Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate

Gong, Kuijie; Shi, Aimin; Liu, Hongzhi; Liu, Li; Hu, Hui; Adhikari, Benu; Wang, Qiang

doi:10.1016/j.jfoodeng.2015.09.011

Cited by 121 publications

(90 citation statements)

References 32 publications

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“…PPI flour preparation was according to the method of Gong et al . () and stored in a 4 °C freezer (BCD‐245, Haier, Qingdao, China). The protein content of the prepared PPI flour was 90.2% (w/w), determined using a fully automated Kjeldahl apparatus (Kjeltec 2300, Foss, Denmark).…”

Section: Methodsmentioning

confidence: 99%

“…Commercial defatted peanut flour was obtained from Gaotang Lanshan Co., Ltd. (Shandong Province, China). PPI flour preparation was according to the method of Gong et al (2016a) and stored in a 4°C freezer Haier,Qingdao,China MO, USA). Human recombinant renin inhibitor screening assay kit was purchased from Cayman (Cayman Chemical, Ann Arbor, MI, USA).…”

Section: Methodsmentioning

confidence: 99%

“…The mixer was settled for 30 min and then centrifuged at 3200 g for 30 min. The protein content (C 1 ) of 5 mL of supernatant was determined according to previously reported (Gong et al, 2016a). The total protein content (C 0 ) of the aqueous solution of PPH was determined by the same method.…”

Section: Determination Of Trichloroacetic Acid-nitrogen Soluble Indexmentioning

confidence: 99%

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High‐pressure microfluidisation pretreatment disaggregate peanut protein isolates to prepare antihypertensive peptide fractions

Gong

Deng

Shi

et al. 2017

Int J of Food Sci Tech

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Summary High‐pressure microfluidisation (HPM) pretreatment was applied to increase in vitro antihypertensive activity of peanut peptide fractions (PPF). The morphology of protein in aqueous dispersion revealed that peanut protein isolate (PPI) disaggregated at relatively low pressure (≤120 MPa) and re‐aggregated at relatively high pressures (150–210 MPa). The treated pressure of 120 MPa could lead to the most disaggregation of PPI. Small peptides contents, trichloroacetic acid‐nitrogen soluble index (TCA‐NSI) and degree of hydrolysis (DH) of peanut protein hydrolysates (PPH) all reached the highest at 120 MPa. Consequently, it possessed the highest angiotensin converting enzyme (ACE) and renin inhibitory activity. The highest surface hydrophobicity occurred at 120 MPa pretreatment samples. Thirty‐nine oligopeptides at 120 MPa pretreatment were identified by ultra‐performance liquid chromatography‐quadrupole time‐of‐flight (UPLC‐Q‐TOF) mass spectrometer combined with Progenesis QI for Proteomics software compared with 29 and 35 at control and 210 MPa, respectively. This meant that disaggregation of PPI at 120 MPa resulted in the release of new hydrophobic peptide.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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High‐pressure microfluidisation pretreatment disaggregate peanut protein isolates to prepare antihypertensive peptide fractions

Gong

Deng

Shi

et al. 2017

Int J of Food Sci Tech

Self Cite

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“…1b). The lower surface hydrophobicity observed in the cod protein powder compared to herring might be related to the lower amount of conformational changes and thereby less exposure of internal hydrophobic side chains (Gong et al 2015) caused by less extreme solubilization pH (pH 11.5) used for this species compared to herring (pH 12). Since both herring and salmon proteins were recovered using the same solubilization pH (12), the lower surface hydrophobicity observed in the salmon Glycine 115.1 ± 3.1 110.4 ± 2.1 76.8 ± 2.7 51.6 ± 3.1 49.4 ± 0.9 47.9 ± 0.9 48.6 ± 1.1 38.9 ± 1.6 18.1 ± 1.3 Alanine 65.8 ± 3.4 64.1 ± 2.0 61.7 ± 0.9 62.5 ± 3.4 63.5 ± 1.1 64.6 ± 0.6 43.6 ± 0.5 56.2 ± 0.7 49.5 ± 1.2 Serine 44.3 ± 1.7 56.3 ± 0.5 48.1 ± 0.6 43.8 ± 1.7 45.5 ± 0.7 42.8 ± 0.1 52.0 ± 0.6 70.8 ± EAA total essential amino acid, NEAA total non-essential amino acid, AA total amino acid *Shows essential amino acids protein powder might be attributed to its higher refolding capacity after pH-readjustment.…”

Section: Surface Hydrophobicitymentioning

confidence: 99%

“…Active and total sulfhydryl groups content of the proteins were measured as explained by Gong et al (2015). Initially, 180 mg of protein was added to 30 mL Triseglycine buffer (0.086 M Tris, 0.09 M glycine, 4 mM EDTA, pH 8.0) containing 8 M urea and stirred for 30 min at room temperature.…”

Section: Active and Total Sulfhydryl Groups Measurementmentioning

confidence: 99%

Structural, functional, and sensorial properties of protein isolate produced from salmon, cod, and herring by-products

Abdollahi

Undeland

2018

Food Bioprocess Technol

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Nutritional, structural, functional, and sensorial properties of protein isolate developed from salmon (Salmo salar), cod (Gadus morhua), and herring (Clupea harengus) by-products using the pH-shift method was studied. Function of the proteins in an emulsion system in terms of viscoelastic properties was also evaluated. Regardless of origin, the proteins showed satisfying nutritional value as reflected in their high essential amino acid content. The proteins contained significantly (p < 0.05) higher proportion of active sulfhydryl groups and surface hydrophobicity compared to whey and egg white protein reflecting conformational changes caused by the pH-shift process. Solubility, emulsion, and foaming capacity of the proteins showed a trend similar to soy protein and dependent on their origin. Cod protein had better emulsion and foaming capacity than salmon and herring proteins which was in line with its high surface hydrophobicity and myosin heavy chain content. Emulsions developed from cod and salmon proteins showed substantially better viscoelastic properties, with higher stability and viscosity compared to herring protein emulsions. Cod protein scored low for sensorial attributes related to lipid oxidation while herring protein showed high levels of fishy and rancid flavor and odor. Altogether, results showed that the proteins from fish filleting by-products have potential to be used as food ingredients, but their application would be governed by their origin and sensorial properties.

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Freeze‐Drying of Meat and Seafood Products

Agregán,

Echegaray,

Munekata

et al. 2024

Freeze Drying of Food Products

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Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate

Cited by 121 publications

References 32 publications

High‐pressure microfluidisation pretreatment disaggregate peanut protein isolates to prepare antihypertensive peptide fractions

High‐pressure microfluidisation pretreatment disaggregate peanut protein isolates to prepare antihypertensive peptide fractions

Structural, functional, and sensorial properties of protein isolate produced from salmon, cod, and herring by-products

Freeze‐Drying of Meat and Seafood Products

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