Rheology of hydroxyethylated starch aqueous systems. Analysis of gel formation

Jáuregui, Belén Cadavid; Muñoz, Manuel López; Santamarı́a, Anton

doi:10.1016/0141-8130(95)93518-3

Cited by 19 publications

(13 citation statements)

References 15 publications

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“…The obtained results are a clear indication that the hydrogen bonding between the big molecules is very weak and that no association occurs. This behavior is known in modified starches in which the presence of hydroxyethyl groups disrupts the hydrogen bonding and result in fluid-like behavior [31,32]. The weakness of hydrogen bonding cannot be explained in our case by the presence of chemical groups, but with the architecture of the polysaccharides.…”

Section: Retrogradation At 4°c Followed By Dscmentioning

confidence: 65%

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Physical properties and structure of enzymatically synthesized amylopectin analogs

et al. 2013

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The mechanism of the enzymatic polymerization of amylopectin analogs with phosphorylase b and glycogen branching enzyme is very intriguing. Recently, size exclusion chromatography with multi‐detection of enzymatically synthesized amylopectin analogs in combination with MALDI‐ToF MS analysis of enzymatically debranched analogs was used to solve parts of the molecular mechanism of analog's enzymatic polymerization. In this work dynamic light scattering (DLS), AFM and cryo‐TEM, respectively were used to determine structural characteristics of the same analogs. The results were compared with SEC analyses. The presented analyses in this work fully agreed with the recently made observations and confirmed the changes in the architecture of the synthesized polysaccharide due to the change of enzymatic polymerization mechanism. Furthermore, we showed that the synthetic amylopectin analogs are stable to retrogradation at 4°C if the main side chain length is no longer than 12 glucose units and that they have mostly fluid‐like behavior in the form of 20% suspensions.

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Section: Retrogradation At 4°c Followed By Dscmentioning

confidence: 65%

“…5. The viscosities were extremely low, especially when compared to other polysaccharide solutions with that concentration [32,33].…”

Section: Retrogradation At 4°c Followed By Dscmentioning

confidence: 81%

Physical properties and structure of enzymatically synthesized amylopectin analogs

et al. 2013

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“…The characteristic decrease in the dynamic viscosity with increasing oscillatory frequency indicated a shear thinning mechanism in response to stress that was also demonstrated by continuous shear analysis. Interestingly (and uncommonly), PAA–Tetronic gels displayed a significant increase in formulation loss tangent with increasing frequency, which is a characteristic of viscoelastic solids 38. This observed frequency dependency of the systems under examination may thus be may be related to molecular interactions (primarily hydrogen bond formation, van der Waals, and electrostatic interactions) between the polymer chains of the PAA and the block copolymer, as identified using FTIR.…”

Section: Discussionmentioning

confidence: 89%

Moisture‐activated rheological structuring of nonaqueous poloxamine–poly(acrylic acid) systems designed as novel biomedical implants

Jones

Muldoon

Woolfson

et al. 2010

Journal of Pharmaceutical Sciences

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“…This method was successfully applied for many liquids in the case when the viscosity measurements were conducted in a relatively narrow range of temperatures (Hayakawa et al, 1991;Bourret et al, 1994;Lopez da Silva et al, 1994;Jauregui et al, 1995;de Paula & Rodrigues, 1995;Kar & Arslan, 1999;de Vasconcelos et al, 2000;Desbrieres, 2002;Durand, 2007;Knoben et al, 2007). In our case, viscosity measurements were made in a broad range of temperatures.…”

Section: Resultsmentioning

confidence: 96%

A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids

Monkos¹

2011

Current Topics in Biophysics

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The paper presents the results of viscosity determinations on aqueous solutions of hen egg-white lysozyme at a wide range of concentrations and at temperatures ranging from 5 o C to 55 o C. On the basis of these measurements and different models of viscosity for glass-forming liquids, the activation energy of viscous flow for solutions and the studied protein, at different temperatures, was calculated. The analysis of the results obtained shows that the activation energy monotonically decreases with increasing temperature both for solutions and the studied protein. The numerical values of the activation energy for lysozyme, calculated on the basis of discussed models, are very similar in the range of temperatures from 5 o C to 35 o C.

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Rheology of hydroxyethylated starch aqueous systems. Analysis of gel formation

Cited by 19 publications

References 15 publications

Physical properties and structure of enzymatically synthesized amylopectin analogs

Physical properties and structure of enzymatically synthesized amylopectin analogs

Moisture‐activated rheological structuring of nonaqueous poloxamine–poly(acrylic acid) systems designed as novel biomedical implants

A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids

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