Structural changes in gluten protein structure after addition of emulsifier. A Raman spectroscopy study

Author(s):  
Evelina G. Ferrer ◽  
Analía V. Gómez ◽  
María C. Añón ◽  
María C. Puppo
2016 ◽  
Vol 443 ◽  
pp. 130-135 ◽  
Author(s):  
Mouritz N. Svenson ◽  
Michael Guerette ◽  
Liping Huang ◽  
Morten M. Smedskjaer

ChemCatChem ◽  
2016 ◽  
Vol 8 (5) ◽  
pp. 976-983 ◽  
Author(s):  
Jana Engeldinger ◽  
Jörg Radnik ◽  
Carsten Kreyenschulte ◽  
François Devred ◽  
Eric M. Gaigneaux ◽  
...  

2014 ◽  
Vol 97 (5) ◽  
pp. 1421-1424 ◽  
Author(s):  
Ran Zhang ◽  
Jing Ren ◽  
Himanshu Jain ◽  
Yinyao Liu ◽  
Zhongwen Xing ◽  
...  

Author(s):  
Selva Rivas-Arancibia ◽  
Erika Rodríguez-Martínez ◽  
Isidro Badillo-Ramírez ◽  
Ulises López-González ◽  
José M. Saniger

2018 ◽  
Vol 55 (5A) ◽  
pp. 211
Author(s):  
Do Thi Yen

Structural changes, textural properties in Tilapia surimi myofibrillar protein during gelation were studied by Raman spectroscopy. The change in the amide I (1600-1700 cm-1) region indicated that the decrease in a-helices content accompanied by increase in ß-sheet and random coil after heating. The conformation of S-S bond was observed in the Raman spectrum near 500-600 cm-1 in the samples of 30-40 oC incubation temperature which produce textural profile with high gel strength. Intensity of the band near 758 cm-1 as well as a slight decrease in I853/I826 ratio when the heat increase 60-70 oC showed that the hydrophobic interaction was involved in the heat-induced gelation of surimi protein. 


2015 ◽  
Vol 57 (11) ◽  
pp. 2286-2289 ◽  
Author(s):  
A. S. Oreshonkov ◽  
A. K. Khodzhibaev ◽  
A. S. Krylov ◽  
M. F. Umarov ◽  
A. N. Vtyurin

Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 48
Author(s):  
Ana M. Herrero ◽  
Claudia Ruiz-Capillas

Considerable attention has been paid to emulsion gels (EGs) in recent years due to their interesting applications in food. The aim of this work is to shed light on the role played by chia oil in the technological and structural properties of EGs made from soy protein isolates (SPI) and alginate. Two systems were studied: oil-free SPI gels (SPI/G) and the corresponding SPI EGs (SPI/EG) that contain chia oil. The proximate composition, technological properties (syneresis, pH, color and texture) and structural properties using Raman spectroscopy were determined for SPI/G and SPI/EG. No noticeable (p > 0.05) syneresis was observed in either sample. The pH values were similar (p > 0.05) for SPI/G and SPI/EG, but their texture and color differed significantly depending on the presence of chia oil. SPI/EG featured significantly lower redness and more lightness and yellowness and exhibited greater puncture and gel strengths than SPI/G. Raman spectroscopy revealed significant changes in the protein secondary structure, i.e., higher (p < 0.05) α-helix and lower (p < 0.05) β-sheet, turn and unordered structures, after the incorporation of chia oil to form the corresponding SPI/EG. Apparently, there is a correlation between these structural changes and the textural modifications observed.


2021 ◽  
Vol 358 ◽  
pp. 129916
Author(s):  
Eloïse Lancelot ◽  
Joran Fontaine ◽  
Joëlle Grua-Priol ◽  
Ali Assaf ◽  
Gérald Thouand ◽  
...  

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