Cyclodextrin glucanotransferases (CGTase) and maltase enzymes were used for transglycosylation of L-ascorbic acid. Thermophilic CGTases showed the highest efficiency, achieving over 60% transglucosylation.
Area of Science:
Biochemistry
Enzymology
Carbohydrate Chemistry
Background:
L-ascorbic acid (Vitamin C) is a vital nutrient with limited stability.
Enzymatic modification offers a route to enhance the stability of L-ascorbic acid.
Cyclodextrin glucanotransferases (CGTase) and maltase are enzymes capable of transferring glycosyl residues.
Purpose of the Study:
To investigate the transglycosylation of L-ascorbic acid using various glycosyl donors.
To compare the efficiency of CGTases from different bacterial sources (mesophilic, thermophilic, halophilic) and maltase from Saccharomyces cerevisiae.
To determine the optimal conditions for enhancing L-ascorbic acid stability through enzymatic modification.
Main Methods:
Enzymatic transglycosylation reactions were performed using L-ascorbic acid as the acceptor.
Glycosyl donors included starch, maltodextrin, gamma-cyclodextrin, and maltose.
Cyclodextrin glucanotransferases (CGTase) from mesophilic, thermophilic, and halophilic bacilli, and maltase from Saccharomyces cerevisiae were utilized.
Reaction products were analyzed to determine the degree of transglucosylation.
Main Results:
Cyclodextrin glucanotransferases (CGTase) and maltase effectively catalyzed the transglycosylation of L-ascorbic acid.
CGTases derived from thermophilic bacilli demonstrated superior efficiency compared to mesophilic and halophilic counterparts.
Transglucosylation degrees exceeding 60% were achieved, indicating significant modification of L-ascorbic acid.
Conclusions:
Thermophilic bacterial cyclodextrin glucanotransferases are highly effective biocatalysts for the synthesis of L-ascorbic acid derivatives.
Enzymatic transglycosylation presents a promising strategy for improving the stability and potentially the bioavailability of L-ascorbic acid.
Further research into optimizing these enzymatic processes could lead to enhanced Vitamin C formulations.