scholarly journals Functional Properties of Lupinus angustifolius Seed Protein Isolates

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
Antonio Hilario Lara-Rivera ◽  
Pedro García-Alamilla ◽  
Laura Mercedes Lagunes-Gálvez ◽  
Ramón Rodríguez Macias ◽  
Pedro M. García López ◽  
...  
Keyword(s):  
Functional Properties ◽  
Foam Stability ◽  
Nitrogen Solubility ◽  
Activity Index ◽  
Stability Index ◽  
Lupinus Angustifolius ◽  
Minimum Concentration ◽  
Protein Isolates ◽  
Isoelectric Ph ◽  
Ph Range

Protein isolates prepared by alkaline solubilization followed by isoelectric precipitation and freeze-drying from six varieties of Lupinus angustifolius (Haags Blaue, Sonate, Probor, Borlu, Boregine, and Boruta) grown in Mexico were evaluated for functional properties: nitrogen solubility, water-holding capacity (WHC), oil holding capacity (OHC), emulsion activity index (EAI), emulsion stability index (ESI), foaming capacity (FC), foam stability (FS), and gelling minimum concentration (GMC). The nitrogen solubility values, WHC, OHC, and FC did not show significant differences between the protein isolates. The solubility of the isolates was minimal at pH of 4.0 and 5.0 while the regions of maximum solubility were found at pH of 2.0 and 10.0. There were significant differences in EAI and ESI depending on the varieties used. The isolates of the Boregine and Borlu varieties showed the highest EAI with 29.3 and 28.3 m2 g−1, respectively, while the lowest index was recorded in the isolate obtained from the Sonate variety (24.6 m2 g−1). Like solubility, these indices also increased at both extremes of pH evaluated; both properties were minimal in the isoelectric pH range (4.0 to 5.0).

Note: Influence of pH on the Extraction Yield and Functional Properties of Macadamia (Macadamia Integrofolia) Protein Isolates

2004 ◽  
Vol 10 (4) ◽  
pp. 263-267 ◽  
Author(s):  
P. S. Bora ◽  
D. Ribeiro
Keyword(s):  
Functional Properties ◽  
Extraction Yield ◽  
Emulsifying Properties ◽  
Alkaline Ph ◽  
Protein Isolates ◽  
Ph Values ◽  
Macadamia Nut ◽  
Isoelectric Ph ◽  
Ph Range ◽  
Influence Of Ph

Three protein isolates from de-fatted macadamia nut kernel flour were prepared by extraction at acidic (pH2.0), neutral (pH7.2 with 0.2M phosphate buffer containing 0.5MNaCl) and alkaline (pH12.0) conditions. Extraction at pH2.0 solubilised nearly 52.0% of the proteins present in defatted macadamia flour, while extraction with buffer (pH7.2) and alkaline pH (12.0) solubilised about 83.0% of proteins. The yield of isoelectrically precipitated protein from acidic extract (pH2.0, isolate A) was about 65.2% and from neutral (isolate B) and alkaline extracts (isolate C) was slightly over 83.0% which accounted for 33.7, 69.1 and 69.4% of the proteins present in defatted flour. The protein content of the isolates was 80.1, 92.1 and 92.0% in A, B and C isolates respectively. The functional properties of these isolates were significantly different. Isolate A presented better solubility at pH below isoelectric pH, isolate C at pH above isoelectric pH and isolate B intermediate solubility at the pH range studied. Isolate B showed best water and oil absorption capacities followed by isolate C and least by isolate A. For each isolate, the emulsifying properties were also significantly different at different pH values.

scholarly journals Characterizing the Structural and Functional Properties of Soybean Protein Extracted from Full-Fat Soybean Flakes after Low-Temperature Dry Extrusion

Molecules ◽  
2018 ◽  
Vol 23 (12) ◽  
pp. 3265 ◽  
Author(s):  
Wenjun Ma ◽  
Fengying Xie ◽  
Shuang Zhang ◽  
Huan Wang ◽  
Miao Hu ◽  
...  
Keyword(s):  
Functional Properties ◽  
Soy Protein ◽  
Activity Index ◽  
Soybean Protein ◽  
Stability Index ◽  
Extrusion Temperature ◽  
Emulsifying Activity ◽  
Protein Isolates ◽  
Soy Protein Isolates ◽  
Structural And Functional Properties

