Designing starch derivatives with desired structures and functional properties via rearrangements of glycosidic linkages by starch-active transglycosylases

Xiaoxiao Li, Yu Wang, Jing Wu, Zhengyu Jin, Lubbert Dijkhuizen, Birte Svensson, Yuxiang Bai*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Modification of starch by transglycosylases from glycoside hydrolase families has attracted much attention recently; these enzymes can produce starch derivatives with novel properties, i.e. processability and functionality, employing highly efficient and safe methods. Starch-active transglycosylases cleave starches and transfer linear fragments to acceptors introducing α-1,4 and/or linear/branched α-1,6 glucosidic linkages, resulting in starch derivatives with excellent properties such as complexing and resistance to digestion characteristics, and also may be endowed with new properties such as thermo-reversible gel formation. This review summarizes the effects of variations in glycosidic linkage composition on structure and properties of modified starches. Starch-active transglycosylases are classified into 4 groups that form compounds: (1) in cyclic with α-1,4 glucosidic linkages, (2) with linear chains of α-1,4 glucosidic linkages, (3) with branched α-1,6 glucosidic linkages, and (4) with linear chains of α-1,6 glucosidic linkages. We discuss potential processability and functionality of starch derivatives with different linkage combinations and structures. The changes in properties caused by rearrangements of glycosidic linkages provide guidance for design of starch derivatives with desired structures and properties, which promotes the development of new starch products and starch processing for the food industry.
Original languageEnglish
JournalCritical Reviews in Food Science and Nutrition
Number of pages14
ISSN1040-8398
DOIs
Publication statusAccepted/In press - 2024

Keywords

  • α-glucanotransferase
  • Glycosidic linkages
  • Starch modification
  • Catalytic mechanism
  • Structure
  • Physiochemical properties

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