Pectinase research paper

Extracting DNA from living things Class practical or demonstration You can extract DNA — to see what it is like — from some plant and some animal material using equipment and chemicals you might find in a kitchen. For more thorough analytical work, you need more control over the components of your chemicals, and it may be worth investing in a kit from one of the major suppliers. This is a rough and ready method that should give reasonable quantities of DNA from quite large quantities of material. Lesson organisation You can run this as a demonstration, or as small group work.

Pectinase research paper

History[ edit ] Very limited information is available about the original discovery of exoenzymes. According to Merriam-Webster dictionary, the term "exoenzyme" was first recognized in the English language in A Course of Lectures Given in the Physiological," by Horace Vernon is thought to be the first publication using this word in that year.

Many bacteria use digestive enzymes to break down nutrients in their surroundings. Once digested, these nutrients enter the bacterium, where they are used to power cellular pathways with help from endoenzymes. Pathogensboth bacterial and fungal, can use exoenzymes as a primary mechanism with which to cause disease.

After moving through the rough endoplasmic reticulumthey are processed through the Golgi apparatuswhere they are packaged in vesicles and released out of the cell.

Breakdown of these Pectinase research paper allows for their incorporation into other metabolic pathways. One of Pectinase research paper best known examples is an exoenzyme produced by Streptococcus pyogenes that causes necrotizing fasciitis in humans.

Coagulase[ edit ] By binding to prothrombincoagulase facilitates clotting in a cell by ultimately converting fibrinogen to fibrin.

Bacteria such as Staphylococcus aureus use the enzyme to form a layer of fibrin around their cell to protect against host defense mechanisms. Fibrin layer formed by Staphyloccocus aureus Kinases[ edit ] The opposite of coagulase, kinases can dissolve clots.

Bacteria such as Clostridium do so by using the enzyme to dissolve collagen and hyaluronic acidthe protein and saccharides, respectively, that hold tissues together.

Hemolysins[ edit ] Hemolysins target erythrocytesor red blood cells. Attacking and lysing these cells allows the pathogen to harm the host organism, and also provides it with a source of iron from the lysed hemoglobinlike the fungus Candida albicans. Examples of digestive exoenzymes[ edit ] Amylases[ edit ] Pancreatic alpha-amylase 1HNY Amylases are a group of extracellular enzymes glycoside hydrolases that catalyze the hydrolysis of starch into maltose.

These enzymes are grouped into three classes based on their amino acid sequences, mechanism of reaction, method of catalysis and their structure. In humans, amylases are secreted by both the pancreas and salivary glands with both sources of the enzyme required for complete starch hydrolysis.

LPL can be found in endothelial cells in fatty tissues, such as adiposecardiacand muscle. Pepsin[ edit ] Discovered inpepsin was one of the first enzymes to be classified as an exoenzyme. Due to its role in the small intestine, trypsin works at an optimal pH of 8. A indicates a positive result, D indicates a negative result.

Bacteria are streaked across the agarand are left to incubate.

Pectinase research paper

The release of the enzyme into the surroundings of the cell cause the breakdown of the macromolecule on the plate. If a reaction does not occur, this means that the bacteria does not create an exoenzyme capable of interacting with the surroundings.

If a reaction does occur, it becomes clear that the bacteria does possess an exoenzyme, and which macromolecule is hydrolyzed determines its identity.

Once the bacteria is streaked on the agar, the plate is flooded with iodine. Since iodine binds to starch but not its digested byproductsa clear area will appear where the amylase reaction has occurred. Bacillus subtilis is a bacterium that results in a positive assay as shown in the picture.

If the bacteria has lipase, a clear streak will form in the agar, and the dye will fill the gap, creating a dark blue halo around the cleared area. Staphylococcus epidermis results in a positive lipase assay. The enzymes that are of particular interest in ethanol production are cellobiohydrolase which solubilizes crystalline cellulose and xylanase that hydrolyzes xylan into xylose.

Genetic Engineering

These applications include the breakdown of agricultural and forestry wastes, working as a feed additive to facilitate greater nutrient uptake by livestock, and as an ingredient in bread making to improve the rise and texture of the bread.

Lipases can serve as a biocatalyst in this reaction Lipases are one of the most used exoenzymes in biotechnology and industrial applications. Lipases make ideal enzymes for these applications because they are highly selective in their activity, they are readily produced and secreted by bacteria and fungitheir crystal structure is well characterized, they do not require cofactors for their enzymatic activity, and they do not catalyze side reactions.Class practical or demonstration You can extract DNA – to see what it is like – from some plant and some animal material using equipment and chemicals you might find in a kitchen.

Pectinase research paper

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Xylanase (EC , endo-(1->4)-beta-xylan 4-xylanohydrolase, endo-1,4-xylanase, endo-1,4-beta-xylanase, beta-1,4-xylanase, endo-1,4-beta-D-xylanase, 1,4-beta-xylan xylanohydrolase, beta-xylanase, beta-1,4-xylan xylanohydrolase, beta-D-xylanase) is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down .

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