Enzyme triggered release of aroma molecules from oil-in-water emulsions

Rebecca C. Wong, Ryan Elias, Joshua D. Lambert, Perla Relkin, John Neil Coupland

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The goal of this work is to demonstrate enzyme-triggered release of a hydrophobic compound from a supercooled oil-in-water emulsion. Ethyl octanoate (EO, 100ppm) is added to a dispersion of crystalline or supercooled liquid eicosane droplets (10wt%, d=200nm) stabilized with sodium caseinate (1wt%) and incubated either with or without trypsin. In the absence of trypsin, the dispersions were stable and the headspace EO concentration in equilibrium with the liquid droplets is less than that in equilibrium with the solid droplets. In the presence of trypsin, the emulsions physically destabilize over 6h as the caseinate is hydrolyzed and the supercooled liquid eicosane crystalizes initially rapidly but then more slowly. Incubation with trypsin does not affect the headspace EO concentration in equilibrium with solid droplets but for supercooled liquid droplets the headspace concentration increases from a low to a high plateau after 16h incubation consistent with the droplets having crystalized. The equilibrium data are modeled in terms of the air-oil and air-caseinate solution partition coefficients of EO (9.0×10-5 and 4.6×10-3 respectively) assuming no interaction between crystalline fat and EO. This work shows that a digestive enzyme can trigger crystallization in an emulsion and be used to control the release of an entrapped hydrophobic compound.

Original languageEnglish (US)
Pages (from-to)19-23
Number of pages5
JournalColloids and Surfaces A: Physicochemical and Engineering Aspects
Volume422
DOIs
StatePublished - Apr 5 2013

Fingerprint

trypsin
Emulsions
emulsions
enzymes
Oils
Enzymes
oils
Trypsin
Molecules
Water
liquids
water
molecules
Liquids
air
fats
Crystalline materials
partitions
plateaus
actuators

All Science Journal Classification (ASJC) codes

  • Surfaces and Interfaces
  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

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title = "Enzyme triggered release of aroma molecules from oil-in-water emulsions",
abstract = "The goal of this work is to demonstrate enzyme-triggered release of a hydrophobic compound from a supercooled oil-in-water emulsion. Ethyl octanoate (EO, 100ppm) is added to a dispersion of crystalline or supercooled liquid eicosane droplets (10wt{\%}, d=200nm) stabilized with sodium caseinate (1wt{\%}) and incubated either with or without trypsin. In the absence of trypsin, the dispersions were stable and the headspace EO concentration in equilibrium with the liquid droplets is less than that in equilibrium with the solid droplets. In the presence of trypsin, the emulsions physically destabilize over 6h as the caseinate is hydrolyzed and the supercooled liquid eicosane crystalizes initially rapidly but then more slowly. Incubation with trypsin does not affect the headspace EO concentration in equilibrium with solid droplets but for supercooled liquid droplets the headspace concentration increases from a low to a high plateau after 16h incubation consistent with the droplets having crystalized. The equilibrium data are modeled in terms of the air-oil and air-caseinate solution partition coefficients of EO (9.0×10-5 and 4.6×10-3 respectively) assuming no interaction between crystalline fat and EO. This work shows that a digestive enzyme can trigger crystallization in an emulsion and be used to control the release of an entrapped hydrophobic compound.",
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AU - Wong, Rebecca C.

AU - Elias, Ryan

AU - Lambert, Joshua D.

AU - Relkin, Perla

AU - Coupland, John Neil

PY - 2013/4/5

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AB - The goal of this work is to demonstrate enzyme-triggered release of a hydrophobic compound from a supercooled oil-in-water emulsion. Ethyl octanoate (EO, 100ppm) is added to a dispersion of crystalline or supercooled liquid eicosane droplets (10wt%, d=200nm) stabilized with sodium caseinate (1wt%) and incubated either with or without trypsin. In the absence of trypsin, the dispersions were stable and the headspace EO concentration in equilibrium with the liquid droplets is less than that in equilibrium with the solid droplets. In the presence of trypsin, the emulsions physically destabilize over 6h as the caseinate is hydrolyzed and the supercooled liquid eicosane crystalizes initially rapidly but then more slowly. Incubation with trypsin does not affect the headspace EO concentration in equilibrium with solid droplets but for supercooled liquid droplets the headspace concentration increases from a low to a high plateau after 16h incubation consistent with the droplets having crystalized. The equilibrium data are modeled in terms of the air-oil and air-caseinate solution partition coefficients of EO (9.0×10-5 and 4.6×10-3 respectively) assuming no interaction between crystalline fat and EO. This work shows that a digestive enzyme can trigger crystallization in an emulsion and be used to control the release of an entrapped hydrophobic compound.

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