Rheological characterization of acylated and dextran conjugated African yam bean (Sphenostylis stenocarpa Hochst. Ex A. Rich.) proteins

Arogundade, Lawrence A.; Eromosele, C. O.; Eromosele, Ighodalo C.; Ademuyiwa, Oladipo

doi:10.1016/j.lwt.2011.08.003

Cited by 8 publications

(4 citation statements)

References 37 publications

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“…Glycation and acylation resulted in an apparent viscosity lower than that of the SPI when the shear rate was low. The viscosity of a protein solution depends not only on protein–water interactions, but also on protein–protein interactions (Arogundade et al., 2012). Glycation and acylation promoted unfolding of the protein molecules, increased protein–water interactions, and decreased protein–protein interactions.…”

Section: Resultsmentioning

confidence: 99%

Effects of glycation and acylation on the structural characteristics and physicochemical properties of soy protein isolate

et al. 2021

Journal of Food Science

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This study examined the effects of different sequential treatments of dextran glycation and succinic anhydride acylation on the structure and physicochemical properties of soy protein isolate (SPI). The tested properties included electrophoresis (SDS‐PAGE), Fourier transform infrared spectroscopy, endogenous fluorescence spectroscopy, surface hydrophobicity (H0), free sulfhydryl (‐SH), solubility, interfacial properties, rheological properties, and scanning electron microscope (SEM). The results show that the two treatments significantly improved the structure and functional characteristics of the SPI. The order of the methods had an important effect on the SPI. The lowest H0 (231.76 ± 11.92), the highest free ‐SH content (3.09 ± 0.09 µmol/g), and the highest solubility at pH = 7 (77 ± 3.97%) were obtained when the acylation treatment was followed by the glycation treatment. Emulsification, emulsion stability, foaming, and foam stability were also the highest. Glycation and acylation caused the viscosity coefficient (k) of the SPI solution to decrease compared with SPI alone, but the flow index (n) value increased, and the sum G' value of the conjugate system decreased as gel time increased. SEM showed that its microstructure has changed significantly. Therefore, this research provided an effective method for improving the functional characteristics of SPI and had potential industrial application prospects. Practical Application Glycation and acylation of soybean protein isolate improved the chemical modification method of protein, improved the functional properties of soybean protein, widened its application in food and materials, and provided a new idea for the further development and utilization of soybean protein.

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Section: Resultsmentioning

confidence: 99%

Effects of glycation and acylation on the structural characteristics and physicochemical properties of soy protein isolate

et al. 2021

Journal of Food Science

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“…The viscosity of protein solutions is primarily determined by the interactions between proteins and water, as well as protein-protein interactions [36]. The viscosity of soy protein solutions is affected by the degree of hydration between proteins and water, and it is directly proportional to the extent of hydration.…”

Section: Viscositymentioning

confidence: 99%

“…The forces that stabilize its natural conformation are mainly hydrophobic interactions and hydrogen bonds [5]. On the other hand, 11S, also known as soy globulin, consists of two subunit groups, the acidic A subunit group (35)(36)(37) and the basic B subunit group (20 KDa). These subunits are connected by disulfide bridges and form a hexameric structure [6] (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

