Microbial fructosyltransferases and the role of fructans
Microbial fructosyltransferases are polymerases that are involved in microbial fructan (levan, inulin and fructo-oligosaccharide) biosynthesis. Structurally, microbial fructosyltransferase proteins share the catalytic domain of glycoside hydrolases 68 family and are grouped in seven phylogenetically...
Saved in:
Published in: | Journal of applied microbiology Vol. 106; no. 6; pp. 1763 - 1778 |
---|---|
Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Oxford, UK
Oxford, UK : Blackwell Publishing Ltd
01-06-2009
Blackwell Publishing Ltd Blackwell |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | Microbial fructosyltransferases are polymerases that are involved in microbial fructan (levan, inulin and fructo-oligosaccharide) biosynthesis. Structurally, microbial fructosyltransferase proteins share the catalytic domain of glycoside hydrolases 68 family and are grouped in seven phylogenetically related clusters. Fructosyltransferase-encoding genes are organized in operons or in clusters associated with other genes related to carbohydrate metabolism or fructosyltransferase secretion. Fructosyltransferase gene expression is mainly regulated by two-component systems or phosphorelay mechanisms that respond to sucrose availability or other environmental signals. Microbial fructans are involved in conferring resistance to environmental stress such as water deprivation, nutrient assimilation, biofilm formation, and as virulence factors in colonization. As a result of the biological and industrial importance of fructans, fructosyltransferases have been the subject of extensive research, conducted to improve their enzymatic activity or to elucidate their biological role in nature. |
---|---|
Bibliography: | http://dx.doi.org/10.1111/j.1365-2672.2008.04120.x ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 1364-5072 1365-2672 |
DOI: | 10.1111/j.1365-2672.2008.04120.x |