Physicochemical properties of Grass pea (Lathyrus sativus L.) protein nanoparticles fabricated by cold atmospheric-pressure plasma

Mehr, Hamed Mahdavian; Koocheki, Arash

doi:10.1016/j.foodhyd.2020.106328

Cited by 31 publications

(14 citation statements)

References 126 publications

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“…On the other hand, the PPI had the maximum fluorescence intensity (λ max ) at 338 nm, which was in agreement with the previous study . Furthermore, λ max shifted from 338 to 337 nm, suggesting that a hypochromatic shift occurred, which proved a decrease in the polarity of the Trp residue microenvironment . Therefore, hydrophobic interactions might be an important driving force in the formation of PPINs.…”

Section: Resultssupporting

confidence: 84%

“…With the increase of K 2 S 2 O 5 concentration, the increase in peak intensity at 1450 and 1396 cm –1 was due to the bending of the −CH 2 and −CH 3 groups belonging to the aliphatic side chain of the protein, which might be due to the enhanced hydrophobic interaction of the polypeptide chain . These phenomena could be further confirmed by the increase of intensity in the spectra at 2930 and 2962 cm –1 , which corresponded to the C–H stretching vibrations of −CH 2 or −CH 3 groups .…”

Section: Resultsmentioning

confidence: 65%

“…44,45 With the increase of K 2 S 2 O 5 concentration, the increase in peak intensity at 1450 and 1396 cm −1 was due to the bending of the −CH 2 and −CH 3 groups belonging to the aliphatic side chain of the protein, which might be due to the enhanced hydrophobic interaction of the polypeptide chain. 17 These phenomena could be further confirmed by the increase of intensity in the spectra at 2930 and 2962 cm −1 , which corresponded to the C−H stretching vibrations of −CH 2 or −CH 3 groups. 46 The results demonstrated that higher concentrations of K 2 S 2 O 5 might break more disulfide bonds, thus exposing more hydrophobic sites and ultimately resulting in the intense hydrophobic interactions between the polypeptide chains.…”

Section: ■ Results and Discussionmentioning

confidence: 91%

“…Furthermore, PPI has a good balance of amino acids, which has more lysine that can make up for the deficiency of lysine in cereal protein . Pea protein isolate nanoparticles have been successfully fabricated by cold atmospheric pressure plasma or induction of calcium. , However, it is necessary to find an uncomplicated and effective way to fabricate nanoparticles, which can be better applied to the food industry.…”

Section: Introductionmentioning

confidence: 99%

“…16 Pea protein isolate nanoparticles have been successfully fabricated by cold atmospheric pressure plasma or induction of calcium. 17,18 However, it is necessary to find an uncomplicated and effective way to fabricate nanoparticles, which can be better applied to the food industry.…”

Section: ■ Introductionmentioning

confidence: 99%

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Self-Assembled Pea Protein Isolate Nanoparticles with Various Sizes: Explore the Formation Mechanism

Xie

Liu

et al. 2021

J. Agric. Food Chem.

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Pea protein isolate nanoparticles (PPINs) were successfully prepared by potassium metabisulfite (K 2 S 2 O 5 ). The disulfide bonds were disrupted by K 2 S 2 O 5 , and then the PPINs were formed through self-assembly. The average diameter of PPINs increased from 124.7 to 297.5 nm as the concentration of K 2 S 2 O 5 was increased from 2 to 8 mM, and the PPINs showed higher ζpotentials (−32.2 to −35.8 mV) and unimodal distribution. The content of free sulfhydryl groups first increased and then decreased with the fracture and reformation of disulfide bonds. Subsequently, the increase of the β-sheet, which has considerable hydrophobicity, promoted the formation of PPINs. The formation mechanism of PPINs was explored by dissociation tests: hydrophobic interactions maintained the basic skeleton of PPINs, disulfide bonds stabilized the internal structure, and hydrogen bonds existed on the exterior of the particles. This study provided a simple and economical method to fabricate nanoparticles.

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 65%

Section: ■ Results and Discussionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Self-Assembled Pea Protein Isolate Nanoparticles with Various Sizes: Explore the Formation Mechanism

Xie

Liu

et al. 2021

J. Agric. Food Chem.

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On treatment options to improve the functionality of pea protein

Mathew,

Kim,

Wang

et al. 2023

J Americ Oil Chem Soc

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Pea proteins have garnered attention as a viable alternative to animal proteins, offering health, and sustainability benefits. However, their functional limitations, such as poor solubility, hinder their application in plant‐based food products. This review details the specific physical, chemical, and biological methods employed to enhance pea protein functionality. Chemical methods have been the most effective, particularly in improving solubility, emulsification, and foaming properties, which are essential for food applications like dairy alternatives and meat analogues. Biological methods significantly enhance water and oil retention, contributing to better food texture. Physical methods, including ultrasound and heat treatment, also show promise but require careful application to avoid protein denaturation. While chemical methods are efficacious, they raise concerns about cost‐effectiveness and environmental impact. The review identifies combined treatment approaches as a fertile area for future research, suggesting that a multi‐faceted strategy may provide comprehensive improvements to pea protein functionality.

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Recent advances in legume protein‐based colloidal systems

Tarahi

Ahmed

2023

Legume Science

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Developing nature‐derived surface‐active ingredients with favorable interfacial and functional properties has recently received increasing attention in the food and pharmaceutical industries. Legume proteins are used extensively in food colloidal systems because of their small particle size, high water absorption capability, excellent functional properties (e.g., emulsification, foamability, and gelation), and film formation. There are some limitations in legume proteins, such as high water vapor permeability and fragility, as well as low stability and solubility. Various conventional and innovative processing technologies (e.g., high‐pressure homogenization, ultrasonication, and cold plasma processing) have been successfully employed in order to modify the functional and interfacial properties of legume proteins. In this review, the formation and stability of legume protein‐based colloidal systems and their applications are discussed.

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Physicochemical properties of Grass pea (Lathyrus sativus L.) protein nanoparticles fabricated by cold atmospheric-pressure plasma

Cited by 31 publications

References 126 publications

Self-Assembled Pea Protein Isolate Nanoparticles with Various Sizes: Explore the Formation Mechanism

Self-Assembled Pea Protein Isolate Nanoparticles with Various Sizes: Explore the Formation Mechanism

On treatment options to improve the functionality of pea protein

Recent advances in legume protein‐based colloidal systems

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