Investigation on solubility, interfacial and emulsifying properties of pumpkin (Cucurbita pepo) seed protein isolate

Bučko, Sandra; Katona, Jaroslav; Popović, Ljiljana; Vaštag, Žužana; Petrović, Ljiljana; Vučinić–Vasić, Milica

doi:10.1016/j.lwt.2015.06.054

Cited by 60 publications

(48 citation statements)

References 29 publications

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“…Unlike β-lactoglobulin, β-casein, and phaseolin, for which it was reported that cross-linking by Tg resulted in products resistant to both pepsin and pancreatic enzymes [11,14,24] polymerization of cucurbitin by Tg had no influence on its digestion process. 2), Tg-C (5); cucurbitin digested by pepsin C1 (3), pepsin, α-chymotrypsin and trypsin C2 (4); enzymatically cross-linked cucurbitin digested by pepsin Tg-C1 (6), pepsin, α-chymotrypsin and trypsin Tg-C2 (7) by pepsin, two bands were still visible, but with reduced intensity (lanes 3 and 6). In the final digests, after treatment by trypsin and α-chymotrypsin, no visible bands were obtained on the gel (lanes 4 and 7).This is in accordance with observations of other researchers, where the products of subsequent hydrolysis of peptide/proteins mixtures by pepsin and pancreatic enzymes were not detected by SDS-PAGE [25,26].…”

Section: Resultsmentioning

confidence: 99%

“…Generally, food proteins are of great importance, not only in contributing to the improvement of the functional roles in food preparation, processing, storage and consumption, but also in increasing the quality of sensory and biological properties of food products (e.g. anti-oxidant, angiotensinconverting-I enzyme (ACE)-inhibition, opioid activity) [7]. Rarely, native proteins possess all the desirable properties for application in different food systems.…”

Section: Introductionmentioning

confidence: 99%

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Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

Popović

Stolić

Čakarević

et al. 2017

J Americ Oil Chem Soc

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The objective of this study was to show that biologically active hydrolysates can be obtained by simulated human gastrointestinal digestion (HGD) of transglutaminase cross‐linked pumpkin oil cake protein (Tg‐C) which was previously reported as a potential functional food additive. A two‐stage in vitro digestion model system (by pepsin and α chymotrypsin and trypsin, simultaneously) was used to simulate the process of HGD on native and Tg‐C major storage pumpkin oil seed/cake protein, cucurbitin (C). The biologically active potential of the digests was evaluated, measuring the angiotensin‐converting‐I enzyme (ACE) inhibitory and anti‐oxidant capacity. The ACE inhibitory activity was determined in both final digests, with IC50 = 0.30 ± 0.04 mg/ml for C and IC50 = 0.28 ± 0.01 for Tg‐C. The anti‐oxidant potency of the examined proteins was enhanced by the digestion process. The 2,2‐diphenyl‐1‐picrylhydrazyl and 2,2′‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulphonic acid) radical cation activities and reducing power testing showed that all the hydrolysates act as a radical quencher and reducing agents. Overall, the results showed that the cross‐linking by Tg did not influence the digestion process, as well as having no effect on the biological activity of the hydrolysates. These also indicate that Tg‐C, if used as functional food additive, after food consumption can be digested and become a source of peptides exerting positive effects on human health.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

Popović

Stolić

Čakarević

et al. 2017

J Americ Oil Chem Soc

Self Cite

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“…For instance, caseins, which have a random spiral conformation, tend to form an interweaved layer; whereas whey proteins that are globular in shape usually form aggre gates at the interface of the colloidal system [64]. Further, bovine serum albumin, whey pro tein and proteins isolated from plant sources such as soybean, pumpkin seed, quinoa and peas have been used as emulsifiers in many encapsulation systems, including W/O and W1/O/ W2 double emulsions [65][66][67]. Proteins could also be combined with other emulsifiers to sta bilize emulsions.…”

Section: Emulsificationmentioning

confidence: 99%

Vegetable Proteins: Non-sensitizing Encapsulation Agents for Bioactive Compounds

Quiroz¹,

Durán²,

Ciro-Gómez³

et al. 2017

Allergen

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Plant-derived proteins are remarkable macromolecules of scientific interest because they represent an alternative to the animal-derived proteins and petroleum-derived polymers. Many food proteins especially those derived from animal sources could act as antigens in humans. For instance, milk proteins extracted from cows may cause food intolerance during infancy. Further, soybean, peanuts, tree nuts, fish, crustacean shellfish and egg proteins may act as antigens in 90% of children. Since the GI tract is permeable to intact antigens the oral intake of these proteins may generate gastrointestinal (50-80%), cutane ous (20-40%) and respiratory symptoms (4-25%). Most of these allergens are water-soluble glycoproteins that are resistant to acids and enzymes. Usually, these proteins have a small molecular weight (10,000-60,000 kDa), water solubility, glycosylation residues, and a rela tive resistance to heat and digestion. Allergenicity is less frequent in vegetable proteins due to their less flexible and non-compact structure. Allergenicity is also related to the resistance to proteolysis, post-translational glycosylation, presence of epitopes, and enzy matic proteolysis. Moreover, proteins serve as a coating material if structural modifica tions in the protein, either by physical, chemical or enzymatic mechanisms are conducted. As a result, their allergenicity is reduced, and their functional properties are enhanced.

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“…The major protein fraction in pumpkin seeds is represented by the 12S globulin, called cucurbitin, followed by the 18S globulin. These two protein fractions and other smaller amounts of albumins represent 59% of the total protein content in pumpkin seeds [86]. The increased production of pumpkin seed oils results in large amounts of by-products, where protein contents can reach up to 60-65 wt%.…”

Section: Agro Seeds As Protein Sourcesmentioning

confidence: 99%

“…But this residue is only currently used as livestock feed [87]. Some authors have reported the functional properties of pumpkin seed protein isolates (PSPI), such as solubility, interfacial and emulsifying properties, as function of pH, ionic strength and PSPI concentration [86].…”

Section: Agro Seeds As Protein Sourcesmentioning

confidence: 99%

Valorization of Agricultural Wastes for the Production of Protein-Based Biopolymers

Burgos¹,

Valdés²,

Jiménez³

2016

j renew mater

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In this study we provide an overview of the latest developments on the extraction, production, modifi cation and applications of fruit residues and by-products in the formation of protein-based biopolymers, in particular for the formulation of edible fi lms. Our aim was mainly to demonstrate the highly transdisciplinary character of these topics by giving an overview of the main developments and research topics in the chemistry and engineering aspects of protein-based biopolymers. These innovative raw materials have been evaluated for the production of biomaterials to be used in some key sectors, such as food packaging.

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Investigation on solubility, interfacial and emulsifying properties of pumpkin (Cucurbita pepo) seed protein isolate

Cited by 60 publications

References 29 publications

Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross‐linking by Transglutaminase

Vegetable Proteins: Non-sensitizing Encapsulation Agents for Bioactive Compounds

Valorization of Agricultural Wastes for the Production of Protein-Based Biopolymers

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