Effect of high intensity ultrasound on physicochemical, interfacial and gel properties of chickpea protein isolate

Wang, Yuntao; Wang, Yingjuan; Li, Ké; Bai, Yanhong; Li, Bin; Xu, Wei

doi:10.1016/j.lwt.2020.109563

Cited by 127 publications

(115 citation statements)

References 42 publications

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“…From Table 3, the foaming properties of ROO· oxidized CPI were compared with those of oxidized white protein (Duan et al., 2018), oxidized rice bran protein (Wu et al., 2020) and ultrasonic CPI (Wang et al., 2020). The foaming performance of ROO· oxidized CPI is significantly better than other processed proteins, and it is nearly twice that of oxidized rice bran protein.…”

Section: Resultsmentioning

confidence: 99%

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Effects of oxidative modification of peroxyl radicals on the structure and foamability of chickpea protein isolates

Zhu

Mao

et al. 2021

Journal of Food Science

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A chickpea protein isolate (CPI) was oxidized using peroxyl radicals derived from 2,2'‐azobis (2‐amidopropane) dihydrochloride (AAPH), and the structural and foaming properties of the oxidized CPI were evaluated. The oxidation degree of protein was determined by measuring carbonyl content, dimer tyrosine content, free thiol content, and total thiol content. The structural changes of oxidized protein were evaluated by surface hydrophobicity, endogenous fluorescence intensity, Fourier transform infrared spectroscopy, SDS‐PAGE, and amino acid content changes. Compared with the control group (0 mmol/L AAPH), moderate oxidation (0.04 mmol/L AAPH) led to the formation of a soluble protein with flexibility, which could improve the foaming properties of the protein (foaming capacity and stability increased by 25.50% and 6.38%, respectively). Over‐oxidized (25 mmol/L AAPH) protein exhibited improved foaming capability, but its foam stability was reduced owing to the formation of insoluble aggregates. The results indicate that oxidation can change protein conformation, and the protein structure can affect the foamability of the CPI. Practical Application CPI is a protein supplement food. Protein oxidation can occur during processing and storage, thereby affecting protein function. In this study, we evaluated how peroxy free radicals affect the structure, solubility and foaming properties of CPI, and clarified the mechanism between them. It has been found that peroxy free radicals can accelerate the oxidation of proteins and have a significant effect on foaming. Therefore, the degree of oxidation should be controlled to improve the quality of CPI.

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Section: Resultsmentioning

confidence: 99%

“…Appropriate modification of proteins has been shown to improve their foaming properties (Meurer et al., 2020). For example, the foaming performance of CPI is improved after ultrasonic treatment (Wang et al., 2020). Chickpeas come in two types—Desi and Kabuli—classified by the morphology and color of the chickpea seeds.…”

Section: Introductionmentioning

confidence: 99%

Effects of oxidative modification of peroxyl radicals on the structure and foamability of chickpea protein isolates

Zhu

Mao

et al. 2021

Journal of Food Science

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“…In this study, the total protein content was increased when CPI was added to MP, which enhanced protein–protein interactions upon heating and induced a more compact gel structure, as will be mentioned later, thus increasing the gel strength. The CPI can also form the gel structure on heating at 80 °C, 30 which was favorable for the improvement of gel strength.…”

Section: Resultsmentioning

confidence: 99%

Effect of chickpea (Cicer arietinum L.) protein isolate on the heat‐induced gelation properties of pork myofibrillar protein

Chen

Dong

et al. 2020

J Sci Food Agric

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BACKGROUND Heat‐induced composite gels were prepared with 30 mg mL−1 pork myofibrillar protein (MP) and chickpea protein isolate (CPI) (0, 3, 6, 9, 12, and 15 g kg−1) in 0.6 mol L−1 NaCl, at pH 7.0. The gel strength, water‐holding capacity, rheological properties, and microstructure of MP‐CPI composite gels were investigated. RESULTS Chickpea protein isolate improved (P < 0.05) gel strength and water‐holding capacity of the MP composite gels. The rheological properties of MP‐CPI composite gels were improved significantly by the addition of CPI. Meanwhile, the effects of CPI on the storage modulus of composite gels were positively correlated with the increased addition of CPI. Furthermore, according to low‐field nuclear magnetic resonance (LF‐NMR) results, the addition of CPI reduced the relaxation time of the composite gels and the relaxation peak area of free water, indicating that CPI could improve the water‐holding capacity of MP‐CPI composite gels. The microstructure of MP‐CPI composite gels presented smaller and more uniform pores, which means that more water could be retained. CONCLUSION The addition of chickpea protein isolate improved the gel strength, water‐holding capacity, rheological properties, and microstructure of MP gels, indicating that CPI could be a potential protein additive to improve the microstructure, texture, and functional quality of meat products. © 2020 Society of Chemical Industry

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“…The Phe and Tyr dichroism intensity of USPIN and SPIN decreased with increasing heating time, that might be due to protein structural unfolding and polypeptide hydrolysis [34] . Ultrasound pretreatment induced an increase in Phe and Tyr dichroism intensity at 0 h. Combined with the particle size results, it is believed that ultrasound could depolymerize larger proteins aggregates into smaller protein particles through cavitation and mechanical effects, exposing more soy protein particles to the solution, thus increasing the soluble tertiary structure [61] , [62] . Ultrasound pretreatment slightly increased the Tyr and Trp dichroism intensity of SPI at 8 h, which indicated that ultrasound changed Tyr and Trp residues microenvironment in USPIN.…”

Section: Resultsmentioning

confidence: 95%

Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils

2021

Ultrasonics Sonochemistry

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Highlights Ultrasound can increase the formation rate of soy protein isolate nanofibrils. Ultrasound-pretreated soy protein isolate nanofibrils has a smaller particle size. Ultrasound can increase β-sheet contents of SPI nanofibrils, promoting the nanofibrils formation. Ultrasound can promote protein unfolding and exposing more binding sites.

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Effect of high intensity ultrasound on physicochemical, interfacial and gel properties of chickpea protein isolate

Cited by 127 publications

References 42 publications

Effects of oxidative modification of peroxyl radicals on the structure and foamability of chickpea protein isolates

Effects of oxidative modification of peroxyl radicals on the structure and foamability of chickpea protein isolates

Effect of chickpea (Cicer arietinum L.) protein isolate on the heat‐induced gelation properties of pork myofibrillar protein

Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils

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