Enzymatic Polymerization of α-D-Maltosyl Fluoride Utilizing α-Amylase as the Catalyst: A New Approach for the Synthesis of Maltooligosaccharides

Shiro Kobayashi, Junji Shimada, Keita Kashiwa, Shin ichiro Shoda

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)

Abstract

Maltooligosaccharides have effectively been prepared by polycondensation of α-d-maltosyl fluoride (1) using α-amylase as the catalyst in a mixed solvent of methanol-phosphate buffer (pH 7) (enzymatic polymerization). The structure of the resulting oligomers was confirmed by means of 13C NMR spectroscopy as well as by an enzymatic hydrolysis experiment. The most appropriate reaction conditions for the production of the higher oligomers were to use methanol/buffer = 2/1 as solvent and to employ an amylase enzyme from Aspergillus oryzae as the catalyst. The stereo-and regioselective formation of an a(1→4)-glycosidic bond is explained by a mechanism involving “double inversion” of the Cl carbon configuration of monomer 1. Other substrates such as d-maltose, α-D-maltosyl fluoride, and α-d-glucosyl fluoride gave no condensation products.

Original languageEnglish
Pages (from-to)3237-3241
Number of pages5
JournalMacromolecules
Volume25
Issue number12
DOIs
Publication statusPublished - 1992 Jun 1

ASJC Scopus subject areas

  • Organic Chemistry
  • Polymers and Plastics
  • Inorganic Chemistry
  • Materials Chemistry

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