scholarly journals THE CHANGES OF PROTEIN STRUCTURE IN TILAPIA SURIMI DURING GELATION BY RAMAN SPECTROSCOPY

2018 ◽  
Vol 55 (5A) ◽  
pp. 211
Author(s):  
Do Thi Yen
Keyword(s):  
Raman Spectroscopy ◽  
Raman Spectrum ◽  
Protein Structure ◽  
Hydrophobic Interaction ◽  
Structural Changes ◽  
Incubation Temperature ◽  
Textural Properties ◽  
Myofibrillar Protein ◽  
Gel Strength ◽  
Random Coil

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. 

scholarly journals FT-Raman Spectroscopy as a Tool to Study the Secondary Structures of Wheat Gliadin Proteins

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5388
Author(s):  
Iwona Stawoska ◽  
Aleksandra Wesełucha-Birczyńska ◽  
Andrzej Skoczowski ◽  
Michał Dziurka ◽  
Jacek Waga
Keyword(s):  
Raman Spectroscopy ◽  
Structural Changes ◽  
Secondary Structures ◽  
Random Coil ◽  
Moderate Increase ◽  
Disulfide Bridges ◽  
Ft Raman Spectroscopy ◽  
Wheat Gliadin ◽  
Wheat Kernels ◽  
Ft Raman

Raman spectroscopy is a useful method in biological, biomedical, food, and agricultural studies, allowing the simultaneous examination of various chemical compounds and evaluation of molecular changes occurring in tested objects. The purpose of our research was to explain how the elimination of ω-fractions from the wheat gliadin complex influences the secondary structures of the remaining αβγ-gliadins. To this aim, we analyzed the endosperm of wheat kernels as well as gliadin proteins extracted from two winter wheat genotypes: wasko.gl+ (control genotype containing the full set of gliadins) and wasko.gl− (modified genotype lacking all ω-gliadins). Based on the decomposition of the amide I band, we observed a moderate increase in β-forms (sheets and turns) at the expense of α-helical and random coil structures for gliadins isolated from the flour of the wasko.gl− line. Since ω-gliadins contain no cysteine residues, they do not participate in the formation of the disulfide bridges that stabilize the protein structure. However, they can interact with other proteins via weak, low-energetic hydrogen bonds. We conclude that the elimination of ω-fractions from the gliadin complex causes minor modifications in secondary structures of the remaining gliadin proteins. In our opinion, these small, structural changes of proteins may lead to alterations in gliadin allergenicity.

scholarly journals Protein structural changes during processing of vegetable feed ingredients used in swine diets: implications for nutritional value

2016 ◽  
Vol 29 (1) ◽  
pp. 126-141 ◽  
Author(s):  
S. Salazar-Villanea ◽  
W. H. Hendriks ◽  
E. M. A. M. Bruininx ◽  
H. Gruppen ◽  
A. F. B. van der Poel
Keyword(s):  
Protein Structure ◽  
Structural Changes ◽  
Protein Digestibility ◽  
Random Coil ◽  
Processing Parameter ◽  
Simultaneous Application ◽  
Feed Ingredients ◽  
Maillard Reactions ◽  
Native Proteins ◽  
Swine Diets

AbstractProtein structure influences the accessibility of enzymes for digestion. The proportion of intramolecular β-sheets in the secondary structure of native proteins has been related to a decrease in protein digestibility. Changes to proteins that can be considered positive (for example, denaturation and random coil formation) or negative (for example, aggregation and Maillard reactions) for protein digestibility can occur simultaneously during processing. The final result of these changes on digestibility seems to be a counterbalance of the occurrence of each phenomenon. Occurrence of each phenomenon depends on the conditions applied, but also on the source and type of the protein that is processed. The correlation between denaturation enthalpy after processing and protein digestibility seems to be dependent on the protein source. Heat seems to be the processing parameter with the largest influence on changes in the structure of proteins. The effect of moisture is usually limited to the simultaneous application of heat, but increasing level of moisture during processing usually increases structural changes in proteins. The effect of shear on protein structure is commonly studied using extrusion, although the multifactorial essence of this technology does not allow disentanglement of the separate effects of each processing parameter (for example, heat, shear, moisture). Although most of the available literature on the processing of feed ingredients reports effects on protein digestibility, the mechanisms that explain these effects are usually lacking. Clarifying these mechanisms could aid in the prediction of the nutritional consequences of processing conditions.

scholarly journals Structural and Technological Approach to Reveal the Role of the Lipid Phase in the Formation of Soy Emulsion Gels with Chia Oil

Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 48
Author(s):  
Ana M. Herrero ◽  
Claudia Ruiz-Capillas
Keyword(s):  
Raman Spectroscopy ◽  
Structural Properties ◽  
Structural Changes ◽  
Protein Secondary Structure ◽  
Lipid Phase ◽  
Α Helix ◽  
Β Sheet ◽  
Shed Light ◽  
Chia Oil

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.

