Functional properties of Grass pea protein concentrates prepared using various precipitation methods

Zeidanloo, Milad Hayati; Ghavidel, Reihaneh Ahmadzadeh; Davoodi, Mehdi; Arianfar, Akram

doi:10.1007/s13197-019-03930-3

Cited by 24 publications

(11 citation statements)

References 34 publications

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“…The surface charge of other pea protein isolates extracted by different methods was reported to be ~21 mV at pH 7.0, which is low when compared to other legumes ( 17 ). Similarly, Hayati Zeidanloo et al ( 45 ) showed that variations exist in surface charge of pea protein prepared by different methods (between −21.73 and 24.96 mV at pH 7.0). On the contrary, another study reported that the surface charge of lab prepared field protein isolate was −44.2 mV and higher than that of kidney bean (40.0 mV) and amaranth protein isolates (37.3 mV) ( 46 ).…”

Section: Resultsmentioning

confidence: 89%

Physicochemical and Functional Properties of Membrane-Fractionated Heat-Induced Pea Protein Aggregates

Asen

Aluko

2022

Front. Nutr.

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This study was carried out to investigate the effect of heat pre-treatment of pea proteins at different pH values on the formation of functional protein aggregates. A 10% (w/v) aqueous mixture of pea protein concentrate (PPC) was adjusted to pH 3.0, 5.0, 7.0, or 9.0 followed by heating at 100°C for 30 min, cooled and centrifuged. The supernatant was sequentially passed through 30 and 50 kDa molecular weight cut-off membranes to collect the <30, 30–50, and >50 kDa fractions. The >50 kDa fractions from pH 3.0 (FT3), 5.0 (FT5), 7.0 (FT7), and 9.0 (FT9) treatments had >60% protein content in contrast to the ≤20% for the <30 and 30–50 kDa fractions. Therefore, the >50 kDa fractions were collected and then compared to the untreated PPC for some physicochemical and functional properties. Protein aggregation was confirmed as the denaturation temperature for FT3 (124.30°C), FT5 (190.66oC), FT7 (206.33oC) and FT9 (203.17oC) was significantly (p < 0.05) greater than that of PPC (74.45oC). Scanning electron microscopy showed that FT5 had a compact structure like PPC while FT3, FT7, and FT9 contained a more continuous network. In comparison to PPC, the >50 kDa fractions showed improved solubility (>60%), oil holding capacity (~100%), protein content (~7%), foam capacity (>10%), foam stability (>7%), water holding capacity (>16%) and surface hydrophobicity (~50%). Least gelation concentration of PPC (18%), FT3 (25%), FT5 (22%), FT7 (22%), and FT9 (25%) was improved to 16, 18, 20, 16, and 18%, respectively, after addition of NaCl.

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Section: Resultsmentioning

confidence: 89%

Physicochemical and Functional Properties of Membrane-Fractionated Heat-Induced Pea Protein Aggregates

Asen

Aluko

2022

Front. Nutr.

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“…To the best of our knowledge, very limited work has been done on the use of solubilization in dilute NaCl, followed by UF, to produce PPI. While ultrafiltration has been used following an alkaline or acidic solubilization step, or as further purification after isoelectric precipitation [ 11 , 16 ], it is not well characterized as a protein concentration step following salt solubilization. Tian [ 19 ] and Taherian [ 20 ] reported the use of ultrafiltration post salt solubilization of pea protein, however, 20 and 50 kDa MWCO membrane were used, respectively, which could potentially lead to loss of a considerable amount of relatively small molecular weight proteins.…”

Section: Resultsmentioning

confidence: 99%

“…Alternative concentration techniques such as membrane filtration may replace the “salting out” step, which could make this extraction method more feasible. There is limited research on the optimization of salt extraction conditions, including salt concentration and type of membrane filtration, for optimal pea protein purity and yield [ 10 , 16 , 17 , 18 , 19 ]. A few of these studies were based on benchtop trials following micellar precipitation and/or using dialysis membranes [ 11 , 17 ], while only one study was based on pilot plant trials using ultrafiltration/diafiltration membranes [ 18 , 19 , 20 ].…”

Section: Introductionmentioning

confidence: 99%

Structure-Function Guided Extraction and Scale-Up of Pea Protein Isolate Production