The soy protein isolates (SPI) extracted from different extruded full-fat soybean flakes (FFSF), and their conformational and functional properties were characterized. Overall, the free thiol (SH) content of SPI increased when the extrusion temperature was below 80 °C and decreased at higher temperatures. Soy glycinin (11S) showed higher stability than β-conglycinin (7S) during extrusion. Results also indicated that the increase in some hydrophobic groups was due to the movement of hydrophobic groups from the interior to the surface of the SPI molecules at extrusion temperatures from 60 to 80 °C. However, the aggregation of SPI molecules occurred at extrusion temperatures of 90 and 100 °C, with decreasing levels of hydrophobic groups. The extrusion temperature negatively affected the emulsifying activity index (EAI); on the other side, it positively affected the emulsifying stability index (ESI), compared to unextruded SPI.

Structural and Functional Changes in Ultrasonicated Oyster Protein Isolates

2019 ◽  
Vol 15 (3-4) ◽  
Author(s):  
Cuiping Yu ◽  
Fan Wu ◽  
Yue Cha ◽  
Henan Zou ◽  
Yingnan Guo ◽  
...  
Keyword(s):  
Particle Size ◽  
Functional Properties ◽  
Activity Index ◽  
Protein Solubility ◽  
Stability Index ◽  
Protein Isolates ◽  
Complex Needs ◽  
Functional Changes ◽  
Structural And Functional Properties ◽  
Water Holding

AbstractStructural and functional changes in ultrasonicated oyster protein isolates (OPI) were investigated. Ultrasound treatments were carried out with probe (20 kHz) at 200, 400 and 600 W for 15 and 30 min. The results showed that functional properties of OPI significantly improved after sonication. Absolute zeta potential and protein solubility increased by 18.40 mV and 82.5 % at 600 W for 15 min. Oil holding capacity, emulsifying activity index, emulsion stability index, foaming ability and foaming stability increased by 300 %, 15.23 m2/g, 9.24 min, 23.9 % and 14.8 % at 600 W for 30 min. However, ultrasound treatment significantly (P < 0.05) decreased particle size and water holding capacity. The conformation of OPI became stretched and unfolded after sonication. Functional improvements resulted from stretched and unfolded conformation and reduction of particle size. Controlled condition of ultrasound can produce OPI with distinct structural and functional properties, which could meet the complex needs of manufactured food products in food industry, but further study is needed to understand the specific mechanism.

scholarly journals Physicochemical properties of soy protein isolates-acacia gum conjugates

2011 ◽  
Vol 29 (No. 2) ◽  
pp. 129-136 ◽  
Author(s):  
L. Mu ◽  
H. Zhao ◽  
M. Zhao ◽  
Ch. Cui ◽  
L. Liu
Keyword(s):  
Physicochemical Properties ◽  
Soy Protein ◽  
Time Course ◽  
Activity Index ◽  
Stability Index ◽  
Heating Method ◽  
Protein Isolates ◽  
Soy Protein Isolates ◽  
Acacia Gum ◽  
Graft Reaction

Protein-polysaccharide conjugates were generally prepared by dry-heating. However, it was time-consuming and the sample gained was inhomogeneous. A faster way of preparing protein-polysaccharide conjugates is needed. Accordingly, soy protein isolates (SPI)-Acacia gum (GA) conjugates prepared by the wet-heating method were studied in the present work. Physicochemical properties of SPI-GA conjugates were also determined. The results showed that the wet-heating method could improve the rate of the graft reaction of protein and polysaccharide. The solubility of SPI-GA conjugates was significantly (P &lt; 0.05) higher than that of unreacted SPI-GA mixtures and SPI at the same pH values. The emulsion activity index (EAI) of the grafted SPI increased remarkably. Moreover, a significant (P &lt; 0.05) improvement on the emulsifying stability index (ESI) was observed and emulsions with a smaller droplet size were obtained. No visible flocculation during extended storage (30 days) was observed. The time course of the development of the graft reaction of SPI with GA was also shown by SDS-PAGE.

