Pumpkin (Cucurbita maxima) Seed Proteins: Sequential Extraction Processing and Fraction Characterization

Rezig, Leila; Chibani, Farhat; Chouaibi, Moncef; Dalgalarrondo, Michèle; Hessini, Kamel; Guéguen, Jacques; Hamdi, Salem

doi:10.1021/jf402323u

Cited by 85 publications

(47 citation statements)

References 24 publications

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“…Moreover, it is difficult to compare results, even within the seeds of one species, if the authors use different raw materials, extraction methods, and electrophoresis conditions. We obtained SDS‐PAGE profiles similar to those that have been described previously for coconut meal, 19,20 flaxseed meal, 21 hemp seed meal and hemp protein isolate, 22,23 milk thistle seed protein isolate, 24 black cumin flour obtained from Nigella damascena , 25 pumpkin seed protein extract, 11,26 rapeseed meal, 27–29 sesame protein isolate and seed flour, 30,31 and finally, from sunflower flour and protein concentrate 32,33 …”

Section: Resultssupporting

confidence: 58%

Proteomic analysis of oilseed cake: a comparative study of species‐specific proteins and peptides extracted from ten seed species

et al. 2020

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Background In recent years there has been a visible trend among consumers to move away from consuming meat in favor of plant products. Meat producers have therefore been trying to meet the expectations of consumers by introducing new products to the food market with a greater proportion of plant ingredients. Meat products are enriched not only by the addition of vegetable oils but also by ground or whole oilseeds or their preparation. In this study, we present in‐solution tryptic digestion and an ultra‐performance liquid chromatography coupled to quadrupole time‐of‐flight mass spectrometry (UHPLC‐Q‐TOF‐MS/MS)‐based proteomics approach to investigate specific proteins and peptides of ten oilseed cakes, by‐products of cold pressing oil from coconut, evening primrose, hemp, flax, milk thistle, nigella, pumpkin, rapeseed, sesame, and sunflower seeds, for authentication purposes. Results We identified a total of 229 unique oilseed proteins. The number of specific proteins varied depending on the sample, from 4 to 48 in evening primrose and sesame. Moreover, we identified approximately 440 oilseed unique peptides in the cakes of all the analyzed oilseeds; the largest amounts were found in sesame (107 peptides), sunflower (100), pumpkin, hemp (42), rapeseed (36), and flax cake (35 peptides). Conclusions We provide novel information on unique / species‐specific peptide markers that will extend the scope of testing the authenticity of a wide range of foods. The results of this peptide discovery experiment may further contribute to the development of targeted methods for the detection and quantification of oilseed proteins in processed foods, and thus to the improvement of food quality. © 2020 Society of Chemical Industry

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Section: Resultssupporting

confidence: 58%

Proteomic analysis of oilseed cake: a comparative study of species‐specific proteins and peptides extracted from ten seed species

et al. 2020

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“…Cucurbitin is a hexameric globular protein whose subunits weigh 54 kDa each. In turn, each subunit consists of an acidic and a basic subunit which are disulfide-bonded and weigh 33 kDa and 22 kDa, respectively [ 21 ]. Peričin et al [ 9 ] describe the standard procedure of cucurbitin extraction.…”

Section: Generation Of Cucurbitaceae Seed Protein Hydrolysatesmentioning

confidence: 99%

Cucurbitaceae Seed Protein Hydrolysates as a Potential Source of Bioactive Peptides with Functional Properties

Ozuna

León-Galván

2017

BioMed Research International

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Seeds from Cucurbitaceae plants (squashes, pumpkins, melons, etc.) have been used both as protein-rich food ingredients and nutraceutical agents by many indigenous cultures for millennia. However, relatively little is known about the bioactive components (e.g., peptides) of the Cucurbitaceae seed proteins (CSP) and their specific effects on human health. Therefore, this paper aims to provide a comprehensive review of latest research on bioactive and functional properties of CSP isolates and hydrolysates. Enzymatic hydrolysis can introduce a series of changes to the CSP structure and improve its bioactive and functional properties, including the enhanced protein solubility over a wide range of pH values. Small-sized peptides in CSP hydrolysates seem to enhance their bioactive properties but adversely affect their functional properties. Therefore, medium degrees of hydrolysis seem to benefit the overall improvement of bioactive and functional properties of CSP hydrolysates. Among the reported bioactive properties of CSP isolates and hydrolysates, their antioxidant, antihypertensive, and antihyperglycaemic activities stand out. Therefore, they could potentially substitute synthetic antioxidants and drugs which might have adverse secondary effects on human health. CSP isolates and hydrolysates could also be implemented as functional food ingredients, thanks to their favorable amino acid composition and good emulsifying and foaming properties.

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“…14 The solubility of pumpkin seed proteins was reported to be very low (< 20 %) at pH < 5. 15 One of the most efficient means of increasing protein solubility as well as improving the functional properties of oilseed proteins is to subject them to enzymatic hydrolysis. 2 Functional properties of particular interest include improved solubility, particularly at pH near the isoelectric point (pI), enhanced emulsifying properties, as well as enriched biological activities.…”

Section: Introductionmentioning

confidence: 99%

Functional properties of pumpkin (Cucurbita pepo) seed protein isolate and hydrolysate

et al. 2016

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Pumpkin seed protein isolate (PSPI) was enzymatically hydrolysed by pepsin to obtain pumpkin seed protein hydrolysate, PSPH. Investigation of the solubility, interfacial and emulsifying properties of both PSPI and PSPH was conducted under different conditions of pH (3-8) and ionic strength (0-1 mol dm-3 NaCl). PSPI had the lowest solubility, i.e., isoelectric point (pI) at pH 5. PSPH had higher solubility than PSPI over the whole range of tested pH and ionic strength values. The decreases in the surface and interfacial tension evidenced that both PSPI and PSPH adsorb at the air/protein solution and oil/ /protein interfaces of the solution. Emulsions (20 % oil in water) stabilized by 10 g dm-3 PSPI or PSPH solution were prepared at pH 3, 5 and 8 and ionic strength of 0 and 0.5 mol dm-3 NaCl. PSPH stabilized emulsions from coalescence at all tested pH and ionic strength values. PSPI was able to stabilize emulsions at pH 3 and 0 mol dm-3 NaCl, and at pH 8 regardless of ionic strength, while emulsions at pH 5 and both 0 and 0.5 mol dm-3 NaCl and at pH 3 when the ionic strength was increased separated into an oil and a serum layer immediately after preparation. All emulsions were susceptible to creaming instability.

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Pumpkin (Cucurbita maxima) Seed Proteins: Sequential Extraction Processing and Fraction Characterization

Cited by 85 publications

References 24 publications

Proteomic analysis of oilseed cake: a comparative study of species‐specific proteins and peptides extracted from ten seed species

Proteomic analysis of oilseed cake: a comparative study of species‐specific proteins and peptides extracted from ten seed species

Cucurbitaceae Seed Protein Hydrolysates as a Potential Source of Bioactive Peptides with Functional Properties

Functional properties of pumpkin (Cucurbita pepo) seed protein isolate and hydrolysate

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