Hansen

Ismail

2022

Foods

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The lack of adequate guidance and control of the extraction conditions as well as the gap between bench- and industrial-scale production, contributes to the poor functionality of commercial pea protein isolate (cPPI). Therefore, pea protein extraction conditions were evaluated and scaled up to maximize protein purity and yield, while maintaining structural integrity, following mild alkaline solubilization with isoelectric precipitation and salt solubilization coupled with membrane filtration. Both extraction methods resulted in high protein yield (>64%) and purity (>87%). Structure-function characterization illustrated the preserved structural integrity of PPI samples and their superior solubility, gelation, and emulsification properties compared to cPPI. Results confirmed, for the first time, that double solubilization at mild pH (7.5) can replace single solubilization at high alkalinity and achieve a similar yield while preserving structural integrity. Additionally, this study demonstrated, the scalability of the benchtop salt extraction coupled with ultrafiltration/diafiltration. Scaling up the production eliminated some structural and functional differences between the salt-extracted PPI and pH-extracted PPI. Scaling-up under mild and controlled conditions resulted in partial denaturation and a low degree of polymerization, coupled with the superior functionality of the produced isolates compared to cPPI. Results of this work can be used as a benchmark to guide the industrial production of functional pea protein ingredients.

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“…It has been reported that proteins obtained from leaf sources via various preparation methods have displayed a similar trend of having a higher protein solubility on either side of the isoelectric point [33,42,44]. Protein solubility of grass pea protein concentrate also reportedly decreased with a decrease in pH until pH 4-5 followed by an increase with an increase in pH [4]. This is also observed in the solubility curve of the GPC, which is due to proteins acquiring net positive or negative charges when in acidic and basic environments.…”

Section: Effect Of Ph On Protein Solubilitymentioning

confidence: 90%

“…However, extraction processes greatly influence the solubility, denaturation state and composition of protein isolates. This in turn influence their functional properties such as gelation, water binding, emulsifying and foaming capacities, which are relevant for food applications [4]. Moreover, the plant species from which the protein is extracted play a significant part in affecting results [5].…”

Section: Introductionmentioning

confidence: 99%

Physico-Chemical Characteristics and In Vitro Gastro-Small Intestinal Digestion of New Zealand Ryegrass Proteins

Kaur

Lamsar

López

et al. 2021

Foods

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Being widely abundant, grass proteins could be a novel source of plant proteins for human foods. In this study, ryegrass proteins extracted using two different approaches-chemical and enzymatic extraction, were characterised for their physico-chemical and in vitro digestion properties. A New Zealand perennial ryegrass cultivar Trojan was chosen based on its higher protein and lower dry matter contents. Grass protein concentrate (GPC) with protein contents of approximately 55 and 44% were prepared using the chemical and enzymatic approach, respectively. The thermal denaturation temperature of the GPC extracted via acid precipitation and enzymatic treatment was found to be 68.0 ± 0.05 °C and 66.15 ± 0.03 °C, respectively, showing significant differences in protein’s thermal profile according to the method of extraction. The solubility of the GPC was highly variable, depending on the temperature, pH and salt concentration of the dispersion. The solubility of the GPC extracted via enzymatic extraction was significantly lower than the proteins extracted via the chemical method. Digestion of raw GPC was also studied via a gastro-small intestinal in vitro digestion model and was found to be significantly lower, in terms of free amino N release, for the GPC prepared through acid precipitation. These results suggest that the physico-chemical and digestion characteristics of grass proteins are affected by the extraction method employed to extract the proteins. This implies that selection of an appropriate extraction method is of utmost importance for achieving optimum protein functionality during its use for food applications.

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Functional properties of Grass pea protein concentrates prepared using various precipitation methods

Cited by 24 publications

References 34 publications

Physicochemical and Functional Properties of Membrane-Fractionated Heat-Induced Pea Protein Aggregates

Physicochemical and Functional Properties of Membrane-Fractionated Heat-Induced Pea Protein Aggregates

Structure-Function Guided Extraction and Scale-Up of Pea Protein Isolate Production

Physico-Chemical Characteristics and In Vitro Gastro-Small Intestinal Digestion of New Zealand Ryegrass Proteins

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