Association-dissociation and denaturation-renaturation of high-molecular-weight protein: Carmin from safflower seed (Carthamus tinctorius L.) in alkaline solution

Rajendran, S.; Prakash, V.

doi:10.1007/bf01025578

Cited by 7 publications

(2 citation statements)

References 17 publications

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“…Table 1). On the other hand, because of the oligomeric structure of API proteins, it is possible that high alkaline environments (pH 12) induce their dissociation, thus increasing low molecular weight species (Konishi, Fumita, Ikeda, Okuno, & Fuwa, 1985;Marcone, 1999;Rajendran & Prakash, 1988). This process causes a drop of the viscosity, consequently preventing the electrospinning process (cf.…”

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confidence: 99%

Development of novel ultrathin structures based in amaranth (Amaranthus hypochondriacus) protein isolate through electrospinning

et al. 2013

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Amaranth protein isolate (API) ultrathin structures have been developed using the electrospinning technique. The effects of pH, type of solvent and surfactant addition on the spinnability, morphology and molecular organization of the obtained structures have been studied. Regarding the effect of pH on API electrospinning, capsule morphologies were only obtained at extreme pH values (i.e. pH 2 and pH 12), which allowed the solubilisation of the proteins, and the process was favoured when the solutions were previously heated to induce protein denaturation. Fibre-like morphologies were only obtained when the solvent used for electrospinning was hexafluoro-2-propanol, as this organic solvent promotes the formation of random coil structures and, thus, an increase in the biopolymer entanglements. Capsule morphologies were obtained from the API-containing formic acid solutions and this solvent was better for electrospraying than the acetic acid, probably due to the higher viscosity and lower surface tension of the solutions thereof. Addition of 20 wt.-% of Tween 80 considerably improved the formation of capsule-like structures from the formic acid solution, as this surfactant contributed to the formation of alpha helical structures. Similar results were obtained when combining the surfactant with the reducing agent 2-mercaptoethanol. However, denaturation of the protein structure was not sufficient for fibre formation through electrospinning, as the solution properties play a fundamental role in determining the morphology of the electrospun structures.

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confidence: 99%

Development of novel ultrathin structures based in amaranth (Amaranthus hypochondriacus) protein isolate through electrospinning

et al. 2013

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“…Protein solutions of 5.1 X 10-6 M were used. The final data were analyzed by established methods (Gutfreund, 1972;Hiromi, 1979;Rajendran & Prakash, 1988). The slow kinetics was followed in a Shimadzu U V-150-02 double-beam spectrophotometer at 600 nm and 27 ± 1 °C using a protein concentration of 3.7 X 10-7 M.…”

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confidence: 99%

Kinetics and thermodynamics of the mechanism of interaction of sodium phytate with .alpha.-globulin

Rajendran¹,

Prakash²

1993

Biochemistry

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The precipitation mechanism of alpha-globulin in the presence of myo-inositol hexaphosphate (sodium phytate) was studied in detail. The maximum interaction was found at pH 2.3 where the protein was in a dissociated state having an 8.3S aggregate and a 1.5S monomer. This interaction was predominantly dependent upon the sodium phytate to protein ratio. Velocity sedimentation studies indicated polymer formation due to preferential progressive binding of ligand to polymer, whose size and concentration increased with an increase in sodium phytate concentration. The polymer formation was shown to be ligand mediated and exists independently in solution along with the monomer. The binding isotherm by equilibrium dialysis confirmed differential binding of sodium phytate to the polymer and the monomer as indicated by two sets of binding sites, one having 7 +/- 2 sites of a K value 1.3 x 10(-4) mol-1 and the other having 56 +/- 3 sites with a K value of 2.8 x 10(-3) mol-1. Binding resulted in perturbation of chromophores of protein due to charge effects. The kinetics of the polymer formation was shown to be a pseudo-first-order reaction having two steps. The initial fast reaction involving conformational changes has rate constants of k1 = 52.4 x 10(-3) s-1 and k' = 67.5 x 10(-3) s-1, followed by a slow reaction step of rate constants k2 = 4.3 x 10(-3) s-1 and k'2 = 2.9 x 10(-3) s-1 at sodium phytate concentrations of 1 x 10(-4) M and 5 x 10(-4) M, respectively.

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Safflower Seed Meal: Progress Towards Obtaining New Protein

Barbhai,

Puranik,

Waghmare

et al. 2024

Oilseed Meal as a Sustainable Contributor to Plant-Based Protein

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Association-dissociation and denaturation-renaturation of high-molecular-weight protein: Carmin from safflower seed (Carthamus tinctorius L.) in alkaline solution

Cited by 7 publications

References 17 publications

Development of novel ultrathin structures based in amaranth (Amaranthus hypochondriacus) protein isolate through electrospinning

Development of novel ultrathin structures based in amaranth (Amaranthus hypochondriacus) protein isolate through electrospinning

Kinetics and thermodynamics of the mechanism of interaction of sodium phytate with .alpha.-globulin

Safflower Seed Meal: Progress Towards Obtaining New Protein

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