The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin

Johnston, Stuart P.; Nickerson, Michael T.; Low, Nicholas H.

doi:10.1007/s13197-014-1523-3

Cited by 82 publications

(55 citation statements)

References 47 publications

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“…The presence of fibre in the protein extracts could be undesirable at large‐scale production, due to it decreases the protein purity; for this reason, additional processing steps should be performed to increase its purity. In a previous study (de la Rosa‐Millán et al ., ), we observe a tightly bounded protein fraction in the pulses bagasses (obtained from the same process) which shows the difficulties of total protein removal without solvents (Johnston et al ., ). Nevertheless, we hypothesised that the fibre fraction promoted molecular interactions with water and oil within the food system and has repercussions on their performance as food ingredient, thus having a direct impact on the economic output of the product (Hoover & Zhou, ; Ma et al ., ).…”

Section: Resultsmentioning

confidence: 97%

“…One of the main uses of protein ingredients in food formulations is to enhance or promote specific functionalities, besides to improve their nutritional characteristics (Ma et al, 2011;Qayyum et al, 2012). From the applications for proteins, this related to water and oil interaction, as well as their ability to form gel structures and foams is of interest, as some proteins obtained from plant sources are used to replace hydrocolloids in food formulations with the aim to increase its nutritional value and at the same time, to maintain or improve some of their textural and functional attributes (Johnston et al, 2015). Our protein extracts showed significant differences in WSI from 13.18% to 27.97% for lentil and chickpea, respectively (Table 3), while broad bean showed the highest WAI when compared with other pulse extracts (4.22% to ≤3.51%, respectively).…”

Section: Functional Characteristics Of Pulse Protein Extractsmentioning

confidence: 99%

“…This decrease can be related to a molecular rearrangement on protein tertiary structure, promoting a less stable structure (Herrero et al, 2012). Previous studies have shown that denatured proteins present lower water solubility, as well as less oil retention, compared with native molecules (Johnston et al, 2015). The FC of proteins is related to their ability to incorporate air into the cells or bubbles that are formed in a protein solution, and it is often related to the net electrochemical charge of terminal and side amino acids in the protein molecular structures (Sai-Ut et al, 2009;Ma et al, 2011).…”

Section: Functional Characteristics Of Pulse Protein Extractsmentioning

confidence: 99%

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Physicochemical, functional andATR‐FTIR molecular analysis of protein extracts derived from starchy pulses

Millán

Orona-Padilla

Flores-Moreno

et al. 2018

Int J of Food Sci Tech

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Summary An alkaline solubilisation and isoelectric point precipitation process were used to isolate proteins from broad bean, chickpea, lentil and white bean. The physicochemical, water solubility and foaming properties as well as their protein digestion characteristics of whole flours and its protein extracts were correlated with their molecular characteristics, analysed by attenuated total reflectance Fourier transform infrared spectroscopy (ATR‐FTIR). The processing of pulses resulted in protein recoveries ≥50.12% and yields up to 30.26% for broad bean. The purity of the protein was from 68.27% to 86.58% for chickpea and broad bean, with in vitro digestion values ≥80.59%. The protein extracts showed up to 0.85 mg g−1 of phenolic compounds (gallic acid eq./100 g). The ATR‐FTIR analysis of the extracts showed different proportions of α‐helix and β‐sheet secondary structures of the amide II group. The analysis of the amide III group reflected inter‐ and intramolecular associations that could have influenced their emulsion and foam characteristics.

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Section: Resultsmentioning

confidence: 97%

Section: Functional Characteristics Of Pulse Protein Extractsmentioning

confidence: 99%

Section: Functional Characteristics Of Pulse Protein Extractsmentioning

confidence: 99%

See 1 more Smart Citation

Physicochemical, functional andATR‐FTIR molecular analysis of protein extracts derived from starchy pulses

