Linked Life Data

8142045

Source:http://linkedlifedata.com/resource/pubmed/id/8142045

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-4-29
pubmed:abstractText
Nisin is a ribosomally synthesized peptide that has broad-spectrum antibacterial activity, including activity against many bacteria that are food-spoilage pathogens. Nisin is produced as a fermentation product of a food-grade bacterium, and the safety and efficacy of nisin as a food preservative have resulted in its widespread use throughout the world, including the U.S. Nisin is a member of the class of antimicrobial substances known as lantibiotics, so called because they contain the unusual amino acid lanthionine. Lantibiotics, in general, have considerable promise as food preservatives, although only nisin has been sufficiently well characterized to be used for this purpose. As the number of known natural lantibiotics has increased and their useful characteristics have been explored, it has become desirable to synthesize structural analogs of nisin and other lantibiotics that do not occur naturally. The fact that lantibiotics are gene-encoded peptides synthesized by transcription and translation allows structural variants to be generated by mutagenesis. This review focuses on the progress that has been made in the construction and biological expression of genetically engineered nisin structural analogs. For example, a host-vector pair has been engineered that permits the construction of mutants of the structural gene for subtilin, which is a naturally occurring structural analog of nisin. The vector is designed in such a way that the mutant gene can be substituted for the natural subtilin gene in the chromosome of Bacillus subtilis, which in turn directs the transcription, translation, posttranslational modifications, and secretion of the mature form of the structural analog. Several structural analogs have been constructed, and their properties have provided insight into some of the structure-function relationships in lantibiotics, as well as their mechanism of antimicrobial action. These advances are assessed together with potential problems in the future development of nisin analogs as valuable new food preservatives.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1040-8398
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-93
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Nisin as a model food preservative.
pubmed:affiliation
Department of Chemistry and Biochemistry, College of Life Sciences, University of Maryland, College Park 20742-2021.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't