The activity of β-glucosidase from the fungus Aspergillus fumigatus was tested on four different substrates. Their activity was used as an analogue to enzymes from the oral bacterium Streptococcus mutans. It was determined that only β-D-galactosidase secreted from S. mutans had the potential to break down lactose in the mouth at a fast-enough rate to increase the sweetness of milk and only if the build-up is enough that the concentration of enzymes is high. This build-up is possible due to the lack of saliva flow during sleep. The two main functions that normally prevents this are the antimicrobial content of saliva and the lack of movement in the oral cavity. Alternately a theory is made to support the idea that secreted enzymes from S. mutans create a build-up of free sugar molecules from degrading the glycan side chains of mucin during the 8 hours of no salivary flow during sleep.
|Uddannelser||Basis - International Naturvidenskabelig Bacheloruddannelse, (Bachelor uddannelse) Bachelor|
|Udgivelsesdato||29 maj 2018|
|Vejledere||Corinna Schiano di Cola|
- Glycosidic bonds
- Enzyme assay
- streptococcus mutans