Millán

Orona-Padilla

Flores-Moreno

et al. 2018

Int J of Food Sci Tech

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“…Many studies have been conducted on plant proteins, in order to overcome structural drawbacks and achieve properties as the animal counterparts in the design of emulsifiers and stabilisers [5]. The results indicate that the bio-and techno-functional properties of plant proteins can be improved through processing, including by heating, crosslinking with natural materials (e.g., genipin) [6] and binding with other biomaterials, like phenolic compounds. Specific treatments have been employed, including ultra-high temperature (UHT), high pressure and ultrasonication, to manipulate the structural behaviour and interactions with bioactive compounds/drugs leading to comparable functionality with corresponding dairy protein and Bovine Serum Albumin (BSA) systems [7][8][9][10].…”

Section: Introductionmentioning

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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“…Recently, there has been a major need to identify surface-active plant protein sources that can be used in food formulations for reasons of sustainability and in satisfying dietary requirements [12]. While soy is the most established source of plant protein, proteins from several legumes, such as those from lentils, are growing in interest [13]. The proteins from pulses have been shown to contain amphiphilic proteins that form relatively thick interfacial layers around oil droplets, thereby enhancing emulsion formation and stability [14].…”

mentioning

confidence: 99%

Thermal and Mineral Sensitivity of Oil-in-Water Emulsions Stabilised using Lentil Proteins

Alonso-Miravalles

Zannini

Bez

et al. 2020

Foods

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Oil-in-water emulsion systems formulated with plant proteins are of increasing interest to food researchers and industry due to benefits associated with cost-effectiveness, sustainability and animal well-being. The aim of this study was to understand how the stability of complex model emulsions formulated using lentil proteins are influenced by calcium fortification (0 to 10 mM CaCl 2 ) and thermal processing (95 or 140 • C). A valve homogeniser, operating at first and second stage pressures of 15 and 3 MPa, was used to prepare emulsions. On heating at 140 • C, the heat coagulation time (pH 6.8) for the emulsions was successively reduced from 4.80 to 0.40 min with increasing CaCl 2 concentration from 0 to 10 mM, respectively. Correspondingly, the sample with the highest CaCl 2 addition level developed the highest viscosity during heating (95 • C × 30 s), reaching a final value of 163 mPa·s. This was attributed to calcium-mediated interactions of lentil proteins, as confirmed by the increase in the mean particle diameter (D[4,3]) to 36.5 µm for the sample with 6 mM CaCl 2 , compared to the unheated and heated control with D[4,3] values of 0.75 and 0.68 µm, respectively. This study demonstrated that the combination of calcium and heat promoted the aggregation of lentil proteins in concentrated emulsions.Foods 2020, 9, 453 2 of 14 coefficients of 7S and 11S, respectively. In contrast, the proteins in the albumin fraction have lower molecular weights (5-80 kDa) and are considered compact globular proteins [10].Oil-in-water emulsion systems formulated with plant proteins are of particular interest to the food industry as the market for plant-based milks, yogurts, spreads, cheeses and infant formula is growing [11]. Recently, there has been a major need to identify surface-active plant protein sources that can be used in food formulations for reasons of sustainability and in satisfying dietary requirements [12]. While soy is the most established source of plant protein, proteins from several legumes, such as those from lentils, are growing in interest [13]. The proteins from pulses have been shown to contain amphiphilic proteins that form relatively thick interfacial layers around oil droplets, thereby enhancing emulsion formation and stability [14]. In this regard, lentil proteins were shown to be very effective natural emulsifiers for oil-in-water emulsion systems, being very stable to environmental and compositional stresses such as heat, pH and added salts [15]. These authors associated the high stability of lentil proteins with their surface hydrophobicity and/or formation of thick viscoelastic films around oil droplets, as also suggested by Can Karaca et al. (2015) [14]. In another recent study by Gumus et al. (2017b) [16] it was demonstrated that lentil proteins could be successfully applied to formulate oil-in-water emulsions, with such systems being used for bioactive lipid delivery, with similar behaviour to whey protein under simulated in vitro gastrointestinal digestion systems. Moreover, Avramenko et al. ...

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The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin

Cited by 82 publications

References 47 publications

Physicochemical, functional andATR‐FTIR molecular analysis of protein extracts derived from starchy pulses

Physicochemical, functional andATR‐FTIR molecular analysis of protein extracts derived from starchy pulses

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

Thermal and Mineral Sensitivity of Oil-in-Water Emulsions Stabilised using Lentil Proteins

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