Structuring colloidal oat and faba bean protein particles via enzymatic modification

Outi Nivala, Outi Mäkinen, Kristiina Kruus, Emilia Nordlund, Dilek Ercili-Cura

Research output: Contribution to journalArticleScientificpeer-review

11 Citations (Scopus)

Abstract

Oat and faba bean protein isolates were treated with transglutaminase from Streptomyces mobaraensis and tyrosinase from Trichoderma reesei to modify the colloidal properties of protein particles in order to improve their colloidal stability and foaming properties. Transglutaminase crosslinked faba bean protein extensively already with 10 nkat/g enzyme dosage. Oat protein was crosslinked to some extent with transglutaminase with higher dosages (100 and 1000 nkat/g). Transglutaminase increased the absolute zeta-potential values and reduced the particle size of oat protein particles. As a result, the colloidal stability and foaming properties were improved. Tyrosinase had limited crosslinking ability on both plant protein materials. Tyrosinase greatly reduced the solubility of oat protein despite limited crosslinking. Tyrosinase did not have effect on zeta-potential or colloidal stability of either protein, but it impaired foaming properties of both. Thus, the crosslinking enzymes studied caused significantly different end product functionality, presumably due to the different mechanism of action.
Original languageEnglish
Pages (from-to)87-95
Number of pages9
JournalFood Chemistry
Volume231
DOIs
Publication statusPublished - 15 Sep 2017
MoE publication typeA1 Journal article-refereed

Fingerprint

Vicia faba
oat protein
protein-glutamine gamma-glutamyltransferase
faba beans
foaming properties
oats
Transglutaminases
Monophenol Monooxygenase
crosslinking
Proteins
Streptomyces mobaraensis
Crosslinking
colloidal properties
proteins
Trichoderma reesei
Zeta potential
protein isolates
plant proteins
dosage
enzymes

Keywords

  • colloidal stability
  • enzymatic crosslinking
  • foam
  • plant proteins
  • transglutaminase
  • tyrosinase

Cite this

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abstract = "Oat and faba bean protein isolates were treated with transglutaminase from Streptomyces mobaraensis and tyrosinase from Trichoderma reesei to modify the colloidal properties of protein particles in order to improve their colloidal stability and foaming properties. Transglutaminase crosslinked faba bean protein extensively already with 10 nkat/g enzyme dosage. Oat protein was crosslinked to some extent with transglutaminase with higher dosages (100 and 1000 nkat/g). Transglutaminase increased the absolute zeta-potential values and reduced the particle size of oat protein particles. As a result, the colloidal stability and foaming properties were improved. Tyrosinase had limited crosslinking ability on both plant protein materials. Tyrosinase greatly reduced the solubility of oat protein despite limited crosslinking. Tyrosinase did not have effect on zeta-potential or colloidal stability of either protein, but it impaired foaming properties of both. Thus, the crosslinking enzymes studied caused significantly different end product functionality, presumably due to the different mechanism of action.",
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Structuring colloidal oat and faba bean protein particles via enzymatic modification. / Nivala, Outi; Mäkinen, Outi; Kruus, Kristiina; Nordlund, Emilia; Ercili-Cura, Dilek.

In: Food Chemistry, Vol. 231, 15.09.2017, p. 87-95.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Nordlund, Emilia

AU - Ercili-Cura, Dilek

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N2 - Oat and faba bean protein isolates were treated with transglutaminase from Streptomyces mobaraensis and tyrosinase from Trichoderma reesei to modify the colloidal properties of protein particles in order to improve their colloidal stability and foaming properties. Transglutaminase crosslinked faba bean protein extensively already with 10 nkat/g enzyme dosage. Oat protein was crosslinked to some extent with transglutaminase with higher dosages (100 and 1000 nkat/g). Transglutaminase increased the absolute zeta-potential values and reduced the particle size of oat protein particles. As a result, the colloidal stability and foaming properties were improved. Tyrosinase had limited crosslinking ability on both plant protein materials. Tyrosinase greatly reduced the solubility of oat protein despite limited crosslinking. Tyrosinase did not have effect on zeta-potential or colloidal stability of either protein, but it impaired foaming properties of both. Thus, the crosslinking enzymes studied caused significantly different end product functionality, presumably due to the different mechanism of action.

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