Effect of Freezing on Soybean Protein Solution

Chen

Wang

et al. 2023

Foods

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To investigate the impact of frozen storage conditions on the physicochemical properties of soybean protein and explore the underlying mechanisms, this study focused on soybean isolate (SPI), ß-soybean companion globulin (7S), and soybean globulin (11S). The protein solutions were prepared at a concentration of 2% and subjected to freezing for 1 and 5 days. Subsequently, the protein content, physicochemical properties, secondary structure, sulfhydryl content, and chemical interaction forces were assessed and analyzed using UV spectrophotometry, Zeta potential measurements, SDS-PAGE, Fourier infrared spectroscopy, and endogenous fluorescence photoemission spectroscopy. The obtained results revealed that the solubility and total sulfhydryl content of SPI, 7S, and 11S exhibited a decreasing trend with prolonged freezing time. Among them, 11S demonstrated the largest decrease in solubility and total sulfhydryl content, followed by SPI, and 7S the least. During freezing, the aromatic amino acids of SPI, 7S, and 11S molecules were exposed, leading to increased hydrophobicity, protein aggregation, and particle size enlargement, and the structure of the protein changed from disordered structure to ordered structure. After freezing, the polarity of the microenvironment of SPI, 7S, and 11S increased, and their maximum fluorescence emission wavelengths were red-shifted. Notably, the largest red shift of SPI was from 332 nm to 335 nm. As freezing time increased, the contribution of hydrogen bonding increased, while the contribution of hydrophobic interactions decreased. This indicates that freezing affects the hydrophobic interactions, hydrogen bonding, and other chemical forces of the protein. The growth of ice crystals leads to the unfolding of protein molecular chains, exposure of internal hydrophobic groups, enhancement of hydrophobicity, and alters the secondary structure of the protein.

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“…Our previous studies showed that S. stenocarpa protein is highly extractable in aqueous media and the isolated protein is of high nutritional composition (Eromosele et al 2008;Arogundade et al 2009). Its rheological behavior has also been examined (Arogundade et al 2011(Arogundade et al , 2012. However, there is limited knowledge on the functional properties of S. stenocarpa protein isolate.…”

Section: Introductionmentioning

confidence: 99%

EFFECTS OF ISOLATION CONDITIONS ON THE FUNCTIONAL PROPERTIES OF AFRICAN YAM BEAN (SPHENOSTYLIS STENOCARPA HOCHST. EX A. RICH.) PROTEINS

Arogundade

Eromosele

et al. 2012

Journal of Food Processing and Preservation

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African yam bean (Sphenostylis stenocarpa) calcium proteinates and isoelectric proteins were characterized to determine their molecular constitution and functional properties. The electrophoretogram of S. stenocarpa proteins obtained from sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing condition showed that both calcium proteinates and isoelectric proteins had three prominent molecular mass, i.e., 29, 43 and 53 kDa. Calcium precipitation of the protein had a blueshift effect on the protein UV absorption with a shift from 269 nm to 257 nm, whereas UV absorption maximum for isoelectric precipitated protein remained 269 nm as obtainable with flour protein and, thus, no conformational change was associated with isoelectric precipitation. Bulk densities, water and oil absorption capacities of the isolates were in the ranges of 0.76–0.86 g/mL, 2.0–2.33 g/g protein and 0.78–0.99 g/g protein, respectively. Its gelation and water absorption properties were better than or comparable to those of soy bean and some other legumes. PRACTICAL APPLICATIONS African yam bean (Sphenostylis stenocarpa) is a crop grown in some countries in Africa. It produces its edibles (seed grains, root and leaves) in abundance and seems capable of delivering record quantities of protein from soils normally considered marginal. Moreover, the protein is of good nutritional quality. Production of protein isolates from this crop for food formulation and new product development is being envisaged. Its functional attributes examined under this study showed that it might be put to similar use in the food industry as obtainable with soy bean, where high gelling property is of interest in the formulation of value‐added food products.

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Rheological characterization of acylated and dextran conjugated African yam bean (Sphenostylis stenocarpa Hochst. Ex A. Rich.) proteins

Cited by 8 publications

References 37 publications

Effects of glycation and acylation on the structural characteristics and physicochemical properties of soy protein isolate

Effects of glycation and acylation on the structural characteristics and physicochemical properties of soy protein isolate

Effect of Freezing on Soybean Protein Solution

EFFECTS OF ISOLATION CONDITIONS ON THE FUNCTIONAL PROPERTIES OF AFRICAN YAM BEAN (SPHENOSTYLIS STENOCARPA HOCHST. EX A. RICH.) PROTEINS

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