Difference between revisions of "Part:BBa K4437001"
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| − | Nisin is an antimicrobial protein derived from Lactococcus lactis bacteria strain. Amongst all the derivatives of nisin, nisin Q has the highest microbial activity and loses its activity the slowest by inhibiting oxidation. The mechanisms of nisin works by it binding to lipid II present on the cell membrane. This binding results in the creation of a pore and prevents the further synthesis of peptidoglycan - a protein found in the cell membrane- which leads to death. Nisin targets both gram positive and gram negative bacteria, however, is more effective towards gram positive bacteria as they have a higher quantity of peptidoglycan present. | + | Nisin is an antimicrobial protein derived from Lactococcus lactis bacteria strain. Amongst all the derivatives of nisin, nisin Q has the highest microbial activity and loses its activity the slowest by inhibiting oxidation. The mechanisms of nisin works by it binding to lipid II present on the cell membrane. This binding results in the creation of a pore and prevents the further synthesis of peptidoglycan - a protein found in the cell membrane- which leads to death. Nisin targets both gram positive and gram negative bacteria, however, is more effective towards gram positive bacteria as they have a higher quantity of peptidoglycan present. Nisin is pH and thermostable. |
Our project focused on developing a fruit packaging which has been integrated with our antimicrobial peptide-nisin. Nisin has been shown to be effective against many fungi but there is scare research done on its effectiveness on bacteria. We designed a gene fragment containing nisin in order to test its effective against bacteria commonly found on fruit. We characterized its properties using Kirby Bauer tests as well as minimum inhibitory concentration tests. | Our project focused on developing a fruit packaging which has been integrated with our antimicrobial peptide-nisin. Nisin has been shown to be effective against many fungi but there is scare research done on its effectiveness on bacteria. We designed a gene fragment containing nisin in order to test its effective against bacteria commonly found on fruit. We characterized its properties using Kirby Bauer tests as well as minimum inhibitory concentration tests. | ||
Revision as of 04:10, 12 October 2022
NisQ with a N-terminus 6x His-tag (NisQ-His)
Nisin is an antimicrobial protein derived from Lactococcus lactis bacteria strain. Amongst all the derivatives of nisin, nisin Q has the highest microbial activity and loses its activity the slowest by inhibiting oxidation. The mechanisms of nisin works by it binding to lipid II present on the cell membrane. This binding results in the creation of a pore and prevents the further synthesis of peptidoglycan - a protein found in the cell membrane- which leads to death. Nisin targets both gram positive and gram negative bacteria, however, is more effective towards gram positive bacteria as they have a higher quantity of peptidoglycan present. Nisin is pH and thermostable.
Our project focused on developing a fruit packaging which has been integrated with our antimicrobial peptide-nisin. Nisin has been shown to be effective against many fungi but there is scare research done on its effectiveness on bacteria. We designed a gene fragment containing nisin in order to test its effective against bacteria commonly found on fruit. We characterized its properties using Kirby Bauer tests as well as minimum inhibitory concentration tests.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 220
- 1000COMPATIBLE WITH RFC[1000]