Colloid science of mixed ingredients

Dickinson, Eric

doi:10.1039/b605670a

Cited by 166 publications

(115 citation statements)

References 98 publications

(141 reference statements)

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“…After this period in which the focus was on liquid foams, and on more or less pure protein systems, the attention seems to have shifted to more complex systems. More researchers are involved in the study of binary solutions of proteins and surfactants [75,76,77 • ,78], or proteins and polysaccharides [79][80][81][82]. The first great value of this work is of course providing new horizons to aim for.…”

Section: Novel Directions In Protein Foam Researchmentioning

confidence: 98%

New views on foams from protein solutions

Wierenga

Gruppen

2010

Current Opinion in Colloid & Interface Science

165

108

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Section: Novel Directions In Protein Foam Researchmentioning

confidence: 98%

New views on foams from protein solutions

Wierenga

Gruppen

2010

Current Opinion in Colloid & Interface Science

165

108

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“…Protein-polysaccharide complexes are also important in industrial applications such as micro-and nano-encapsulation processes 1 -4 , the design of multi-layers structures, the formation and the stabilization of food emulsions 6 , the formation of new food gels 12 and the recovery of proteins from industrial by-products 8 -10 . Supra-molecular structures formed by non-covalent interactions between protein and polysaccharides (complexes, aggregated complexes and coacervates) have represented a very active research area in the last 3 -4 years.…”

Section: Introductionmentioning

confidence: 99%

Improvement of enzyme stability via non-covalent complex formation with dextran against temperature and storage lifetime

Altıkatoğlu

Kuzu

2010

Polish Journal of Chemical Technology

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The optimal methodology to prepare the novel modified enzyme, polymer-enzyme complex, was developed to give a high catalytic activity in aqueous solution. The non-covalent complexes of two different enzymes (horseradish peroxidase and glucose oxidase) were prepared with various molar ratios (n D /n E 0,05; 0,1; 1; 5; 10; 15; 20) by using 75kDa dextran. The thermal stabilities of the obtained complexes were evaluated with the activities determined at different temperatures (25, 30,35, 40, 50, 60, 70, 80 o C) applying 60 minutes incubation time for pH 7. The complexes with the molar ratio n D /n HRP : 10 and n D /n GOD : 5 showed the highest thermal stability. Its activity was very high (ca. 1,5-fold higher activity than pure enzyme for HRP-dextran complexes) and almost the same between applying one hour incubation time and without incubation, and could also be measured at high temperatures (70, 80 °C). We finally succeeded in preparing dextran-enzyme complexes which showed higher activity than pure enzyme in aqueos solution at all temperatures for pH 7. In addition, the mentioned complexes at pH 7 had very long storage lifetime compared to purified enzyme at +4 o C; which is considered as a good feature for the usage in practice.

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“…Usually, the system is considered stable when the energy barrier between the particles is larger than the thermal fluctuations. 6 Such stability may refer, for instance, to stability against flocculation in emulsions, phase separation in mixed biopolymer systems, gelation in single biopolymer solutions or stabilization of biopolymer matrices below their glass transition temperature. As foods are metastable materials (out of equilibrium) they are susceptible to structural re-organization through various relaxation mechanisms.…”

mentioning

confidence: 99%