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Recommended: Discussion on enzymes
Starch hydrolyzing enzymes comprise of 30% of worldwide enzyme consumption and are the second most important commercial enzymes with 25% of world enzyme market share. Among them α-amylase is the most important starch hydrolytic enzyme and has diverse applications in starch processing, baking, automatic dishwashing detergents, textile desizing, medicine, pulp and paper, and brewing industry. However, requirements for each industry are very specific, mainly concerning with pH, oxidative stability, chelator resistance, and temperature behavior. Thus, a single enzyme cannot fulfill all the industrial demands and therefore, there is a constant demand for the search for novel enzyme having better thermostability, broad pH working range, surfactant stable and raw starch digesting properties to suit various industrial applications.
Nature harbors several novel microorganisms which may produce novel enzymes suitable for industrial applications. Thus, an effort was made to isolate strains capable of producing high-titer of industrially important amylases, which could retain their activity and stability under various industrial conditions by screening the soil sample of Assam, India. Subsequently, the taxonomic identification of isolated strains was done by polyphasic approach, and then the culture conditions of such potent bacteria were optimized for maximizing their α-amylase production. Thereafter, efforts were also made to isolate, purify and biochemically characterize the α-amylase(s) from promising microbial strains, and also to search for the possible industrial applications of such purified enzymes. Successively, the gene for promising α-amylase was cloned and expressed in E. coli to produce commercially acceptable yields.
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...spectively after six hours of incubation at 60°C. It also formed deep holes and erodes the smooth surface of all the tested starch granules, indicating its usefulness in starch processing industries. The bread supplementation studies with the AmyBS-I and commercial α-amylase (Himedia) showed that the AmyBS-I supplemented bread had better bread amelioration quality as compared to control and commercial enzyme supplemented ones. The partially purified α-amylase from B. subtilis strain AS01a was also used for immobilization studies on magnetic nanoparticles (MNP) and it was found that with the immobilization of resulted in ~ 26-fold increase in specific activity was observed as compared to the free enzymes. The continuous starch hydrolysis experiment by MNP bound enzyme showed that there was significant increase in starch hydrolysis as compared to free unbound enzymes.
The isolate possesses some enzymes required for hydrolytic reactions. Hydrolytic enzymes found to be secreted from the bacterium, are -amylase, casein, and PYRase. In the starch hydrolysis and casein tests, there was a zone of clearing around the bacterium, which was indicative of the secreted enzymes necessary to break down starch and casein. In the PYR test, the presence of PYRase was detected by a color change to red on the PYR disc after the addition of the PYR reagent (p-dimethylaminocinnamaldehyde). Hydrolytic enzymes for which the EI tested negative were urease, gelatinase, and DNAse. In the Urea Hydrolysis test, it was observed that the urea broth did not have a color change, indicating that there was no urease secreted to break down urea in the broth. Similarly, there was no gelatinase present to break down gelatin in the Gelatin Hydrolysis test, so the nutrient gelatin remained solid. It was concluded that the EI does not possess DNase because there was no clearing zone around the bacteria, indicating that DNA had not been
Streak plate technique was used to isolate pure culture for each bacteria (2). The Gram stain was used to determine Gram reaction and morphology of each bacteria (2) Selective and differential media such as, salt agar, MacConkey agar and blood agar were used for bacterial identification (2). Gelatin deeps were inoculated to detect production of gelatinase (2). Starch Agar plate were inoculated to detect amylase (2). Ocular reticle used to determine bacteria size (2). Motility deeps were inoculated to detect motility on bacteria (2). Thioglycollate broth used to determine oxygen requirements (2). Carbohydrate fermentation
Finally, the last part of the experiment examined the enzyme activity at different pH levels. Four sets of 11 tubes were set up in this part. The procedure for this part is the same as before, but 4 other buffers were substituted for the standard pH 7.3 phosphate buffer. Set A used the 5.5 pH buffer while set B used the 6.5 pH buffer. The buffer of pH 8.5 was used for set B and for set D the pH was 9. The absorbance readings for 4 sets were taken and recorded in table 13. Using the linear equation that the best-fit line gave for each set, the Km and the Vmax of each set were determined. Then, table 15 was made by dividing the Vmax by the Km. of the four pHs. The Vmax and Km of the control set were also used to make
called an active site. This active site is made by a few of the amino
Most of everyone loves deep-fried foods, especially French fries and fried chicken; one can find them in almost every fast-food restaurant for a cheap price. Early in 2002, the Swedish National Food Administration found that certain foods form a compound called acrylamide when fried or baked; this compound is toxic and found to cause cancer in lab rats. This discovery became a concern as to the possibility that humans will also develop cancer from eating large amounts of fried foods.
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: = == ==
The artificial enzymes have a higher optimum temperature, (temperature at which they react fastest), and so also have a higher point of denaturisation. This means that the enzymes did not denature at 60 degrees Celsius as I predicted, so a reading at 80 degrees Celsius was taken. In this temperature the enzymes did denature as expected meaning that the reaction did not occur, so had the slowest rate of reaction possible. Evaluation ---------- I believe that the results recorded for the experiments undergone are reliable enough to base my conclusions upon.
Because of its undeniable and scientifically-proven powerful antioxidant properties, catalase enzyme has a wide commercial application. Primarily in combination with the enzyme glucose oxidase, catalase is used as a preserving system in mayonnaise and egg products such as whole eggs or dried egg white, in the preparation of milk and cheese, in the manufacture of baked goods, beverages, textile industry, cosmetic industry (as face mask), and in cleaning agents for contact lenses, for the elimination of the hydrogen peroxide that is present in some products, (Worthington Biochemical Corporation,
Effect of Lead Ions On Bacterial and Fungal Amylase Amylases are enzymes, which hydrolyse starch into Maltose. There are two types of amylase: Alpha amylase that degrades starch, which is a polysaccharide, into fragments 10 glucose residues long. Beta Amylase breaks these down into maltose, which is a disaccharide of two glucose molecules joined together. Both enzymes work by hydrolysis of the glycosidic link in carbohydrates. Enzyme amylase are produced from different sources but in my experiment I will be concerned with Bacterial and fungal amylase.
at a volume of 4cm3. The preliminary work also proved to me that my basic method worked without any setbacks that may affect my results. Variables:.. The variables involved in the rate of reaction between amylase and starch are. The volume of amylase The volume of starch
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
If I was to do this experiment again I might use a Fungi amylase to
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
I blanked it with 2 cm³ water, 1 cm³ amylase and 3 drops of iodine.
and a fall in temperature will slow them down. In many cases a rise in