Emulsifying Properties of Chemically Deamidated Corn (Zea Mays) Gluten Meal

Flores, Idalia; Cabra, Vanessa; Quirasco, Maricarmen; Farrés, Amelia; Gálvez, Amanda

doi:10.1177/1082013210366750

Cited by 14 publications

(9 citation statements)

References 38 publications

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“…The results in the present study are consistent with those of Motoki et al, working on glutamine-specific deamidation of α s1 -casein by transglutaminase, who found no changes in molecular weights. Similarly, Flores et al, working on maize protein isolate emulsions, found similar electrophoretic band patterns for deamidated and nondeamidated emulsions, despite their difference in emulsion stability. The fact that films prepared from transglutaminase-treated kafirin microparticles were rough (Figure Bn–p) may be attributed to an increase in negative charges in the kafirin due to deamidation, making the microparticles less soluble in acetic acid casting solution.…”

Section: Resultsmentioning

confidence: 80%

Improvement in Water Stability and Other Related Functional Properties of Thin Cast Kafirin Protein Films

Anyango

Taylor

2011

J. Agric. Food Chem.

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Improvement in the water stability and other related functional properties of thin (<50 µm) kafirin protein films was investigated. Thin conventional kafirin films and kafirinmicroparticle films were prepared by casting in acetic acid solution. Thin kafirin films cast from microparticles were more stable in water than conventional cast kafirin films.Treatment of kafirinmicroparticles with heat and transglutaminase resulted in slightly thicker films with reduced tensile strength. In contrast,glutaraldehyde treatment resulted in up to 43% increase in film tensile strength. The films prepared from microparticles treated with glutaraldehyde were quite stable in ambient temperature water, despite the loss of plasticizer.This was probably due to the formation of covalent cross-linking between free amino groups of the kafirin polypeptides and carbonyl groups of the aldehyde. Thus, such thin glutaraldehyde-treated kafirinmicroparticle films appear to have good potential for use as biomaterials in aqueous applications.

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Section: Resultsmentioning

confidence: 80%

Improvement in Water Stability and Other Related Functional Properties of Thin Cast Kafirin Protein Films

Anyango

Taylor

2011

J. Agric. Food Chem.

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“…In a similar but different experiment, Zhao, Tian, and Chen (2010) reported increased solubility, foaming capacity (FC), and ES of barley hordein at pH 3 to 7 compared to unmodified hordein. Flores, Cabra, Quirasco, Farres, and Galvez (2010) reported an increased emulsification activity index of corn gluten meal from 6.8 to 16.8 m 2 /g protein and ES from 0% to 90.6% oil retention for a 0.1 N HCl deamidation for 6 hr at 70°C. Most data on cereal protein deamidation showed the best improvements in functionality when the degree of deamidation was kept below 45% with a minimal (<3%) degree of hydrolysis (Cabra et al., 2007; Flores et al., 2010; Zhao et al., 2010).…”

Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning

confidence: 97%

“…Flores, Cabra, Quirasco, Farres, and Galvez (2010) reported an increased emulsification activity index of corn gluten meal from 6.8 to 16.8 m 2 /g protein and ES from 0% to 90.6% oil retention for a 0.1 N HCl deamidation for 6 hr at 70°C. Most data on cereal protein deamidation showed the best improvements in functionality when the degree of deamidation was kept below 45% with a minimal (<3%) degree of hydrolysis (Cabra et al., 2007; Flores et al., 2010; Zhao et al., 2010). However, an increase in solubility, EAI, ESI, and foamability but a decrease in FS were recorded for up to 72.1% degree of deamidation when soymilk residue protein was deamidated at 65 °C for 48 hr using 0.01 to 0.3 N HCl (Chan & Ma, 1999).…”

Section: Modification Of Plant Proteins By Various Processing Techniquesmentioning

confidence: 97%

Modification of plant proteins for improved functionality: A review

Akharume

Aluko

Adedeji

2021

Comp Rev Food Sci Food Safe

349

136

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The market trend towards plant‐based protein has seen a significant increase in the last decade. This trend has been projected to continue in the coming years because of the strong factors of sustainability and less environmental impact associated with the production of plant‐based protein compared to animal, aside from other beneficial health claims and changes in consumers' dietary lifestyles. In order to meet market demand, there is a need to have plant‐based protein ingredients that rival or have improved quality and functionality compared to the traditional animal protein ingredients they may replace. In this review article, we present a detailed and concise summary of the functionality challenges of some plant protein ingredients with associated physical, chemical, and biological processing techniques (traditional and emerging technologies) that have been attempted to enhance them. We cataloged the differences between several studies that seek to address the functionality challenges of selected plant‐based protein ingredients without overtly commenting on a general technique that addresses the functionality of all plant‐based protein ingredients. Additionally, we elucidated the chemistry behind some of these processing techniques and how they modify the protein structure for improved functionality. Although, many food industries are shifting away from chemical modification of proteins because of the demand for clean label product and the challenge of toxicity associated with scale‐up of this technique, so physical and biological techniques are widely being adopted to produce a functional ingredient such as texturized vegetable proteins, hydrolyzed vegetable protein, clean label protein concentrates, de‐flavored protein isolates, protein flour, and grits.

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“…Most previous researches have been done on chemical deamidation of proteins from wheat, corn, barley, and soy, but not from pulses. These previous data suggest that favorable functionality can achieve by controlled deamidation level < 45% from cereal proteins and 72% from soy proteins 42‐45 …”

Section: Modification Methods Of Pulse Protein Ingredientsmentioning

confidence: 86%

“…These previous data suggest that favorable functionality can achieve by controlled deamidation level < 45% from cereal proteins and 72% from soy proteins. [42][43][44][45] Glycosylation involves the attachment of carbohydrate moieties to the amino acid side chain lysine residues or the N-terminus of a protein. This reaction usually occurs during the Maillard reaction.…”

Section: Chemical Modificationmentioning

confidence: 99%

Pulse protein ingredient modification

Fernando

2021

J Sci Food Agric

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Increasing population and depletion of resources have paved the way to find sustainable and nutritious alternative protein sources. Pulses have been identified as a nutritious and inexpensive alternative source of protein that can meet this market demand. Pulses can be converted into protein concentrates and isolates through dry and wet separation techniques. Wet extraction results in relatively pure protein isolates but less sustainable due to higher energy requirements and high waste generation. Dry separation focuses on ingredient functionality rather than molecular level purity. These extracted pulse protein ingredients can be incorporated into different food systems to increase the nutritional value and to achieve the desired functionality. But many plant-based alternative proteins including pulses, face several formulation challenges especially in nutritional, sensory, and functional aspects. Native pulse protein ingredients can contain antinutrients, beany flavor, and undesirable functionality. Modification by biological (enzymatic, fermentation), chemical (acylation, deamidation, glycosylation, phosphorylation), and physical (cold plasma, extrusion, heat, high pressure, ultrasound) methods or a combination of these can improve pulse protein ingredients at the macro and micro level for their desired use. These modification processes will thermodynamically change the structural and conformational characteristics of proteins and expect to improve the quality.

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Emulsifying Properties of Chemically Deamidated Corn (Zea Mays) Gluten Meal

Cited by 14 publications

References 38 publications

Improvement in Water Stability and Other Related Functional Properties of Thin Cast Kafirin Protein Films

Improvement in Water Stability and Other Related Functional Properties of Thin Cast Kafirin Protein Films

Modification of plant proteins for improved functionality: A review

Pulse protein ingredient modification

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