Peanut proteins: Applications, ailments and possible remediation

Ghatak, Sumanta Kumar; Sen, Kamalika

doi:10.1016/j.jiec.2012.09.009

Cited by 24 publications

(17 citation statements)

References 66 publications

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“…It is seen that the electrophoretic patterns of control PPI and control EPPI were similar, both displayed five major bands, S66, S41, S40, S38, and S26, named by their molecular weights (MW). Among them, Band S66 was identified as the subunit of conarachin, bands S41, S40, and S38 were identified as the acidic subunits (AS) of arachin, and band S26 was identified as the basic subunit (BS) of arachin (Ghatak et al, 2013;Zhao et al, 2011). According to the literature, arachin and conarachin are the major constitutive proteins in PPI, which account for approximately 90% of the total proteins (Ghatak et al, 2013).…”

Section: Influences Of Extrusion Pretreatment On the Enzymic Proteolysis Of Ppimentioning

confidence: 99%

“…Many legume protein isolates have been investigated as possible emulsifying agents in emulsionbased food (Benjamin, Stilcock, Beaucham, Buettner, & Everett, 2014;Ghatak & Sen, 2013;Karaca, Low, & Nickerson, 2011;Ma, Boye & Simpson, 2016). Among them, peanut protein isolate (PPI) is usually preferred due to the good surface active properties of its major constitutive proteins arachin and conarachin, which have shown to be able to substantially lower the oil/water interfacial tension (Benjamin et al, 2014;Karaca et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…Among them, peanut protein isolate (PPI) is usually preferred due to the good surface active properties of its major constitutive proteins arachin and conarachin, which have shown to be able to substantially lower the oil/water interfacial tension (Benjamin et al, 2014;Karaca et al, 2011). In addition, PPI has been considered as a good nutritional source due to its high content of essential amino acids, low risk of allergic reactions and steady supply, which has gained preference among both consumers and producers (Ghatak et al, 2013). However, due to the rigid globular structures of native peanut proteins, PPI is less capable as an emulsifying agent when compared to milk proteins with flexible molecular structures (McClements & Gumus, 2016).…”

Section: Introductionmentioning

confidence: 99%

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Emulsification performance and interfacial properties of enzymically hydrolyzed peanut protein isolate pretreated by extrusion cooking

Lin

Chen

et al. 2018

Food Hydrocolloids

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Section: Influences Of Extrusion Pretreatment On the Enzymic Proteolysis Of Ppimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Emulsification performance and interfacial properties of enzymically hydrolyzed peanut protein isolate pretreated by extrusion cooking

Lin

Chen

et al. 2018

Food Hydrocolloids

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“…Protein in peanut can be extracted to produce peanut protein isolate (PPI) as food additive [2,3]. In recent years, peanut protein has been receiving increasing attention in food industry due to their unique flavor and amino acid composition [4].…”

Section: Instructionmentioning

confidence: 99%

Effect of Protein Oxidation on the Conformational Properties of Peanut Protein Isolate

Ye¹,

Liao²,

Zhao³

et al. 2013

Journal of Chemistry

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Peanut protein isolate (PPI) was oxidized by peroxyl radicals derived from 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH), and the conformational properties of oxidized PPI were investigated. Oxidation of PPI resulted in gradual carbonyl generation and free sulfydryl group degradation. The analysis of the maximum emission wavelength indicated change in the tertiary conformation of PPI after oxidation. Lower level oxidation could generate soluble protein aggregates with more flexible structure, while higher level oxidation would induce the formation of insoluble aggregates. Result from dynamic light scattering (DLS) and protein solubility showed that protein aggregation was correlated with protein surface hydrophobicity, indicating that protein oxidation and heat treatment could induce protein aggregation, leading to PPI conformational changes.

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“…Peanut protein contains a large number of essential amino acids. It is widely used in the food industry as a kind of plant protein resource [2] . Due to the high nutritional value, peanut protein has an attractive fragrance [3] .…”

Section: Introduction mentioning

confidence: 99%

Rheological properties of peanut protein isolate aggregation suspension and acid-induced gel

Huang¹,

Chi²,

Hua³

et al. 2021

International Journal of Agricultural and Biological Engineering

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The dynamic rheological properties of peanut protein isolate (PPI) suspension and acid-induced PPI gels were studied. In frequency sweep test, the storage modulus (G′) and the loss modulus (G″) of PPI aggregation suspensions at different concentrations increased with the increase of frequency. The steady state shear flow test showed that PPI aggregation suspension had a thinning behavior of the shear, and the image of steady shear curve fitted the Carreau model. After gel formation, acid-induced PPI gels showed a typical Type I behavior (strain thinning) in strain sweep test, meaning that PPI gel got easily broken down, and there was a very small opportunity for the protein molecules to re-establish the network. Compared with the strain sweep of PPI aggregation suspensions and gels, the range of the storage modulus existed a dramatic difference, which could get about tenfold. As the frequency increased, both elasticity and viscosity increased in frequency sweep test, which indicated that the frequency dependence of the storage modulus increased with the increase of concentration.

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Peanut proteins: Applications, ailments and possible remediation

Cited by 24 publications

References 66 publications

Emulsification performance and interfacial properties of enzymically hydrolyzed peanut protein isolate pretreated by extrusion cooking

Emulsification performance and interfacial properties of enzymically hydrolyzed peanut protein isolate pretreated by extrusion cooking

Effect of Protein Oxidation on the Conformational Properties of Peanut Protein Isolate

Rheological properties of peanut protein isolate aggregation suspension and acid-induced gel

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