Molecular characterization of some amylopectins

L. A. Bello-Pérez, O. Paredes-López, P. Roger, P. Colonna

Research output: Contribution to journalArticlepeer-review

61 Scopus citations

Abstract

Amylopectins from different sources were studied to gain information on their molecular structure. High-performance size-exclusion chromatography was used to assess the profiles of isoamylase-debranched, pullulanase-debranched, β-amylase-hydrolyzed, and α-amylase-hydrolyzed amylopectins. With the two debranching enzymes, two principal fractions were generated. However, amylopectin depolymerized with pullulanase left a higher amount of nondegraded polymer, indicating that the two enzymes follow a different mode of action on amylopectin structure. Profiles obtained after hydrolysis with β- or α-amylase in general showed that shorter chains were generated at higher enzyme concentrations. Static and dynamic light scattering were used to determine solution behavior, molecular weight, gyration radius, and hydrodynamic radius of amylopectins. These parameters suggested substantial structural differences within tested amylopectins.

Original languageEnglish
Pages (from-to)12-17
Number of pages6
JournalCereal Chemistry
Volume73
Issue number1
StatePublished - 1996

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