Factors Affecting Emulsion Capacity as a Measure of Protein Functionality for Nonmeat Proteins

Amundson, C. M.; Sebranek, Joseph G.

doi:10.1111/j.1365-2621.1990.tb06072.x

Cited by 6 publications

(3 citation statements)

References 12 publications

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“…Data in Table 2 show that the emulsion capacities of FFC-PC and DFC-PC were dependent on P H Similar P H dependence of emulsifying capacities of proteins has been reported [19][20][21]. The emulsifying capacities of soluble proteins depend upon the hydrophilic-lipid balance, which is affected by P H .…”

Section: Emulsion Propertiessupporting

confidence: 72%

Solubility, emulsion and foraming properties of coconut (<i>Cocos Nucifera</i>) proteins concentrate.

Horsfall¹,

Achinewhu²,

Ademiluyi³

2008

African Journal of Food, Agriculture, Nutrition and Development

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Full-fat and defatted coconut protein concentrates containing 27.80% and 30.20% proteins (on a dry weight basis), respectively, were prepared from freeze-dried coconut meal samples. Selected functional properties such as: nitrogen solubility, emulsion and foaming properties were determined. Nitrogen solubility was measured in the range of P H 2.0-12.0 in three dispersion media including water, 0.1M NaCl (low salt) and 1.0M NaCl (high salt). The emulsion properties of the protein concentrates were measured at varying P H values (2.0-10.0) and sample concentrations.Foaming properties were determined using same parameters including the use of additives (NaCl solutions and carbohydrates). Below and above the isoelectric P H (4.0-5.0) the nitrogen solubility increased. The coconut protein samples showed a fairly high solubility (more than 54.0% and 53.0%) for full-fat coconut protein concentrate (FFC-PC) and defatted coconut protein concentrate (DFC-PC), respectively at pH 2.0. FFC-PC sample had maximum solubility (more than 73%) at 10.5 and minimum solubility (13.2%) at P H 4.0. On the alkaline P H scale, FFC-PC sample had maximum solubility of more than 43% at P H 10.5 in high salt (1.0M NaCl) solution while DFC-PC sample had maximum solubility of 50.2% in 1.0M NaCl solution and more than 80% in low salt (0.1M NaCl) dispersion medium.The emulsions prepared had good stability. A maximum of 92.5ml/g protein of emulsification capacity, at P H 10.0 and minimum of 45.3ml/g protein at P H 4.0 were obtained for FFC-PC while DFC-PC had a maximum EC of 86.4ml/g protein. FFC-PC samples produced significantly (P≤0.05) higher emulsion capacities than DFC-PC samples at all the dispersion P H and sample concentrations investigated. The FFC-PC samples had a significantly low foaming capacity than the DFC-PC samples at all the tested P H values. Similarly, the foaming capacities of FFC-PC and DFC-PC decreased with increasing P H of the sample medium. Both FFC-PC and DFC-PC foams collapsed completely, after 3hr standing at ambient temperature. Foaming was concentration dependent. The FFC-PC and DFC-PC foams increased sharply at 0.2% NaCl content of the sample slurries and progressed steadily to a peak of 92.0% and 113% in FFC-PC and DFC-PC samples respectively in 0.8% NaCl solution and then declined gradually with increased salt concentration. Addition of polymeric carbohydrates (sucrose, corn starch, gum acacia and pectins) significantly improved foaming properties of the protein concentrates but the foam stabilities were not significantly affected.

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Section: Emulsion Propertiessupporting

confidence: 72%

Solubility, emulsion and foraming properties of coconut (<i>Cocos Nucifera</i>) proteins concentrate.

Horsfall¹,

Achinewhu²,

Ademiluyi³

2008

African Journal of Food, Agriculture, Nutrition and Development

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“…Dekanterewicz et al (1987) measured the EC of proteins based on their water-oil absorption index which describes the relative hydrophilic-lipophilic character of proteins. In addition, Amundson and Sebranek (1990) found that the EC of sodium caseinate (salt of a type of milk protein) was lower than that of soy protein isolate but this investigation was based on different conditions. Furthermore, the oil used was corn oil which was a different oil compared to the oil used in this study (flaxseed oil).…”

Section: Emulsifying Capacity Of Emulsifiersmentioning

confidence: 99%

Characterization of flaxseed oil emulsions

Lee

Choo

2014

J Food Sci Technol

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The emulsifying capacity of surfactants (polysorbate 20, polysorbate 80 and soy lecithin) and proteins (soy protein isolate and whey protein isolate) in flaxseed oil was measured based on 1 % (w/w) of emulsifier. Surfactants showed significantly higher emulsifying capacity compared to the proteins (soy protein isolate and whey protein isolate) in flaxseed oil. The emulsion stability of the flaxseed oil emulsions with whey protein isolate (10 % w/w) prepared using a mixer was ranked in the following order: 1,000 rpm (58 min)≈ 1,000 rpm (29 min) ≈ 2,000 rpm (35 min) >2,000 rpm (17.5 min). The emulsion stability of the flaxseed oil emulsions with whey protein isolate (10 % w/w) prepared using a homogenizer (Ultra Turrax) was independent of the speed and mixing time. The mean particle size of the flaxseed oil emulsions prepared using the two mixing devices ranged from 23.99±1.34 μm to 47.22±1.99 μm where else the particle size distribution and microstructure of the flaxseed oil emulsions demonstrated using microscopic imaging were quite similar. The flaxseed oil emulsions had a similar apparent viscosity and exhibited shear thinning (pseudoplastic) behavior. The flaxseed oil emulsions had L* value above 70 and was in the red-yellow color region (positive a* and b* values).

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“…Although plasma is a protein, like myosin and actin, it has a different native pH plus coagulation and denaturation points (Foegeding et al, 1986). It is known that different nonmeat proteins will function very differently in a processed meat environment (Amundson and Sebranek, 1990) A 10% plasma solution (by weight in water or 76 mg/mL protein) has a pH of approximately 9.0. When incorporating plasma proteins into a buffering system such as postrigor meat, it is important to consider plasma functionality in the pH range of 5.5 to 5.8.…”

Section: Introductionmentioning

confidence: 99%

Characteristics of Bovine Plasma Gels as Affected by pH Sodium Chloride, and Sodium Tripolyphosphate

Knipe

Frye

1990

Journal of Food Science

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A model system, which simulated the pH, sodium chloride (NaCI), and alkaline phosphate (STP) levels of typical processed meat products, was used to determine the effect of NaCI, STP and pH on firmness and percent cooked yield of bovine plasma gels. Bovine plasma gel firmness increased with increasing plasma pH, whereas percent cooked yield was not affected. In contrast, when the pH, of the plasma solutions, was adjusted to a constant 5.6 to simulate the pH and buffering of meat, percent cooked yield was affected; gel firmness was not affected. With increased levels of NaCl and SIP, the percent cooked plasma gel yield increased.

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Factors Affecting Emulsion Capacity as a Measure of Protein Functionality for Nonmeat Proteins

Cited by 6 publications

References 12 publications

Solubility, emulsion and foraming properties of coconut (<i>Cocos Nucifera</i>) proteins concentrate.

Solubility, emulsion and foraming properties of coconut (<i>Cocos Nucifera</i>) proteins concentrate.

Characterization of flaxseed oil emulsions

Characteristics of Bovine Plasma Gels as Affected by pH Sodium Chloride, and Sodium Tripolyphosphate

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