A novel dextrin produced by the enzymatic reaction of 6-α-glucosyltransferase. I. The effect of nonreducing ends of glucose with by α-1,6 bonds on the retrogradation inhibition of high molecular weight dextrin

Author:

Yasuda Akiko1,Miyata Manabu1,Sano Osamu1,Sogo Tatsufumi1,Kishishita Seiichiro1,Yamamoto Takuo1,Aga Hajime1,Yamamoto Koryu1

Affiliation:

1. HAYASHIBARA CO., LTD., Okayama, Japan

Abstract

ABSTRACT We prepared a high-molecular-weight modified dextrin (MWS-1000) from a partial hydrolysate of waxy corn starch with a weight average molecular weight of 1 × 106 (WS-1000) using Paenibacillus alginolyticus PP710 α-glucosyltransferase. The gel permeation chromatography showed that the weight average molecular weight of MWS-1000 was almost the same as that of WS-1000. The side chain lengths of WS-1000 and MWS-1000 after isomaltodextranase digestion were also shown to be similar to each other by high-performance anion exchange chromatography with pulsed amperometric detection. Since MWS-1000 confirmed the presence of α-1,6 bonds by enzyme digestibility, methylation, and 1H-NMR analyses, it was presumed that the structure of MWS-1000 was based on the introduction of α-1,6 glucosyl residues at the nonreducing ends of the partial hydrolysate of waxy corn starch. Furthermore, the MWS-1000 solution was not retrograded even during refrigerated storage or after repeated freeze–thaw cycles.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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