Amaranth protein films prepared with high-pressure treated proteins

Condés, María Cristina; Añón, Marı́a Cristina; Mauri, Adriana Noemí

doi:10.1016/j.jfoodeng.2015.05.005

Cited by 47 publications

(29 citation statements)

References 26 publications

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“…The opacity value (2.35 nm mm −1 ) of the DPFF was a little high (Table ). Other authors reported opacity values ranging from 1.1 to 2.2 for films prepared using high‐pressure modified amaranth proteins (Condés et al ., ) and from 1.2 to 3.0 in amaranth proteins films, reinforced with amaranth starch granules and nanocrystals (Condés et al ., ).…”

Section: Resultsmentioning

confidence: 99%

Film preparation with high protein defatted peanut flour: characterisation and potential use as food packaging

Riveros

Martín

Aguirre

et al. 2017

Int J of Food Sci Tech

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Summary The purpose of this study was to prepare a defatted peanut flour‐based film (DPFF); to characterise their physicochemical, optical, barrier and mechanical properties; and to evaluate the defatted peanut flour package efficacy to preserve the chemical quality of sunflower oil during storage. The film presented high lightness values (L* = 86.83). The water vapour permeability was 5.44 × 10−11 g m−1 s−1 Pa−1. Tensile strength and percentage of elongation were 1.01 MPa and 84.01%, respectively. Sunflower oil samples packaged in defatted peanut flour packages (DPFP) were stored during 67 days at room temperature. Peroxide value and conjugated dienes increased less for sunflower oil conditioned in DPFP and high barrier plastic pouches (EVOH) during storage than sunflower oil conditioned in Petri dishes (C). The use of DPFP improved the chemical stability of sunflower oil during storage. The DPFF showed suitable film properties, and also, the capacity to be incorporated in food packaging applications.

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Section: Resultsmentioning

confidence: 99%

Film preparation with high protein defatted peanut flour: characterisation and potential use as food packaging

Riveros

Martín

Aguirre

et al. 2017

Int J of Food Sci Tech

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“…Whereas the proteins with lower T d are almost completely denatured after treatment at 200 MPa, those of higher thermal stability partially retain their native structures. Furthermore, the proteins with low and high T d that resist high‐pressure treatment have lower and higher thermal stability, respectively, than the untreated protein fractions (Condes and others ; Condes and others ).…”

Section: Denaturation and Aggregation Behaviormentioning

confidence: 99%

“…High‐pressure treatment of amaranth protein isolates affects the degree of dissociation or association of amaranth proteins obtained by alkaline isolation. High‐pressure treatment induces the formation of insoluble aggregates, triggers the dissociation of soluble aggregates, and increases surface hydrophobicity (Condes and others , ).…”

Section: Denaturation and Aggregation Behaviormentioning

confidence: 99%

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Janssen

Pauly

Rombouts

et al. 2016

Comp Rev Food Sci Food Safe

142

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There is currently much interest in the use of pseudocereals for developing nutritious food products. Amaranth, buckwheat, and quinoa are the 3 major pseudocereals in terms of world production. They contain high levels of starch, proteins, dietary fiber, minerals, vitamins, and other bioactives. Their proteins have well-balanced amino acid compositions, are more sustainable than those from animal sources, and can be consumed by patients suffering from celiac disease. While pseudocereal proteins mainly consist of albumins and globulins, the predominant cereal proteins are prolamins and glutelins. We here discuss the structural properties, denaturation and aggregation behaviors, and solubility, as well as the foaming, emulsifying, and gelling properties of amaranth, buckwheat, and quinoa proteins. In addition, the technological impact of incorporating amaranth, buckwheat, and quinoa in bread, pasta, noodles, and cookies and strategies to affect the functionality of pseudocereal flour proteins are discussed. Literature concerning pseudocereal proteins is often inconsistent and contradictory, particularly in the methods used to obtain globulins and glutelins. Also, most studies on protein denaturation and techno-functional properties have focused on isolates obtained by alkaline extraction and subsequent isoelectric precipitation at acidic pH, even if the outcome of such studies is not necessarily relevant for understanding the role of the native proteins in food processing. Finally, even though establishing in-depth structure-function relationships seems challenging, it would undoubtedly be of major help in the design of tailor-made pseudocereal foods.

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“…Electrostatic bonds are very labile, hydrophobic interactions are easily disrupted and oxidation of sulfhydryl groups is favoured through the application of high pressure processing (HPP) on proteins [43]. This is accompanied by an increase in surface hydrophobicity and formation of disulfide bridges known as protein denaturation leading to aggregation and eventual gelation [44][45][46]. In relatively dilute systems of amaranth protein isolate (5%, w/w), HPP at 200 MPa induced partially unfolding of the protein structure and generated some free sulfhydryl groups [7].…”

Section: Effect Of High Pressurementioning

confidence: 99%

“…The same pressure intensity increased the water-holding and oil-binding capacity of peanut protein isolate [47]. Extensive conformational changes were recorded upon high pressure application (400 MPa) on amaranth solutions resulting in protein aggregation and the formation of biofilms [45]. Seed and legume protein pressurisation up to 600 MPa showed an excessive formation of high molecular weight and large particle-size protein aggregates, yielding reduced protein solubility in aqueous solutions.…”

Section: Effect Of High Pressurementioning

confidence: 99%

Molecular Functionality of Plant Proteins from Low- to High-Solid Systems with Ligand and Co-Solute

Paramita¹,

Panyoyai

Kasapis

2020

IJMS

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In the food industry, proteins are regarded as multifunctional systems whose bioactive hetero-polymeric properties are affected by physicochemical interactions with the surrounding components in formulations. Due to their nutritional value, plant proteins are increasingly considered by the new product developer to provide three-dimensional assemblies of required structure, texture, solubility and interfacial/bulk stability with physical, chemical or enzymatic treatment. This molecular flexibility allows them to form systems for the preservation of fresh food, retention of good nutrition and interaction with a range of microconstituents. While, animal- and milk-based proteins have been widely discussed in the literature, the role of plant proteins in the development of functional foods with enhanced nutritional profile and targeted physiological effects can be further explored. This review aims to look into the molecular functionality of plant proteins in relation to the transport of bioactive ingredients and interaction with other ligands and proteins. In doing so, it will consider preparations from low- to high-solids and the effect of structural transformation via gelation, phase separation and vitrification on protein functionality as a delivery vehicle or heterologous complex. Applications for the design of novel functional foods and nutraceuticals will also be discussed.

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Amaranth protein films prepared with high-pressure treated proteins

Cited by 47 publications

References 26 publications

Film preparation with high protein defatted peanut flour: characterisation and potential use as food packaging

Film preparation with high protein defatted peanut flour: characterisation and potential use as food packaging

Proteins of Amaranth (Amaranthus spp.), Buckwheat (Fagopyrum spp.), and Quinoa (Chenopodium spp.): A Food Science and Technology Perspective

Molecular Functionality of Plant Proteins from Low- to High-Solid Systems with Ligand and Co-Solute

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