Protein Solubility, Emulsifying Stability and Capacity of Two Defatted Corn Germ Proteins

Lin, C. S.; Zayas, J.F.

doi:10.1111/j.1365-2621.1987.tb05890.x

Cited by 28 publications

(18 citation statements)

References 11 publications

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“…In the screening phase for temperature selection, less than 30% protein was extracted from finished germ by the saline solution at 40°C and this amount did not increase when 50 or 60°C was used (Table 1). In contrast, Lin and Zayas [22] reported that solubility of corn germ protein decreased at higher incubation temperatures (50-70°C). Aggregation of protein at the higher temperatures or an already-existing denatured state caused by the drying step during wet-milling may have prevented more finished germ protein from being isolated.…”

Section: Protein Extraction Efficienciesmentioning

confidence: 84%

Extraction and Functional Properties of Non‐Zein Proteins in Corn Germ from Wet‐Milling

Hojilla-Evangelista

2011

J Americ Oil Chem Soc

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This study was conducted to evaluate the extractability of wet-milled corn germ protein, characterize the recovered protein and identify its potential applications. Protein was extracted from both wet germ and finished (dried) germ using 0.1 M NaCl as solvent. The method involved homogenization, stirring, centrifugation, dialysis and freeze-drying. Factors evaluated were temperature (40, 50, or 60°C) and the presence of reducing or denaturing agents. The recovered protein was analyzed for proximate composition and functional properties. Protein recovery was greater from wet germ. For both germ samples, protein recovery was not improved by using higher temperatures; thus, subsequent extractions were done at 40°C. Addition of 2% SDS and 1% b-mercaptoethanol to the solvent nearly doubled protein yield; but, SDS-PAGE indicated some protein denaturation. The recovered freezedried proteins from both germ samples were least soluble at pH 2.0-4.0, but solubility increased at higher pH values. Wet germ protein extract was more soluble than finished germ protein at all pH values; however, the finished germ protein showed much better foaming and emulsifying properties and water-holding capacity.

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Section: Protein Extraction Efficienciesmentioning

confidence: 84%

Extraction and Functional Properties of Non‐Zein Proteins in Corn Germ from Wet‐Milling

Hojilla-Evangelista

2011

J Americ Oil Chem Soc

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“…Correlation was established between EC and protein solubility and the effects of pH on emulsion formation [19]. As protein solubility increased the capacity of a protein to form and stabilize emulsion was improved.…”

Section: Hydrophobic and Hydrophilic Properties Of Proteinsmentioning

confidence: 99%

“…Defatted com genn protein flour (CGPF) produced by a hexane extraction method had good nutritional quality [116], high water retention, fat binding, emulsifying capacity, and emulsion stability [64,117]. The level of fat emlllsified during sausage batter processing affected the textural and water binding properties of the finished product [104].…”

Section: Corn and Wheat Germ Proteinsmentioning

confidence: 99%

“…The solubility of CGPF preparations for pH values between 6 and 8 was determined to relate protein solubility to EC and ES [117]. A knowledge of the emulsifying properties of defatted CGPF is necessary to evaluate their potential use as food additives.…”

Section: Corn Proteinsmentioning

confidence: 99%

“…Functional properties have been tested for two CGPF preparations, supercritical carbon dioxide (SC-COz)-defatted and hexane-defatted in relation to their protein solubility, emulsifying capacity and emulsion stability in a model system that corresponded to the conditions for sausage batter processing [117]. Within a pH range of 7-9 of the protein solution, higher protein solubility was observed, which certainly increased the EC of that protein.…”

Section: Corn Proteinsmentioning

confidence: 99%

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Emulsifying Properties of Proteins

