Heating Reduces Proso Millet Protein Digestibility via Formation of Hydrophobic Aggregates

Paridhi Gulati, Aixia Li, David Holding, Dipak Santra, Yue Zhang, Devin J. Rose

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

Proso millet protein has reported structural similarities with sorghum. In order to explore the potential of this crop as an alternative protein source for people with gluten sensitivity, in vitro protein digestibility was analyzed. Dehulled proso millet flour was subjected to various processing techniques (dry heating and wet heating). Regardless of the processing technique there was a significant decline in digestibility of protein in proso millet flour when compared with unprocessed flour (from 79.7 ± 0.8% to 42.0 ± 1.2%). Reduced digestibility persisted even when cooking with reducing agents. Heating in the presence of urea (8 M) and guanidine-HCl (4.5 M) prevented the reduction in observed digestibility (urea cooked 77.4 ± 0.8%; guanidine HCl cooked 84.3 ± 0.9%), suggesting formation of hydrophobic aggregates during heating in water. This was supported by an increase in surface hydrophobicity upon cooking. Thus, the proso millet protein, termed panicin, forms hydrophobic aggregates that are resistant to digestion when subjected to heat.

Original languageEnglish (US)
Pages (from-to)1952-1959
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume65
Issue number9
DOIs
StatePublished - Mar 8 2017

Keywords

  • disulfide bonds
  • in vitro
  • prolamins
  • sorghum
  • urea

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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