Characterization of flaxseed oil emulsions

Lee, Pei En; Choo, Wee Sim

doi:10.1007/s13197-014-1495-3

Cited by 17 publications

(10 citation statements)

References 25 publications

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“…ments, 1998). Sharp reduction at lower shear rates, followed by smooth curve at higher shear rates, were due to the deformation and reduction in aggregated particles (Lee and Choo, 2015).…”

Section: Apparent Viscosity Of Wp or Pwp In The Presence Of Slmentioning

confidence: 91%

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Sun

Wang

Guo

2018

Journal of Dairy Science

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Soybean lecithin is often used as a surfactant in food formulation. The aim of this study was to investigate the interactions between soybean lecithin (SL, 0-3%, wt/vol) and whey protein (WP, 10%, wt/vol) or polymerized whey protein (PWP, 10%, wt/vol) induced by heating WP solutions at 85°C for 0 to 20 min at pH 7.0. The samples were evaluated for zeta potential, particle size, morphology, rheological properties, thermal properties, secondary structure, and surface hydrophobicity. Zeta potential of WP increased linearly as SL level increased from 0 to 3%, whereas that of PWP changed with plateau at SL level of 1%, which may be due to the aggregation of SL. The addition of SL increased the particle size and apparent viscosity of both WP and PWP. All the samples exhibited different morphology depending on SL level and heating time according to transmission electron microscopy images. Whey protein showed obviously decreased gelation time and increased storage modulus in the presence of SL. Differential scanning calorimetry curves confirmed the effects of SL on the thermal properties of both WP and PWP. Circular dichroism spectra indicated that SL had effects on the secondary structure of both WP and PWP. The changes in surface hydrophobicity indicated the hydrophobic interactions between WP/PWP and SL. Data indicate that the physicochemical and functional properties of WP and PWP can be altered by adding soybean lecithin.

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“…ments, 1998). Sharp reduction at lower shear rates, followed by smooth curve at higher shear rates, were due to the deformation and reduction in aggregated particles (Lee and Choo, 2015).…”

Section: Apparent Viscosity Of Wp or Pwp In The Presence Of Slmentioning

confidence: 91%

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Sun

Wang

Guo

2018

Journal of Dairy Science

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“…[23] For a creaming index (CI), the emulsions were stored in a refrigerator (4°C) for two weeks and CI was assessed using the former equation. [24] Apparent viscosity measurement of emulsions A Brookfield viscometer (Brookfield RV, DVII, USA) equipped with a small sample adaptor (spindle no. 21) was applied to measure the apparent viscosity of emulsions at 25°C.…”

Section: Emulsion Activity (Ea) and Emulsion Stability (Es)mentioning

confidence: 99%

The emulsifying properties of Persian gum (Amygdalus scoparia Spach) as compared with gum Arabic

Golkar

Taghavi

Dehnavi

2018

International Journal of Food Properties

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The current study compares the emulsifying properties of Persian gum (PG) and gum Arabic (GA) in emulsions. The effects of concentration (0.5-3% w/v PG, 2.5-15% w/v PG), pH (2-7), ionic strength [NaCl, CaCl 2 (0-300 mM)], and temperature (40-90°C) were investigated. The surface-volume mean diameter (D 32 ) of the emulsions showed that the minimum values were 9.89 ± 0.68 and 4.52 ± 0.03 µm for emulsions containing 1.5% w/v PG and 15% w/v GA, respectively. In addition, the zeta potential of PG and GA emulsion changed from −23.5 to −39.5 and −30.5 to −46.0 mV, respectively. The interfacial tensions of PG and GA emulsions were varied in the ranges of 34.0-15.0 and 29.0-9.0 mN/m, respectively. Changes in the D 32 value of GA emulsions showed were not significantly different (p > 0.05) with respect to the effects of pH, NaCl, CaCl 2, and temperature. The NaCl concentration had no significant effect on D 32 ; but its value decreased from 13.11 to 5.70 µm as the CaCl 2 concentration increased. The interfacial tension of PG significantly increased with decreasing pH 7-2 and increasing 0-300 mM salts. After heating (25-90°C), the D 32 values of PG and GA emulsions changed to 11.04-14.54 and 4.21-4.21 μm, respectively. The results of this study can be useful for the application of PG as an emulsifier in beverage emulsions. ARTICLE HISTORY

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“…They modulate the expression of genes that control lipid metabolism [ 13 ], thermogenesis and energetic expenditure [ 14 ], but their benefit on human health is mainly associated to the binding of PCs to macromolecules such as enzymes [ 15 , 16 ]. In this scenario, specific binding of dietary PCs with enzymes of the digestive tract that are responsible for the lipid absorption in the small intestine may be considered one of the main mechanisms by which PCs can prevent obesity [ 11 , 17 , 18 , 19 , 20 , 21 ]. It has been suggested that the inhibition of digestive enzymes could decrease postprandial hyperlipidemia and obesity [ 22 ].…”

Section: Introductionmentioning

confidence: 99%

Polyphenolic Compounds and Digestive Enzymes: In Vitro Non-Covalent Interactions

et al. 2017

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The digestive enzymes–polyphenolic compounds (PCs) interactions behind the inhibition of these enzymes have not been completely studied. The existing studies have mainly analyzed polyphenolic extracts and reported inhibition percentages of catalytic activities determined by UV-Vis spectroscopy techniques. Recently, pure PCs and new methods such as isothermal titration calorimetry and circular dichroism have been applied to describe these interactions. The present review focuses on PCs structural characteristics behind the inhibition of digestive enzymes, and progress of the used methods. Some characteristics such as molecular weight, number and position of substitution, and glycosylation of flavonoids seem to be related to the inhibitory effect of PCs; also, this effect seems to be different for carbohydrate-hydrolyzing enzymes and proteases. The digestive enzyme–PCs molecular interactions have shown that non-covalent binding, mostly by van der Waals forces, hydrogen binding, hydrophobic binding, and other electrostatic forces regulate them. These interactions were mainly associated to non-competitive type inhibitions of the enzymatic activities. The present review emphasizes on the digestive enzymes such as α-glycosidase (AG), α-amylase (PA), lipase (PL), pepsin (PE), trypsin (TP), and chymotrypsin (CT). Existing studies conducted in vitro allow one to elucidate the characteristics of the structure–function relationships, where differences between the structures of PCs might be the reason for different in vivo effects.

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Characterization of flaxseed oil emulsions

Cited by 17 publications

References 25 publications

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

The emulsifying properties of Persian gum (Amygdalus scoparia Spach) as compared with gum Arabic

Polyphenolic Compounds and Digestive Enzymes: In Vitro Non-Covalent Interactions

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