Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate

Zhang, Qiuting; Tu, Zong–cai; Xiao, Hui; Wang, Hui; Huang, Xiaoqin; Liu, Guangxian; Liu, Chengmei; Shi, Yan; Li, Fan; Lin, Derong

doi:10.1016/j.fbp.2013.07.006

Cited by 252 publications

(145 citation statements)

References 33 publications

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“…6c). This finding was in agreement with the results obtained by some researchers [48,49]. Untreated zeins were aggregated into large protein masses because of their high hydrophobicity (Fig.…”

Section: Scanning Electron Microscopy (Sem)supporting

confidence: 95%

Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal

Jun-ze

Wang

et al. 2015

Ultrasonics Sonochemistry

190

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The aim of this study was to investigate the effect of multi-frequency power ultrasound (sweeping frequency and pulsed ultrasound (SFPU) and sequential dual frequency ultrasound (SDFU)) on the enzymolysis of corn gluten meal (CGM) and on the structures of the major protein fractions (zein, glutelin) of CGM. The results showed that multi-frequency power ultrasound pretreatments improved significantly (P<0.05) the degree of hydrolysis and conversion rate of CGM. The changes in UV-Vis spectra, fluorescence emission spectra, surface hydrophobicity (H0), and the content of SH and SS groups indicated unfolding of zein and glutelin by ultrasound. The circular dichroism analysis showed that both pretreatments decreased α-helix and increased β-sheet of glutelin. The SFPU pretreatment had little impact on the secondary structure of zein, while the SDFU increased the α-helix and decreased the β-sheet remarkably. Scanning electron microscope indicated that both pretreatments destroyed the microstructures of glutelin and CGM, reduced the particle size of zein despite that the SDFU induced aggregation was observed. In conclusion, multi-frequency power ultrasound pretreatment is an efficient method in protein proteolysis due to its sonochemistry effect on the molecular conformation as well as on the microstructure of protein.

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Section: Scanning Electron Microscopy (Sem)supporting

confidence: 95%

Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal

Jun-ze

Wang

et al. 2015

Ultrasonics Sonochemistry

190

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“…The surface hydrophobicity also correlated positively with the emulsification indices of peanut proteins/peptides (for EAI, R 2 ¼ 0.982; for ESI, R 2 ¼ 0.906; n ¼ 12). These results were consistent with those from a recent report for peanut proteins (Zhang et al, 2014) and earlier studies for other proteins (Kato & Nakai, 1980;Moro, Gatti, & Delorenzi, 2001). On the other hand, Hiller and Lorenzen (2008) reported a negative correlation between surface hydrophobicity and emulsion stability, and detected no clear correlation between the surface hydrophobicity and the emulsion activity for enzymatically and physico-chemically treated milk proteins.…”

Section: Emulsification Propertiessupporting

confidence: 93%

Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

Zhang

2015

Food Hydrocolloids

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“…As shown in Figure 5b, both treatments could significantly decrease (p < 0.05) the water absorption capacity and increase the oil absorption capacity. Our finding is similar to previous studies about peanut and soy protein (Hu et al, 2013;Zhang et al, 2014). Those results indicated that both treatments could induce the unfolding of protein by exposure hydrophobic groups initially buried in the interior of the molecule.…”

Section: Effect Of Ultrasound Pretreatment On Structure Of Qpisupporting

confidence: 93%

Effects of high‐intensity ultrasound pretreatment with different levels of power output on the antioxidant properties of alcalase hydrolyzates from Quinoa (Chenopodium quinoa Willd.) protein isolate

et al. 2018

Cereal Chem

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Background and objectives:The effects of ultrasound pretreatment with different levels of power output (200, 400, and 600 W) on hydrolysis degree of Quinoa protein isolate (QPI) and antioxidant activity of QPI hydrolyzate were studied.The secondary structure, surface hydrophobicity, intrinsic fluorescence, and scanning electron microscopy (SEM) of QPI treated by ultrasound were measured.The untreated QPI and high-temperature treatment (90°C for 30 min) were used as control. Findings:The results showed that ultrasound pretreatment at 400 W significantly improved the hydrolysis degree of QPI and antioxidant activity of QPI hydrolyzate. The changes in secondary structure, surface hydrophobicity, and intrinsic fluorescence indicated the unfolding of QPI after ultrasound. The SEM results showed that ultrasound treatment resulted in the deformation of QPI. Conclusions:The improvement in degree of hydrolysis might be related to the changes in structure induced by ultrasound treatment, which supported more groups for the process of enzymatic hydrolysis. Significance and novelty: The power output selection of ultrasound pretreatment is essential for improvement of accessibility of QPI to the alcalase and preparation of antioxidant peptides. K E Y W O R D Santioxidant activity, Quinoa protein isolate, structure, ultrasound pretreatment

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Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate

Cited by 252 publications

References 33 publications

Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal

Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal

Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

Effects of high‐intensity ultrasound pretreatment with different levels of power output on the antioxidant properties of alcalase hydrolyzates from Quinoa (Chenopodium quinoa Willd.) protein isolate

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