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Levansucrases: a review of their catalytic properties, product characterization and applications in food systems.

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Title: Levansucrases: a review of their catalytic properties, product characterization and applications in food systems.
Authors: Wong Min, Muriel1 (AUTHOR), Karboune, Salwa1 (AUTHOR) salwa.karboune@mcgill.ca
Source: Critical Reviews in Food Science & Nutrition. 2025, Vol. 65 Issue 34, p8937-8957. 21p.
Subjects: Fructooligosaccharides, Food industry, Oligosaccharides, Biosynthesis, Bioactive compounds, Enzyme regulation, Glycosyltransferases, Research & development
Abstract: Owing to the promising physiological effects of levan and levan-type fructooligosaccharides, levansucrase (LS, EC 2.4.1.10) has garnered much interest in recent years for pharmaceutical, cosmetic, and food applications. LS is a fructosyl-transferase that catalyzes the synthesis of complex oligosaccharides by acquiring a fructosyl residue from a donor molecule and performing non-Leloir transfer to an acceptor molecule. The mechanism of action of LS toward various carbohydrates has been well documented, and increasing interest has been drawn to the ability of alkyl and phenolic compounds to act as acceptor substrates for LS-catalyzed transfructosylation reactions. Many studies have also focused on improving the production of LSs and their product spectrum, whether by increasing their overall activity or shifting their selectivity toward a particular reaction. With these advances, the possibility of applying LS to food processing has gradually gained momentum. This review provides a comprehensive discussion of the catalytic properties of LS and full characterization of its reaction products. We then discuss some applications of microbial LS for the biogeneration of functional ingredients in food systems. [ABSTRACT FROM AUTHOR]
Copyright of Critical Reviews in Food Science & Nutrition is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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  Data: Levansucrases: a review of their catalytic properties, product characterization and applications in food systems.
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  Data: <searchLink fieldCode="AR" term="%22Wong+Min%2C+Muriel%22">Wong Min, Muriel</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Karboune%2C+Salwa%22">Karboune, Salwa</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> salwa.karboune@mcgill.ca</i>
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  Data: <searchLink fieldCode="JN" term="%22Critical+Reviews+in+Food+Science+%26+Nutrition%22">Critical Reviews in Food Science & Nutrition</searchLink>. 2025, Vol. 65 Issue 34, p8937-8957. 21p.
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  Data: <searchLink fieldCode="DE" term="%22Fructooligosaccharides%22">Fructooligosaccharides</searchLink><br /><searchLink fieldCode="DE" term="%22Food+industry%22">Food industry</searchLink><br /><searchLink fieldCode="DE" term="%22Oligosaccharides%22">Oligosaccharides</searchLink><br /><searchLink fieldCode="DE" term="%22Biosynthesis%22">Biosynthesis</searchLink><br /><searchLink fieldCode="DE" term="%22Bioactive+compounds%22">Bioactive compounds</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+regulation%22">Enzyme regulation</searchLink><br /><searchLink fieldCode="DE" term="%22Glycosyltransferases%22">Glycosyltransferases</searchLink><br /><searchLink fieldCode="DE" term="%22Research+%26+development%22">Research & development</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: Owing to the promising physiological effects of levan and levan-type fructooligosaccharides, levansucrase (LS, EC 2.4.1.10) has garnered much interest in recent years for pharmaceutical, cosmetic, and food applications. LS is a fructosyl-transferase that catalyzes the synthesis of complex oligosaccharides by acquiring a fructosyl residue from a donor molecule and performing non-Leloir transfer to an acceptor molecule. The mechanism of action of LS toward various carbohydrates has been well documented, and increasing interest has been drawn to the ability of alkyl and phenolic compounds to act as acceptor substrates for LS-catalyzed transfructosylation reactions. Many studies have also focused on improving the production of LSs and their product spectrum, whether by increasing their overall activity or shifting their selectivity toward a particular reaction. With these advances, the possibility of applying LS to food processing has gradually gained momentum. This review provides a comprehensive discussion of the catalytic properties of LS and full characterization of its reaction products. We then discuss some applications of microbial LS for the biogeneration of functional ingredients in food systems. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Critical Reviews in Food Science & Nutrition is the property of Taylor & Francis Ltd and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1080/10408398.2025.2513521
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        Text: English
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        Type: general
      – SubjectFull: Food industry
        Type: general
      – SubjectFull: Oligosaccharides
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      – SubjectFull: Biosynthesis
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      – SubjectFull: Bioactive compounds
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      – SubjectFull: Enzyme regulation
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      – SubjectFull: Glycosyltransferases
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              Text: 2025
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