The substrate specificity of amylopectin-debranching enzymes from sweet corn

E. Y.C. Lee, J. J. Marshall, W. J. Whelan

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

An enzyme showing pullulanase activity has been purified from sweet corn, and separated on hydroxylapatite into what appear to be two isoenzyme forms. The specificities of the two fractions are identical. Pullulan, α-limit dextrins and amylopectin β-limit dextrin are rapidly hydrolyzed by the enzyme; amylopectin is slowly debranched, but there is no significant action on glycogen unless the enzyme is allowed to act simultaneously with β-amylase. The enzyme therefore resembles pullulanase [bacterial R-enzyme, EC 3.2.1.9] from Aerobacter aerogenes. The in vivo significance of this enzyme is discussed.

Original languageEnglish (US)
Pages (from-to)365-374
Number of pages10
JournalArchives of Biochemistry and Biophysics
Volume143
Issue number2
DOIs
StatePublished - Apr 1971

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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