Effects of ultrasound on the structure and physical properties of black bean protein isolates

Jiang, Lianzhou; Wang, Jing; Li, Yang; Wang, Zhongjiang; Liang, Jing; Wang, Rui; Chen, Yong; Ma, Wenjun; Qi, Baokun; Zhang, Min

doi:10.1016/j.foodres.2014.04.022

Cited by 475 publications

(318 citation statements)

References 48 publications

Supporting

Mentioning

261

Contrasting

Unclassified

Order By: Relevance

“…The fluorescence intensity of ANS and protein is positively correlated with the surface hydrophobicity of protein [34,50]. As can be seen from Figure 3, the surface hydrophobicity of the protein samples pretreated by ultrasound was significantly higher than that of the control group (without sonication), ultrasound pretreatment significantly ( < 0.05) improved the surface hydrophobicity of rapeseed protein hydrolysates, and these results are consistent with the results reported in the literature [24,51,52]. The increased hydrophobicity of the protein surface indicates that the protein molecules are stretched under the cavitation of the ultrasound, thus exposing the hydrophobic groups located inside the protein molecule.…”

Section: Effect Of Ultrasound Power On Surface Hydrophobicity (Ho) Ofsupporting

confidence: 89%

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

Wali

Shahnawaz

et al. 2017

Journal of Chemistry

View full text Add to dashboard Cite

The effects of power ultrasound pretreatments on the degree of hydrolysis (DH), angiotensin-I-converting enzyme (ACE) inhibitory activity, amino acid composition, surface hydrophobicity, protein solubility, and thermal stability of ACE inhibition of rapeseed protein hydrolysates were evaluated. Ultrasonic pretreatments before enzymolysis in terms of power and exposure time increased the DH and ACE inhibitory activities over the control (without sonication). In this study, maximum DH 22.07% and ACE inhibitory activity 72.13% were achieved at 600 W and 12 min pretreatment. Compared to the hydrolysates obtained without sonication, the amino acid profile of ultrasound pretreated hydrolysates showed significant changes particularly in the proline content and hydrophobic amino acids with an increased rate of 2.47% and 6.31%, respectively. Ultrasound pretreatment (600 watts, 12 min) improved functional properties of protein hydrolysates over control by enhancing surface hydrophobicity and solubility index with an increased rate of 130.76% and 34.22%. Moreover, the stability test showed that the ACE inhibitory activity remains stable against heat treatments. However, extensive heat, prolonged heating time, and alkaline conditions were not in the favor of stability test, while under mild heat and acidic conditions their ACE inhibitory activities were not significantly different from unheated samples.

show abstract

Section: Effect Of Ultrasound Power On Surface Hydrophobicity (Ho) Ofsupporting

confidence: 89%

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

Wali

Shahnawaz

et al. 2017

Journal of Chemistry

View full text Add to dashboard Cite

show abstract

“…[11] In contrast, an increase in the β-sheet structure with a concomitant decrease in α-helix structure has been observed in black bean protein isolates under sonication. [27] However, ultrasound did not lead to significant changes in the secondary conformation, except for increasing strand 1. [1] These different changes to the secondary structure under the different treatments might be due to different treatment conditions, protein type, dominant secondary structure type, and degree of ordered structure.…”

Section: Secondary Structural Analysismentioning

confidence: 90%

“…Similar results have been obtained in the SDS-PAGE studies of ultrasonication-treated β-Lg, [21] ovalbumin, [19] and black bean protein isolate. [27] The band intensity of β-Lg had slightly decreased after UV-C treatment, especially the 30-min UV-C treatment (Figure 1). Similarly, UV-C treatment for 15 min resulted in reduced β-Lg band intensities, which reduced more with increasing treatment time.…”

Section: Sds-page Of β-Lgmentioning

confidence: 96%

“…[36] However, ultrasound treatment also causes an increase in the surface hydrophobicity for soy protein isolate (SPI) and ovalbumin. [19,27] The Ho of the ultrasound-treated samples increased due to protein unfolding or decreased due to protein aggregation/partial denaturation of proteins, [27] which was closely related to the protein type and composition, as well as the ultrasound conditions.…”

Section: Surface Hydrophobicity (Ho)mentioning

confidence: 99%

See 1 more Smart Citation

Structural and oxidative modifications, and antioxidant activity of β-lactoglobulin treated by ultraviolet light-C and ultrasound

Zheng²,

Wang

et al. 2017

International Journal of Food Properties

View full text Add to dashboard Cite

“…Arzeni et al [24] reported that dual-frequency ultrasound can significantly increase the cavitation yield compared with that by two individual ultrasonic irradiation types. This higher cavitation yield is due to increased transfer of the input electrical energy and an increased resonance effect, which contribute to bubble growth and yield the maximum bubble size [25]. Furthermore, the dual sweeping frequency ultrasound contributed to unfolding of the molecular structure of zein and hydrolysis of zein-releasing peptides with high ACE inhibitory activity.…”

Section: Effect Of Ultrasound Pretreatment On Ace Inhibitory Activitymentioning

confidence: 99%

Effects of Different Working Modes of Ultrasound on Structural Characteristics of Zein and ACE Inhibitory Activity of Hydrolysates

Ren

Zhang

Liang

et al. 2017

Journal of Food Quality

View full text Add to dashboard Cite

Ultrasound was used as a new technology to pretreat protein prior to proteolysis to improve enzymolysis efficiency. The effects of different working modes of ultrasound on the angiotensin I-converting enzyme (ACE) inhibitory activity of zein hydrolysates and the structural characteristics of zein were investigated. The solubility, surface hydrophobicity ( 0 ), ultraviolet-visible (UV-Vis) spectra, intrinsic fluorescence spectra, and circular dichroism (CD) spectra of zein pretreated with ultrasound were determined. All ultrasound pretreatments significantly improved the ACE inhibitory activity of zein hydrolysates ( < 0.05). The highest ACE inhibitory activity, representing an increase of 99.21% over the control, was obtained with dual sweeping frequency ultrasound of 33 ± 2 and 68 ± 2 kHz. The effects of single sweeping frequency and dual fixed frequency ultrasound were stronger than those of single fixed frequency ultrasound for improving the ACE inhibitory activity of zein. Structural changes in zein were induced by ultrasound, as confirmed by changes in the solubility, 0 , UV-Vis spectra, intrinsic fluorescence spectra, and CD spectra of zein, and these were consistent with the corresponding ACE inhibitory activities of zein hydrolysates. Thus, ultrasound working mode and frequency have significant effects on the structure of zein and the ACE inhibitory activity of zein hydrolysates.

show abstract

Effects of ultrasound on the structure and physical properties of black bean protein isolates

Cited by 475 publications

References 48 publications

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

Structural and oxidative modifications, and antioxidant activity of β-lactoglobulin treated by ultraviolet light-C and ultrasound

Effects of Different Working Modes of Ultrasound on Structural Characteristics of Zein and ACE Inhibitory Activity of Hydrolysates

Contact Info

Product

Resources

About