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

Carbohydr Res. 1977 Aug:57:281-9. doi: 10.1016/s0008-6215(00)81937-0.

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 alpha-limit dextrins containing (1 leads to 4)- and (1 leads to 6)-alpha-D-glucosidic bonds. The structures of the limit dextrins containing a single (1 leads to 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 alpha-limit dextrins. The structures of the limit dextrins afforded information about those (1 leads to 4)-alpha-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-alpha-maltotriosyl-D-glucose, 6(3)-alpha-maltotriosylmaltotriose, and 6(3)-alpha-maltotriosylmaltotetraose were examined.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amylases / metabolism*
  • Amylopectin
  • Humans
  • Salivary Glands / enzymology*
  • Substrate Specificity
  • alpha-Amylases / metabolism*

Substances

  • Amylopectin
  • Amylases
  • alpha-Amylases