Peptization of Soybean Proteins Extraction of Nitrogenous Constituents from Oil-Bases with and Without Added Slats

Smith, A. K.; Circle, Sidney J.

doi:10.1021/ie50348a014

Cited by 84 publications

(35 citation statements)

References 4 publications

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“…TSP levels varied from 1.36 mg/mL (for pH 4.0 and 30 mmol/L NaCl) to 8.13 mg/mL (for pH 7.6 and 100 mmol/L NaCl), as pH and ionic strength were changed. These results are very similar to the ones found by Smith and Circle [25], who reported that the concentration of soybean seed protein extract at pH 7.6 was 4.3 times that extracted at pH 4.0 using a solution of 100 mmol/L NaCl.…”

Section: Total Soluble Proteinsupporting

confidence: 91%

Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase

Robić

Farinas

Rech

et al. 2009

Appl Biochem Biotechnol

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Soybean is one of the plant species with potential to be used as seed-based bioreactor. As part of the downstream processing (DSP) of this technology, extraction is a key step, since it defines the composition of the solution from which the recombinant product will be purified. In the present work, the characteristics of soybean seeds used as a bioreactor were evaluated from a process engineering standpoint through analysis of the influence of pH and ionic strength on the extraction of recombinant beta-glucuronidase (rGUS). Concentrations of recombinant protein and native soybean compounds were analyzed and compared with similar data from extraction studies using transgenic corn seeds as bioreactor. Efficient rGUS extraction was obtained at pH of around 5.5 with no addition of salt. Soybean seed extracts had lower levels of co-extracted native compounds, than corn seed extracts, and should be considered as a potential plant bioreactor in terms of DSP.

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Section: Total Soluble Proteinsupporting

confidence: 91%

Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase

Robić

Farinas

Rech

et al. 2009

Appl Biochem Biotechnol

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“…The solubility evolution of protein during BMEA (Figure 1) was modeled as a sigmoidal curve (R 2 ) 0.99 at 10 and 27°C). These results are in accordance with data in the literature (Wolf and Cowan, 1971;Smith and Circle, 1938;Bazinet et al, 1998a;1999).…”

Section: Resultssupporting

confidence: 93%

Effect of Temperature on the Separation of Soybean 11 S and 7 S Protein Fractions during Bipolar Membrane Electroacidification

et al. 2000

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The purpose of this study was to evaluate the effect of temperature (10 and 27 degrees C) on the efficiency of bipolar membrane electroacidification (BMEA) to fractionate soybean proteins. BMEA is a technology derived from electrodialysis, based on the isoelectric precipitation of proteins. It appears that temperature has a significant effect on the selective precipitation of the soybean protein fractions, mainly 11 S and 7 S, during BMEA. At 27 degrees C, the precipitation profile of the four protein fractions is situated in a pH range from 6.6 to 4.4, with no possibility of separating any of theses fractions. However, at 10 degrees C, the 11 S globulin precipitates at a higher pH than at 27 degrees C, pH 6.7 vs 5.9, allowing the fractionation of 11 S from the other fractions. Using electroacidification it is possible to obtain a precipitate solution enriched in the 11 S fraction (71.8% of 11 S and 10.8% of 7 S) and a supernatant solution enriched in the 7 S fraction (46.6% of 7 S and 4.6% of 11S).

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“…The solubility behavior of soy protein as plotted in Fig. 2 corresponds to characteristic extraction curves of defatted soybean meal (Smith and Circle, 1938). Dispersions of defatted soybean flour in water at pH 11.0 resulted in very high solubility of proteins as compared to a pronounced minimum solubility at pH 4.5, the isoelectric region.…”

Section: Resultsmentioning

confidence: 98%

Twin‐Screw Extrusion Texturization of Acid and Alkali Denatured Soy Proteins

Dahl

Villota

1991

Journal of Food Science

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Effect of pH on functional characteristics of soy protein was investigated by modifying soy flour through acid (HCI) or alkali (NaOH) addition. Acid-and alkali-treated proteins were evaluated and texturized by twin-screw extrusion. Products were analyzed by rheological, functional, and ultrastructural methods. Acid-modified texturized protein had little expansion, increased peak force, increased work of shearing, and a nonoriented fiber arrangement. Slightly alkaline extrudates had increased rehydration but poorer texture. Stronger alkaline treatment resulted in denser products with high peak force measurements, which disintegrated when extrudates were rehydrated. The physicochemical state of soy protein, particularly conformation and protein-water interactions as affected by pH, may influence expansion of textured products and development of plexilamellar structure.

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Peptization of Soybean Proteins Extraction of Nitrogenous Constituents from Oil-Bases with and Without Added Slats

Cited by 84 publications

References 4 publications

Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase

Transgenic Soybean Seed as Protein Expression System: Aqueous Extraction of Recombinant β-Glucuronidase

Effect of Temperature on the Separation of Soybean 11 S and 7 S Protein Fractions during Bipolar Membrane Electroacidification

Twin‐Screw Extrusion Texturization of Acid and Alkali Denatured Soy Proteins

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