Oat protein solubility and emulsion properties improved by enzymatic deamidation

Zhongqing Jiang, Tuula S. Sontag-Strohm, Hannu O. Salovaara, Juhani K. Sibakov, Päivi M. Kanerva, Jussi Loponen

Research output: Contribution to journalArticleScientificpeer-review

89 Citations (Scopus)


Oat protein produced by a dry milling process was enzymatically deamidated by a food-grade protein-glutaminase (PG), and the effects on structure, solubility and emulsifying properties of oat proteins were studied. The reactions were conducted at neutral pH and low salt concentration conditions. Oat proteins were deamidated up to a deamidation degree of 59%. The solubility of proteins doubled. Oil-in-water emulsions prepared with the native and deamidated oat proteins differed as the emulsions prepared from oat proteins with high deamidation degree had a more uniform oil droplet particle size and longer stability. Fourier transform infrared (FT-IR) analysis demonstrated that oat protein secondary structure became more flexible by deamidation. Protein-glutaminase mediated deamidation appeared to be a promising technique to improve oat protein functionality such as emulsifying ability and solubility.
Original languageEnglish
Pages (from-to)126-132
JournalJournal of Cereal Science
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed


  • deamidation
  • emulsions
  • oat proteins
  • solubility


Dive into the research topics of 'Oat protein solubility and emulsion properties improved by enzymatic deamidation'. Together they form a unique fingerprint.

Cite this