Acceptor specificity of amylomaltase from Corynebacterium glutamicum and transglucosylation reaction to synthesize PALATINOSE (cas 13718-94-0) glucosides

Add time:09/08/2019    Source:sciencedirect.com

Acceptor specificity for intermolecular transglucosylation reaction of amylomaltase from Corynebacterium glutamicum was investigated using starch as glucosyl donor and various saccharide acceptors. Maltooligosaccharides (G1–G4), mannose, PALATINOSE (cas 13718-94-0) and sucrose were efficient acceptors; the best one was glucose. This amylomaltase preferred hexose sugar containing the same configuration of C2-, C4- and C6-hydroxyl groups as glucopyranose. Palatinose was chosen as suitable acceptor for the synthesis of palatinose glucosides (PGs). The optimal condition was to incubate 5 U/ml amylomaltase with 7.5 mM palatinose and 1.0% (w/v) soluble potato starch at 30 °C for 24 h. In addition to PGs, maltooligosaccharides were also produced as by product. The product yield was 67.9%, in which the ratio of PGs to maltooligosaccharides was 1:1. Then PGs were separated by Bio-Gel-P2 column chromatography and analyzed by HPAEC. PG1–PG13 were identified with PG1 and PG2 as major products. NMR analysis showed that the PGs produced are novel products, PG1 and PG2 were a tri- and tetra-saccharide with the structure [O-α-d-glucopyranosyl-(1→4)]n-O-α-d-glucopyranosyl-(1→6)-d-fructofuranose, where n = 1–2. PG was less sweet than palatinose and sucrose, more hygroscopic with similar prebiotic activity as palatinose. PGs thus have potential to replace sucrose or palatinose in food products for health benefits.

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