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Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications
Cyclodextrin glucanotransferases (CGTases) are industrially important enzymes that produce cyclic α-(1,4)-linked oligosaccharides (cyclodextrins) from starch. Cyclodextrin glucanotransferases are also applied as catalysts in the synthesis of glycosylated molecules and can act as antistaling agents i...
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Formato: | Texto |
Lenguaje: | English |
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Springer-Verlag
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2804789/ https://www.ncbi.nlm.nih.gov/pubmed/19763564 http://dx.doi.org/10.1007/s00253-009-2221-3 |
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author | Leemhuis, Hans Kelly, Ronan M. Dijkhuizen, Lubbert |
author_facet | Leemhuis, Hans Kelly, Ronan M. Dijkhuizen, Lubbert |
author_sort | Leemhuis, Hans |
collection | PubMed |
description | Cyclodextrin glucanotransferases (CGTases) are industrially important enzymes that produce cyclic α-(1,4)-linked oligosaccharides (cyclodextrins) from starch. Cyclodextrin glucanotransferases are also applied as catalysts in the synthesis of glycosylated molecules and can act as antistaling agents in the baking industry. To improve the performance of CGTases in these various applications, protein engineers are screening for CGTase variants with higher product yields, improved CD size specificity, etc. In this review, we focus on the strategies employed in obtaining CGTases with new or enhanced enzymatic capabilities by searching for new enzymes and improving existing enzymatic activities via protein engineering. |
format | Text |
id | pubmed-2804789 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-28047892010-01-22 Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications Leemhuis, Hans Kelly, Ronan M. Dijkhuizen, Lubbert Appl Microbiol Biotechnol Mini-Review Cyclodextrin glucanotransferases (CGTases) are industrially important enzymes that produce cyclic α-(1,4)-linked oligosaccharides (cyclodextrins) from starch. Cyclodextrin glucanotransferases are also applied as catalysts in the synthesis of glycosylated molecules and can act as antistaling agents in the baking industry. To improve the performance of CGTases in these various applications, protein engineers are screening for CGTase variants with higher product yields, improved CD size specificity, etc. In this review, we focus on the strategies employed in obtaining CGTases with new or enhanced enzymatic capabilities by searching for new enzymes and improving existing enzymatic activities via protein engineering. Springer-Verlag 2009-09-18 2010 /pmc/articles/PMC2804789/ /pubmed/19763564 http://dx.doi.org/10.1007/s00253-009-2221-3 Text en © The Author(s) 2009 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Mini-Review Leemhuis, Hans Kelly, Ronan M. Dijkhuizen, Lubbert Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications |
title | Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications |
title_full | Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications |
title_fullStr | Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications |
title_full_unstemmed | Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications |
title_short | Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications |
title_sort | engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications |
topic | Mini-Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2804789/ https://www.ncbi.nlm.nih.gov/pubmed/19763564 http://dx.doi.org/10.1007/s00253-009-2221-3 |
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