Functional Properties of Ultrasonically Treated Wheat Gluten

2012 ◽  
Vol 463-464 ◽  
pp. 855-860
Author(s):  
Lei Zhao ◽  
Guo Qin Liu ◽  
Bing Li ◽  
Lin Li
Keyword(s):  
Molecular Weight ◽  
Functional Properties ◽  
Treatment Time ◽  
Emulsion Stability ◽  
Foam Stability ◽  
Wheat Gluten ◽  
Stability Index ◽  
Gel Permeation Chromatography ◽  
Ultrasonic Power ◽  
Emulsifying Capacity

Ultrasonic was employed to improve the functional properties of wheat gluten. The results showed their solubility, emulsifying capacity and emulsion stability index of ultrasonically treated wheat gluten gradually increased as the ultrasonic power and treatment time increase, when ultrasonic treated for 20min at 240W, the solubility, emulsifying capacity and emulsion stability reached the maximum, then the solubility slightly decreased when the ultrasonic power exceeded 240W. However, the forming capacity and foam stability of ultrasonically treated gluten samples gradually increased with ultrasonic power and treatment time increasing. Gel Permeation Chromatography (GPC) observations revealed that the molecular weight of gluten decreased as the ultrasonic power increased, implying that the molecular of wheat gluten was broken by ultrasonic. Lower molecular weight of wheat gluten showed better functional properties.

scholarly journals Comparative Study of the Structural and Functional Properties of Membrane-Isolated and Isoelectric pH Precipitated Green Lentil Seed Protein Isolates

Membranes ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 694
Author(s):  
Etinosa C. Osemwota ◽  
Adeola M. Alashi ◽  
Rotimi E. Aluko
Keyword(s):  
Functional Properties ◽  
Food Systems ◽  
Protein Extraction ◽  
Seed Proteins ◽  
Protein Digestibility ◽  
Protein Isolates ◽  
Structural And Functional Properties ◽  
Lentil Flour ◽  
Droplet Sizes ◽  
Isoelectric Ph

The demand for isolated seed proteins continues to increase but functionality in food systems can be greatly dependent on the extraction method. In this work, we report the physicochemical and functional properties of lentil seed proteins isolated using various protocols. Lentil flour was defatted followed by protein extraction using isoelectric pH precipitation (ISO) as well as NaOH (MEM_NaOH) and NaCl (MEM_NaCl) extractions coupled with membrane ultrafiltration. The MEM_NaCl had significantly (p < 0.05) higher protein content (90.28%) than the ISO (86.13%) and MEM_NaOH (82.55%). At pH 3–5, the ISO was less soluble (2.26–11.84%) when compared to the MEM_NaOH (25.74–27.22%) and MEM_NaCl (27.78–40.98%). However, the ISO had higher yield and protein digestibility (48.45% and 89.82%) than MEM_NaOH (35.05% and 77.87%) and MEM_NaCl (13.35% and 77.61%), respectively. Near-UV circular dichroism spectra showed that the MEM_NaOH had loose tertiary conformation at pH 3, 5, 7 and 9 while ISO and MEM_NaCl had more compact structures at pH 7 and 9. The three protein isolates formed better emulsions (lower oil droplet sizes) at pH 7 and 9 when compared to pH 3 and 5. In contrast, foaming capacity was better at pH 5 than pH 3, 7, and 9.

scholarly journals Modification of wheat gluten for improvement of binding capacity with keratin in hair

2018 ◽  
Vol 5 (2) ◽  
pp. 171216 ◽  
Author(s):  
Shukun Wang ◽  
Danyang Meng ◽  
Sisi Wang ◽  
Zhong Zhang ◽  
Ruijin Yang ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Disulfide Bonds ◽  
Foam Stability ◽  
Activity Index ◽  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Stability Index ◽  
Nitrogen Solubility Index ◽  
Degree Of Hydrolysis ◽  
Wheat Protein

