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Related Concept Videos

Colloids03:22

Colloids

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Children at play often make suspensions such as mixtures of mud and water, flour and water, or a suspension of solid pigments in water known as tempera paint. These suspensions are heterogeneous mixtures composed of relatively large particles that are visible to the naked eye or can be seen with a magnifying glass. They are cloudy, and the suspended particles settle out after mixing. On the other hand, a solution is a homogeneous mixture in which no settling occurs and in which the dissolved...
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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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Structuring colloidal oat and faba bean protein particles via enzymatic modification.

Outi Nivala1, Outi E Mäkinen1, Kristiina Kruus1

  • 1VTT Technical Research Centre of Finland, Ltd., P.O. Box 1000, FI-02044 VTT, Finland.

Food Chemistry
|April 29, 2017
PubMed
Summary

Enzymatic modification using transglutaminase improved oat and faba bean protein functionality, enhancing colloidal stability and foaming properties. Tyrosinase showed limited benefits, impacting solubility and foaming negatively.

Keywords:
Colloidal stabilityEnzymatic crosslinkingFoamPlant proteinsTransglutaminaseTyrosinase

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Area of Science:

  • Food Science and Technology
  • Biochemistry
  • Protein Chemistry

Background:

  • Plant-based proteins like oat and faba bean are gaining importance as alternatives to animal proteins.
  • Modifying protein colloidal properties is crucial for improving their functionality in food applications.
  • Enzymatic treatments offer targeted approaches to alter protein structures and enhance functional attributes.

Purpose of the Study:

  • To investigate the effects of transglutaminase and tyrosinase on the colloidal properties of oat and faba bean protein isolates.
  • To evaluate the impact of these enzymatic modifications on the colloidal stability and foaming properties of the plant proteins.
  • To understand the differential effects of enzymes based on their distinct mechanisms of action.

Main Methods:

  • Treatment of oat and faba bean protein isolates with transglutaminase (Streptomyces mobaraensis) and tyrosinase (Trichoderma reesei).
  • Analysis of protein crosslinking, particle size, zeta potential, solubility, and foaming properties.
  • Dosage-dependent evaluation of enzyme activity (10, 100, 1000 nkat/g).

Main Results:

  • Transglutaminase extensively crosslinked faba bean protein and moderately crosslinked oat protein, improving their colloidal stability and foaming.
  • Transglutaminase increased zeta-potential and reduced particle size in oat protein, correlating with improved functionality.
  • Tyrosinase exhibited limited crosslinking, reduced oat protein solubility, and impaired foaming properties of both proteins without affecting zeta potential or colloidal stability.

Conclusions:

  • Enzymatic crosslinking with transglutaminase significantly enhances the functional properties of oat and faba bean protein isolates.
  • Tyrosinase has a limited beneficial effect and can negatively impact protein solubility and foaming.
  • The distinct mechanisms of action of transglutaminase and tyrosinase lead to significantly different outcomes in protein functionality.