Improvement in enzymolysis efficiency and changes in conformational attributes of corn gluten meal by dual-frequency slit ultrasonication action

•DFSU pretreatment enhanced enzymolysis efficiency of CGM.•CGM conformation was significantly altered upon sonication.•Protein fragments with uniform size could be associated with changes in enzymolysis.•Proposed mechanism of sonicated CGM was summarized. The influences of dual-frequency slit ultras...

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Bibliographic Details
Published in:Ultrasonics sonochemistry 2020-06, Vol.64, p.105038-105038, Article 105038
Main Authors: Wang, Yang, Zhang, Zhaoli, He, Ronghai, Liu, Dandan, Kumah Mintah, Benjamin, Dabbour, Mokhtar, Ma, Haile
Format: Article
Language:English
Subjects:
Conformational characteristics
Corn gluten meal (CGM)
Disulfides - chemistry
Dual-frequency slit ultrasound (DFSU)
Enzymolysis
Food Handling
Glutens - chemistry
Glutens - metabolism
Hydrolysis
Kinetics
Models, Molecular
Protein Conformation
Proteolysis
Sonication
Subtilisins - metabolism
Temperature
Zea mays - chemistry
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Summary:•DFSU pretreatment enhanced enzymolysis efficiency of CGM.•CGM conformation was significantly altered upon sonication.•Protein fragments with uniform size could be associated with changes in enzymolysis.•Proposed mechanism of sonicated CGM was summarized. The influences of dual-frequency slit ultrasound (DFSU) pretreatment with various working parameters on the enzymolysis efficiency and conformational characteristics of corn gluten meal (CGM) were studied. Results indicated that under the conditions of ultrasonic power density of 80 W/L, time of 30 min, ultrasonic intermittent ratio of 5:2 s/s, temperature of 30 °C, and substrate concentration of 50 g/L, the relative enzymolysis efficiency (REE) of CGM reached a maximum of 21.05%, and the protein dissolution rate was 68.50%. In addition, ultrasonication had considerable impact on the conformation of CGM and consequently improved the susceptibility to alcalase proteolysis. Changes in free sulfhydryl (SHF) and disulfide bonds (SS) groups indicated spatial conformation of CGM was altered following sonication (sonochemical) treatment. Fourier Transform Infrared Spectrum (FITR) analysis showed a reduction in α-helix and β-turn content; and an increase in β-sheet and random coil content of CGM. Alterations in the particle size, particle size distribution, microstructure and surface roughness (Ra, Rq) indicated generation of smaller and more uniform protein fragments of CGM by sonochemical pretreatment. The proposed mechanism of sonicated CGM was elaborated. Our findings suggest that using DFSU in pretreating CGM may be an efficacious approach to enhance proteolysis.
ISSN:1350-4177
1873-2828
DOI:10.1016/j.ultsonch.2020.105038