Foaming Properties of Proteins: Evaluation of a Column Aeration Apparatus Using Ovalbumin

HANSCH analysis for quantitative structure-activity relationship (QSAR) was applied to aspartyl proteinases and it was found that higher hydrophobicity, tighter molecular structure, and lower charge are required for milk clotting enzymes compared to proteolytic enzymes. For simplicity in analysis of food proteins, the use of fluorescence hydrophobicity, solubility and steric relating parameters, e.g., SH-SS content and viscosity. are used instead of hydrophobic, electrical and steric parameters in the original QSAR concept. Solubility of milk and soy proteins after different heat treatments was investigated and it was found that aromatic hydrophobicity measured by anilinonaphthalenesulfonate fluorometry and by phenyl-Sepharose chromatography showed better correlation than aliphatic cis-parinarate (CPA) hydrophobicity. The use of CPA hydrophobicity in conjunction with solubility is, therefore, justified in an attempt to avoid multicollinearity in regression study.Significant correlations were found for emulsifying and fat binding capacity of both unheated and heated food proteins when the apparent hydrophobicity with CPA was used as a predictor variable. For foaming property, CPA hydrophobicity measured for unfolded protein (S,) and viscosity played important roles. Se and SH-group content showed good correlation with thermal functionality of proteins.Emulsifying and fat binding properties of crude salt extracts of meat proteins from beef and fish which had been subjected to different processing conditions were explained by using CPA hydrophobicity, solubility and SH-group content.

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“…A method similar t o WANISKA et al [26] In(FS + 0.3) = constant + 1 3 0 . 4~ ( r = 0.855; n = 1 1 ; P < 0.01)…”

Section: For Foamitiy Poprrtiesmentioning

confidence: 99%

Contribution of protein hydrophobicity to its functionality

Nakai

Li‐Chan

Hayakawa

1986

Nahrung

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“…For example, protein solubility has been reported to increase upon succinylation as has been demonstrated for rapeseed preparations (Dua et al, 1996), flax protein isolate (Wanasundara & Shahidi, 1997), oat protein isolate (Mirmoghatadaie et al, 2009), and soy protein isolate (Franzen & Kinsella, 1976a). Improved solubility has been related to the ability of proteins to perform more efficiently as stabilizers in emulsions and foams (Nakai & Li-Chan, 1988;Waniska & Kinsella, 1979), which, in turn, is greatly affected by their ability to absorb at the air-water interface (Wierenga et al, 2005). It has indeed been shown that treatment of a variety of proteins with succinic anhydride leads to increased foam capacity (Dua et al, 1996;Franzen & Kinsella, 1976a;Mirmoghatadaie et al, 2009), although others suggest that succinylation leads to decreased foam expansion capacity (Wanasundara & Shahidi, 1997).…”

Section: Charge Modification By Methylation and Succinylationmentioning

confidence: 99%

Application Potential of Food Protein Modification

Jongh¹,

Broersen²

2012

Advances in Chemical Engineering

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“…pH was measured using a pH meter (Accumet AP61, Fisher Scientific Inc, ON, Canada). Functional properties studied included water holding capacity using AACC method 88-04 (AACC, 1983); fat absorption capacity according to the method described by Lin, Humbert, & Sosulski (1974); protein solubility was measured based on the amount of protein in solution at specified pH values as measured using UV-visible light according to the Bradford method (1976); emulsifying properties were determined with the method described by Pearce & Kinsella (1978); and foaming capacity was studied using the method described by Waniska & Kinsella (1979).…”

Section: Functional Properties Of Pulse Ingredientsmentioning

confidence: 99%

Functional, Physical and Sensory Properties of Pulse Ingredients Incorporated into Orange and Apple Juice Beverages

Zare¹,

Orsat²,

Boye³

2015

JFR

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The objective of this study was to explore the use of pulse ingredients in the development of orange juice and apple juice supplemented beverages. Commercially available pulse ingredients including pea protein (PP), chickpea flour (CPF), lentil flour (LF) and pea fibre (PF) were selected and characterized with respect to specific functional properties (water holding capacity, fat absorption capacity, protein solubility, emulsifying and foaming properties). Apple juice was supplemented with 1-4% pulse ingredients, whereas a supplementation level of 1-2% was used for orange juice. The physical and sensory properties of the supplemented beverages were measured after production and during 3 weeks of refrigerated storage. Sensory attributes for both orange and apple juice supplemented with 1% and 2% pulse ingredients were similar to their respective controls (with and without pectin added). In terms of turbidity, supplementation increased the turbidity of apple juice and orange juice beverages at all levels, in comparison with control and pectin-added control samples. Supplemented samples, showed less satisfactory results in terms of cloud stability and color especially for orange juice beverages in comparison with their respective controls. Overall, while there are some hurdles to be overcome, the results suggest that when used at the 1-2% levels, PP, PF, CPF and LF could serve as potential value-added ingredients for beverage supplementation based on their physical and sensory properties. Further studies are, however, required in this promising area to improve the stability of the final production especially during storage.

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Foaming Properties of Proteins: Evaluation of a Column Aeration Apparatus Using Ovalbumin

Cited by 116 publications

References 14 publications

Contribution of protein hydrophobicity to its functionality

Contribution of protein hydrophobicity to its functionality

Application Potential of Food Protein Modification

Functional, Physical and Sensory Properties of Pulse Ingredients Incorporated into Orange and Apple Juice Beverages

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