Study of structural changes of gluten proteins during bread dough mixing by Raman spectroscopy

2021 ◽  
Vol 358 ◽  
pp. 129916
Author(s):  
Eloïse Lancelot ◽  
Joran Fontaine ◽  
Joëlle Grua-Priol ◽  
Ali Assaf ◽  
Gérald Thouand ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Structural Changes ◽  
Bread Dough ◽  
Gluten Proteins ◽  
Dough Mixing

scholarly journals Overview of Popular Techniques of Raman Spectroscopy and Their Potential in the Study of Plant Tissues

Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1537
Author(s):  
Aneta Saletnik ◽  
Bogdan Saletnik ◽  
Czesław Puchalski
Keyword(s):  
Raman Spectroscopy ◽  
Cell Walls ◽  
Structural Changes ◽  
Spatial Information ◽  
Technological Development ◽  
Analytical Techniques ◽  
High Sensitivity ◽  
Plant Tissues ◽  
Wide Range ◽  
Identification Technique

Raman spectroscopy is one of the main analytical techniques used in optical metrology. It is a vibration, marker-free technique that provides insight into the structure and composition of tissues and cells at the molecular level. Raman spectroscopy is an outstanding material identification technique. It provides spatial information of vibrations from complex biological samples which renders it a very accurate tool for the analysis of highly complex plant tissues. Raman spectra can be used as a fingerprint tool for a very wide range of compounds. Raman spectroscopy enables all the polymers that build the cell walls of plants to be tracked simultaneously; it facilitates the analysis of both the molecular composition and the molecular structure of cell walls. Due to its high sensitivity to even minute structural changes, this method is used for comparative tests. The introduction of new and improved Raman techniques by scientists as well as the constant technological development of the apparatus has resulted in an increased importance of Raman spectroscopy in the discovery and defining of tissues and the processes taking place in them.

scholarly journals Structural Changes in Doped Ge2Sb2Te5 Thin Films Studied by Raman Spectroscopy

2013 ◽  
Vol 44 ◽  
pp. 82-90 ◽  
Author(s):  
S. Kozyukhin ◽  
M. Veres ◽  
H.P. Nguyen ◽  
A. Ingram ◽  
V. Kudoyarova
Keyword(s):  
Thin Films ◽  
Raman Spectroscopy ◽  
Structural Changes

Effects of in-Office and at-Home Bleaching on Human Enamel and Dentin: An in vitro Application of Fourier Transform Infrared Study

2008 ◽  
Vol 62 (11) ◽  
pp. 1274-1279 ◽  
Author(s):  
Feride Severcan ◽  
Kurtulus Gokduman ◽  
Ayca Dogan ◽  
Sukran Bolay ◽  
Saadet Gokalp
Keyword(s):  
Fourier Transform ◽  
Structural Changes ◽  
Protein Denaturation ◽  
Random Coil ◽  
Protein Ratio ◽  
Band Frequency ◽  
Human Enamel ◽  
Ft Ir ◽  
At Home

In-office and at-home bleaching techniques are widely used methods for the whitening of teeth. However, the safety of these techniques has not been clarified yet. The aim of the current study is to investigate the in-office- and at-home-bleaching-induced structural and quantitative changes in human enamel and dentin at the molecular level, under in vitro conditions. The Fourier transform mid-infrared (mid-FT-IR) spectroscopic technique was used to monitor bleaching-induced structural changes. Band frequency and intensity values of major absorptions such as amide A, amide I, phosphate (PO4), and carbonate (CO3−2) bands, for treatment groups and control, were measured and compared. The results revealed that both procedures have negligible effects on dentin constituents. In office-bleached enamel, in addition to demineralization, a decrease in protein and polysaccharide concentrations, mineral-to-protein ratio, and the strength of hydrogen bonds around NH groups, as well as a change in protein secondary structure were observed. The protein structure changed from β-sheet to random coil, which is an indication of protein denaturation. However, no significant variations were observed for at-home bleached enamel. The control, at-home, and in-office bleached enamel samples were differentiated with a high accuracy using cluster analysis based on FT-IR data. This study revealed that office bleaching caused deleterious alterations in the composition and structure of enamel that significantly affected the crystallinity and mineralization of the tissue. Therefore, at-home bleaching seems to be much safer than in-office bleaching in terms of molecular variations.

Raman Studies of the Adduct Structure of Cl2 and Br2 with Piaselenole

1980 ◽  
Vol 34 (6) ◽  
pp. 636-638
Author(s):  
J. J. Blaha ◽  
W. Brittain ◽  
C. E. Meloan ◽  
W. G. Fateley
Keyword(s):  
Molecular Structure ◽  
Raman Spectroscopy ◽  
Raman Spectrum ◽  
Long Time

The affinity of 2,1,3-benzoselenadiazole, commonly called piaselenole, for chlorine and bromine molecules has been known for a long time. Raman spectroscopy provides a very interesting method for determining the molecular structure of these 1:1 adducts. The Raman spectrum shows the Cl2 and Br2 molecules in the adduct remain as a dimer molecule.

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