Structural Characterization, In Vitro Digestion Property, and Biological Activity of Sweet Corn Cob Polysaccharide Iron (III) Complexes

Molecules. 2023 Mar 26;28(7):2961. doi: 10.3390/molecules28072961.

Abstract

This study aimed to enhance the utilization value of sweet corn cob, an agricultural cereal byproduct. Sweet corn cob polysaccharide-ron (III) complexes were prepared at four different temperatures (40 °C, 50 °C, 60 °C, and 70 °C). It was demonstrated that the complexes prepared at different temperatures were successfully bound to iron (III), and there was no significant difference in chemical composition; and SCCP-Fe-C demonstrated the highest iron content. The structural characterization suggested that sweet corn cob polysaccharide (SCCP) formed stable β-FeOOH iron nuclei with -OH and -OOH. All the four complexes' thermal stability was enhanced, especially in SCCP-Fe-C. In vitro iron (III) release experiments revealed that all four complexes were rapidly released and acted as iron (III) supplements. Moreover, in vitro antioxidant, α-glucosidase, and α-amylase inhibition studies revealed that the biological activities of all four complexes were enhanced compared with those of SCCP. SCCP-Fe-B and SCCP-Fe-C exhibited the highest in vitro antioxidant, α-glucosidase, and α-amylase inhibition abilities. This study will suggest using sweet corn cobs, a natural agricultural cereal byproduct, in functional foods. Furthermore, we proposed that the complexes prepared from agricultural byproducts can be used as a potential iron supplement.

Keywords: in vitro antioxidant activity; in vitro digestion property; in vitro hypoglycemic activity; structural characterization; sweet corn cob polysaccharide-iron (III) complexes.

MeSH terms

  • Antioxidants*
  • Digestion
  • Iron / chemistry
  • Polysaccharides / chemistry
  • Polysaccharides / pharmacology
  • Zea mays* / chemistry
  • alpha-Amylases
  • alpha-Glucosidases

Substances

  • Antioxidants
  • alpha-Glucosidases
  • Iron
  • Polysaccharides
  • alpha-Amylases