The action pattern of human salivary alpha-amylase in the vicinity of the branch points of amylopectin

Mukhtar Abdullah, William J. Whelan, Brian J. Catley

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Salivary alpha-amylase hydrolyses amylopectin in stages. At the end of the so-called second stage, there are present glucose, maltose, and a series of α-limit dextrins containing (1→4)- and (1→6)-α-d-glucosidic bonds. The structures of the limit dextrins containing a single (1→6)-bond were examined. Six such dextrins were found. Of these, two were capable of being further hydrolysed by alpha-amylase, whereas the remaining four were true, amylase-resistant α-limit dextrins. The structures of the limit dextrins afforded information about those (1→4)-α-d-glucosidic bonds of amylopectin that are capable of being cleaved by salivary alpha-amylase and those that are resistant. In order to define further the action of alpha-amylase, the alpha-amylolytic products of 6-α-maltotriosyl-d-glucose, 63-α-maltotriosylmaltotriose, and 63-α-maltotriosylmaltotetraose were examined.

Original languageEnglish (US)
Pages (from-to)281-289
Number of pages9
JournalCarbohydrate Research
Volume57
Issue numberC
DOIs
StatePublished - Aug 1977

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

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