Zayas

1997

Functionality of Proteins in Food

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Emulsification is the most important process in the manufacturing of many formulated foods. Food emulsions are classified as macroemulsions with droplet size of 0.2 to 50 f..lm. Emulsion represents a heterogeneous mixture of fat globules. Food emulsions can be of the oil in water (OfW) or water in oil (W/0) type. The difference between OfW and W/0 emulsions is that an OfW emulsion commonly exhibits a creamy texture, while a W/0 system has greasy textural properties.Protein emulsifying activity is the ability of the protein to participate in emulsion formation and to stabilize the newly created emulsion. The emulsifying capacity is the ability of the protein solution or suspension to emulsify oil. Emulsifying properties are useful functional characteristics which play an important role in the development of new sources of plant protein products for uses as foods. Proteins are the components that dominate in most food emulsions. A significant number of foods are emulsions, dispersions, and foams, and in these systems, proteins, in combination with lipids and carbohydrates, are important stabilizers. The review of Halling [1] on the use of food proteins as stabilizers of emulsions and foams, provides extensive references to earlier reviews and reports. Walstra [2] presented the physical and colloidal aspects of emulsification and whipping for milk and milk products.Required functional properties of proteins are affected by product utilization, for example in dairy foods, emulsifying properties are important, and milk substitutes should possess proper emulsifying capacity (EC), color, mouthfeel, flavor and solubility characteristics. In comminuted and other meats, limiting functional properties are: water holding capacity, emulsifying capacity, and emulsion stability (ES), fat binding and resistance of the functional properties to heat treatment. Comparative studies of the emulsifying properties of different proteins are difficult until all factors influencing protein emulsifying properties and methods of testing are standardized.The characteristics used to describe emulsifying properties of proteins are EC, ES, and emulsifying activity (EA). They are used to describe the emulsifying properties of proteins in food emulsion systems. EC is presented as the amount of J. F. Zayas, Functionality of Proteins in Food © Springer-Verlag Berlin Heidelberg 1997 1. Diffusion of proteins to the interface, 2. Protein adsorption at the interface, 3. Changes of protein conformation resulted from unfolding and reorientation of protein molecules. 140The first step in surface film formation is protein diffusion to the interface.During emulsification the soluble protein diffuses and concentrates at the interface. The diffusion is influenced by protein concentration, molecular size, temperature, pH, ionic strength, and solubility. Soy proteins diffuse slowly to the interface when compared to other food proteins (whey proteins and caseinates). The difference in diffusion rate is probably related to the large size of soy protein particles...

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Foods, Nonconventional

Litchfield

2000

Kirk-Othmer Encyclopedia of Chemical Technology

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Nonconventional foods can be produced from chemicals such as carbohydrates, hydrocarbons, and industrial organic chemicals by processes such as microbiological, enzymatic, or chemical synthesis; or from existing natural products containing carbohydrates, proteins, and fats by physical, chemical, microbiological, or enzymatic modification. Examples of nonconventional foods include single‐cell proteins, eg, dried cells of microorganisms such as algae bacteria, actinomycetes, yeasts, molds, and higher fungi; derived plant and animal products, eg, leaf meals and leaf protein concentrates, and fish and meat protein concentrates and isolates; synthetic products, eg, carbohydrates, fats, proteins, peptides, amino acids, and vitamins prepared by chemical, microbiological, or enzymatic synthesis; and manufactured or combination foods, eg, engineered, restructured, or textured foods. Nonconventional foods must have nutritional value to humans or animals, and functional value in foods which ensure quality and social and cultural acceptability. They also must meet regulatory agency requirements for safety for human consumption, including freedom from toxic, mutagenic, and carcinogenic substances and pathogenic microorganisms.

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Protein Solubility, Emulsifying Stability and Capacity of Two Defatted Corn Germ Proteins

Cited by 28 publications

References 11 publications

Extraction and Functional Properties of Non‐Zein Proteins in Corn Germ from Wet‐Milling

Extraction and Functional Properties of Non‐Zein Proteins in Corn Germ from Wet‐Milling

Emulsifying Properties of Proteins

Foods, Nonconventional

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