Hi, need to submit a 2250 words paper on the topic Clostridium Botulinum. Clostridium botulinum is widely present in the soil and grows best under conditions where there is low oxygen. They can produce spores, which helps them to remain dormant until favorable conditions are available that support their growth. Clostridium botulinum is “sensitive to low pH (<.4.6), lower Aw (0.93), and moderately high salt (5.5%)” (Dilbaghi and Sharma 2007: 22). The spores produced by the bacillus are heat-resistant in nature (they are killed only at very high temperatures, above 1000 degrees Celsius) and are mainly found in foods that lack proper processing or are nominally processed. Foods that are affected by the C. botulinum bacteria are vegetables with low acidities, such as, spinach, mushroom, pepper, corn, asparagus and green beans. fruits such as peaches and figs and also improperly cooked, smoked or fermented poultry, eggs, meat, and fish, sold in sealed containers.
C. botulinum .can produce seven different forms of immunological toxins, designated by the alphabets A to G, with types A, B, E, and sometimes F (quite rarely) causing food poisoning in humans. Other related species such as .Clostridium butyricum and Clostridium baratii .are also capable of producing Botulinum exotoxins. The toxins are synthesized as single large polypeptides that work by affecting the cholinergic mechanism of the presynaptic terminal of a motor neuron and cuts off transmission of acetylcholine across the neuromuscular connection, which results in neuromuscular obstruction, and subsequently causing flaccid paralysis (Sugiyama .1980).
The single polypeptide chain of a Botulinum toxin has an average molecular weight of 150 kDa, and in this form, it shows a low potency (Todar 2009). When the toxin is cleaved by a bacterial protease or by .gastric proteases to form two chains, a light chain with 50 kDa as molecular weight and a heavier chain with 100kDa as molecular weight are formed, and the chains remain linked by a disulfide bond (Fig 1). The lighter fragment of the polypeptide chain, which is a protease (an enzyme) is the most potent form of toxin that is available naturally, and it acts as “a zinc (Zn2+) endopeptidase similar to tetanus toxin with proteolytic activity located at the N-terminal end (see image below). The heavy chain (~100 kD – amino acids 449-1280) provides cholinergic specificity and is responsible for binding the toxin to pre-synaptic receptors. it also promotes light-chain translocation across the endosomal membrane” (Kedlaya, 2012).
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