Lysozyme Activity
| Lysozyme activity | Observed in tears and saliva | | Connie Jamieson | 3/1/2012 |
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Abstract Lysozyme is an enzyme found in both tears and saliva. Each time we blink our eyes, our eyelids wash tears over the surface of our eyes. In addition, our mouth is continually producing saliva. A spectrophotometer set to 450nm was used to measure the effect of lysozyme on bacteria. The absorbance or optical density was measured for each sample at specific times with a total measuring time of twenty minutes. In this experiment, it was shown that lysozyme inhibits microbial growth in saliva and synthetic tears and in lysozyme standard control. The results showed a decrease in absorbance readings over time as the lysozyme activity was observed.
Introduction
In 1922, Alexander Fleming caught a cold and a drop of nasal drainage fell from his nose into a Petri dish that happened to contain microorganisms [1]. He noticed there was a reaction between the bacteria and the fluid from his nose. Fleming realized the fluid contained a bacteriolytic element; he started his research to isolate this compound [1]. Later in 1922, Fleming named this compound lysozyme because of the lysing action on the observed microorganisms [1]. Fleming isolated the enzyme from the egg whites of a hen. After 1930, the bactericidal action of lysozyme was established and numerous studies conveyed that all living organisms produced lysozyme [1].
Tear lysozyme is a long chain glycolytic enzyme secreted by the lachrymal gland [3]. Lysozyme constitutes around twenty to forty percent of the total tear protein [3]. Its concentration in the tear is higher than in any other fluid of the body [1]. This protein has the ability to break down bacterial walls by the enzymatic digestion of mucopolysaccharides [4]. Because of this bactericidal action, lysozyme can be considered as one of the vital elements of the protective tear film barrier against ocular infection [5]. Innate immunity is an
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Abstract Lysozyme is an enzyme found in both tears and saliva. Each time we blink our eyes, our eyelids wash tears over the surface of our eyes. In addition, our mouth is continually producing saliva. A spectrophotometer set to 450nm was used to measure the effect of lysozyme on bacteria. The absorbance or optical density was measured for each sample at specific times with a total measuring time of twenty minutes. In this experiment, it was shown that lysozyme inhibits microbial growth in saliva and synthetic tears and in lysozyme standard control. The results showed a decrease in absorbance readings over time as the lysozyme activity was observed.
Introduction
In 1922, Alexander Fleming caught a cold and a drop of nasal drainage fell from his nose into a Petri dish that happened to contain microorganisms [1]. He noticed there was a reaction between the bacteria and the fluid from his nose. Fleming realized the fluid contained a bacteriolytic element; he started his research to isolate this compound [1]. Later in 1922, Fleming named this compound lysozyme because of the lysing action on the observed microorganisms [1]. Fleming isolated the enzyme from the egg whites of a hen. After 1930, the bactericidal action of lysozyme was established and numerous studies conveyed that all living organisms produced lysozyme [1].
Tear lysozyme is a long chain glycolytic enzyme secreted by the lachrymal gland [3]. Lysozyme constitutes around twenty to forty percent of the total tear protein [3]. Its concentration in the tear is higher than in any other fluid of the body [1]. This protein has the ability to break down bacterial walls by the enzymatic digestion of mucopolysaccharides [4]. Because of this bactericidal action, lysozyme can be considered as one of the vital elements of the protective tear film barrier against ocular infection [5]. Innate immunity is an
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