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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.
Yasuda, Akiko; Miyata, Manabu; Sano, Osamu; Sogo, Tatsufumi; Kishishita, Seiichiro; Yamamoto, Takuo; Aga, Hajime; Yamamoto, Koryu.
Affiliation
  • Yasuda A; HAYASHIBARA CO., LTD., Okayama, Japan.
  • Miyata M; HAYASHIBARA CO., LTD., Okayama, Japan.
  • Sano O; HAYASHIBARA CO., LTD., Okayama, Japan.
  • Sogo T; HAYASHIBARA CO., LTD., Okayama, Japan.
  • Kishishita S; HAYASHIBARA CO., LTD., Okayama, Japan.
  • Yamamoto T; HAYASHIBARA CO., LTD., Okayama, Japan.
  • Aga H; HAYASHIBARA CO., LTD., Okayama, Japan.
  • Yamamoto K; HAYASHIBARA CO., LTD., Okayama, Japan.
Biosci Biotechnol Biochem ; 85(7): 1737-1745, 2021 Jun 24.
Article in En | MEDLINE | ID: mdl-33836083
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Dextrins / Glucose / Glucosyltransferases Language: En Journal: Biosci Biotechnol Biochem Journal subject: BIOQUIMICA / BIOTECNOLOGIA Year: 2021 Type: Article Affiliation country: Japan

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Dextrins / Glucose / Glucosyltransferases Language: En Journal: Biosci Biotechnol Biochem Journal subject: BIOQUIMICA / BIOTECNOLOGIA Year: 2021 Type: Article Affiliation country: Japan