favors rearrangement for a more stable carbocation; this reaction favors a Zaitsev product, which attacks the most substituted beta hydrogen. The base-induced dehydration of a secondary and primary bromide undergoes an E2 mechanism and favors a Hoffman product because of the presence of a sterically bulky base, which attacks the least substituted beta hydrogen. The percent compositions obtained through Gas Chromatography revealed that these favored types of products were present in the highest