Characteristics of Medicated and Unmedicated Microglobules Recovered from Complex Coacervates of Gelatin–Acacia

Newton, David W.; McMullen, J.N.; Becker, Charles H.

doi:10.1002/jps.2600660931

Cited by 20 publications

(7 citation statements)

References 10 publications

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“…To investigate their microstructural evolution upon pH transition, four images were chosen from their individual pH range for each MR and presented in Figs. 1e3. According to the mainly spherical-like objects shown in the three figures, it could be concluded that the observed were coacervates (Newton, McMullen, & Becker, 1977;Remuñán-López & Bodmeier, 1996). In addition, small water vacuoles were detected entrapped, which were recognized as an enthalpic contribution to the formation mechanism from the thermodynamics perspective.…”

Section: Resultsmentioning

confidence: 94%

The study of pH-dependent complexation between gelatin and gum arabic by morphology evolution and conformational transition

Zhang

et al. 2013

Food Hydrocolloids

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Section: Resultsmentioning

confidence: 94%

The study of pH-dependent complexation between gelatin and gum arabic by morphology evolution and conformational transition

Zhang

et al. 2013

Food Hydrocolloids

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“…drug particle or an oil droplet containing flavors) has been investigated extensively and commercialized [7]. Gelatin/gum arabic (GA) coacervate system was extensively used for microencapsulation [8][9][10]. On the other hand, complexation has been studied in the purification and recovery of the macromolecules (e.g.…”

Section: Introductionmentioning

confidence: 99%

Complex coacervation of silk fibroin and hyaluronic acid

Malay

Bayraktar

Batıgün

2007

International Journal of Biological Macromolecules

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This study aimed to investigate the pH-induced complexation of silk fibroin (SF) and hyaluronic acid (HA). SF-HA complex coacervation was investigated by monitoring turbidity of the SF-HA system under slow acidification. Gravimetric analysis was performed to determine the yield of complex coacervation and viscosity of the system was measured to study the formation of the complexes at different pH values. The influences of total biopolymer concentration and biopolymer weight ratio on complex coacervation were examined during the analyses. Formation of the complexes was evidenced by the minimum viscosity and the maximum turbidity observed in the system. SF-HA complexes were formed within the pH-window of 2.5-3.5 regardless of the total biopolymer concentration or biopolymer ratio. Complex coacervation of SF-HA showed a reversible behavior and coacervation could be handled even in excess amounts of the biopolymers, which pointed out a non-stoichiometric complexation.

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“…On the same image, the smaller white particles were visible with a diameter of ∼150 nm. Due to the round clear structure of these particles, they could be coacervates . However, in the case of BLG–ALG, at the same pH value, the black aggregates are larger (0.4–3 μm) but the coacervates are smaller than BSA–ALG (Figure b) This could be because of the low molecular weight of BLG than BSA .…”

Section: Results and Discussionmentioning

confidence: 96%

“…Due to the round clear structure of these particles, they could be coacervates. 45 However, in the case of BLG−ALG, at the same pH value, the black aggregates are larger (0.4−3 μm) but the coacervates are smaller than BSA−ALG (Figure 3 b) This could be because of the low molecular weight of BLG than BSA. 46 Considering our results at pH 4.2 for BSA−ALG and BLG−ALG, it could be used for further application such as encapsulation due to maximum coacervate production.…”

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 92%

Complex Coacervation of Milk Proteins with Sodium Alginate

Gorji

Waheed

Ludwig

et al. 2018

J. Agric. Food Chem.

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Beta-lactoglobulin (BLG) and bovine serum albumin (BSA) coacervate formation with sodium alginate (ALG) was investigated by turbidimetric analysis, zeta potential, particle size, viscosity, transmission electron microscopy (TEM) and isothermal titration calorimetric (ITC) measurements as a function of pH (1.0–7.0) and protein/alginate mixing ratio (1:1, 1.5:1, 2:1, 1:0, and 0:1 wt.). Critical pH values of phase transitions for BSA–ALG complexes (pHC, pHφ1, and pHφφ2) representing the formation of soluble and insoluble complexes of a protein–ALG mixture (2:1) at pH 4.8, 4.2, and 1.8, respectively. In the case of BLG–ALG, critical pH values (pHC, pHφ1, and pHφ2) were found to be 4.8, 4.2, and 1.6, respectively. The pHopt values, expressed by the highest optical density, were pH 2.8 for BSA–ALG and 2.4 for BLG–ALG. TEM and zeta-potential results showed that maximum coacervate formation occurred at pH 4.2 for both protein–polysaccharide solutions. The interaction between BLG–ALG and BSA–ALG was spontaneously exothermic at pH 4.2 according to ITC measurements. The findings of this study provide insights to a thorough understanding about the nature of interactions between milk proteins and ALG and formulate new applications for food, pharmaceutical, nutraceutical, and cosmetics applications.

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Characteristics of Medicated and Unmedicated Microglobules Recovered from Complex Coacervates of Gelatin–Acacia

Cited by 20 publications

References 10 publications

The study of pH-dependent complexation between gelatin and gum arabic by morphology evolution and conformational transition

The study of pH-dependent complexation between gelatin and gum arabic by morphology evolution and conformational transition

Complex coacervation of silk fibroin and hyaluronic acid

Complex Coacervation of Milk Proteins with Sodium Alginate

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