In this study, enzymatic hydrolysis and cationization with epoxypropyldodecyldimethylammonium chloride of wheat protein, an economic protein complex containing great amount of disulfide bonds, were conducted to improve properties such as solubility and disassociation behaviour for recovery of damaged hair when used in shampoo. The optimal conditions for enzymatic hydrolysis were pH 8.2, 55°C with Alcalase for 60 min. After the selected hydrolysis, the degree of hydrolysis, nitrogen solubility index, foaming capacity index, foam stability index, emulsifying activity index and emulsion stability index of hydrolysate with 58.71% of short-chain peptides (less than 1000 Da) were 8.81%, 39.07%, 225%, 56.67%, 9.62 m 2  g −1 and 49.08, respectively. The cationization was followed to raise the isoelectric point of wheat protein hydrolysate from 7.0 to 10.0, which could facilitate the quaternized protein hydrolysate to adhere to the surface of hair at the range of pH 5–6 of hair care products to form more disulfide bonds. The results show that a shampoo with quaternized wheat proteins hydrolysate possesses excellent properties in recovering damaged hair, making the surface of hair smooth and compact.

scholarly journals Chemical and Functional Characterization of Sarcoplasmic Proteins from Giant Squid (Dosidicus gigas) Mantle

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Rosa Linda Lopez-Enriquez ◽  
Victor Manuel Ocano-Higuera ◽  
Wilfrido Torres-Arreola ◽  
Josafat Marina Ezquerra-Brauer ◽  
Enrique Marquez-Rios
Keyword(s):  
Functional Properties ◽  
Activity Index ◽  
Functional Characterization ◽  
Stability Index ◽  
Dosidicus Gigas ◽  
Sarcoplasmic Proteins ◽  
Giant Squid ◽  
Jumbo Squid ◽  
Nacl Concentration

Modification of pH and NaCl concentration changed the physicochemical properties of sarcoplasmic proteins (SP) from jumbo squid mantle and consequently their functional properties. Better results of emulsifying activity index (EAI) and foam capacity (FC) were exhibited at pH 11 in NaCl absence due to higher solubility. But better emulsifying stability index (ESI) was obtained at pH 11 in 0.5 M NaCl, while, foaming stability (FS) was better at pH near to isoelectric point (pI). These results suggest that SP from jumbo squid may be a promising ingredient, whose functional properties can be manipulated by changing pH and NaCl concentration.

scholarly journals The Functional Properties of Buffalo skin Gelatin Extracted Using Crude Acid Protease from Cow’s Abomasum

2019 ◽  
Vol 6 (2) ◽  
Author(s):  
Sri Mulyani ◽  
Yudi Pranoto ◽  
Francis M.C. Sigit Setyabudi ◽  
Anang Muhammad Legowo ◽  
Umar - Santoso
Keyword(s):  
Functional Properties ◽  
Emulsion Stability ◽  
Activity Index ◽  
Stability Index ◽  
Acid Protease ◽  
Concentration Variation ◽  
Hydrolysis Temperature ◽  
Emulsion Stability Index ◽  
Swamp Buffalo

The study was investigated the functional properties of buffalo skin gelatine. Gelatine was extracted from swamp buffalo skin using crude acid protease from cow’s abomasum (CAPC) in concentration variation 0; 2.5; 5; and 7.5 U/mg. The temperature to hydrolysis included at 28 °C, 37°C and 40°C. The emulsion activity index (EAI), Emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS) were investigated. The interaction between CAPC concentration and hydrolysis temperature has a significant effect (P <0.05) on the emulsion activity index (EAI), emulsion stability index (ESI), foaming expansion (FE) and foaming stability (FS). The highest EAI was obtained in CAPC concentration of 5 U /mg, hydrolysis temperature of 40°C, which was 12.04 m2/g. The higher concentration of CAPC decreased the ESI. The hydrolysis temperature of 40°C produces higher FE than 28°C and 40°C. The highest FE is obtained at CAPC 5U/mg, 37°C hydrolysis temperature, which is 102.93%. The FS values range from 44.91-55.00%. This value is higher than commercial gelatin (bovine skin gelatin) which is 34.90%. The conclusion of this study is that buffalo skin gelatin with the best functional properties was obtained using CAPC 5 U/mg, the hydrolysis temperature of 40°C.

Sign in / Sign up

Export Citation Format

Share Document