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- Hermansson, Ann-Marie
(author)
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Ingen mat utan vatten.
- 1985
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In: Livsmedelsteknik. ; 27:8-9, s. 318, 320-321
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Journal article (other academic/artistic)
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5. |
- Hermansson, Ann-Marie
(author)
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Kolloidal struktur.
- 1988
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In: Livsmedelsteknik. ; 30:4, s. 144-146
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Journal article (other academic/artistic)
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6. |
- Hermansson, Ann-Marie
(author)
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Microstructure of chocolate.
- 1988
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In: Bioscience and Technology. ; 26:8, s. 533-536
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Journal article (peer-reviewed)
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7. |
- Hermansson, Ann-Marie
(author)
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Rheological and microstructural evidence for transient states during gelation of kappa-carrageenan in the presence of potassium
- 1989
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In: Carbohydrate Polymers. - 0144-8617 .- 1879-1344. ; 10:3, s. 163-181
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Journal article (peer-reviewed)abstract
- Kappa-carrageenan gelation was studied by a combination of electron microscopy and dynamic viscoelastic measurements. There was an initial maximum in the storage modulus during cooling and gel formation of 1% kappa-carrageenan in the presence of potassium. The structure of the transient state was found to consist of a fine network structure, where the junction zones were believed to be double helices. The structure had the characteristics of a true gel but was unstable. When the temperature was lowered aggregation took place and the fine network structure was partly broken down. Ordered superstrands formed which aligned themselves in parallel or were densely packed together. The degree of aggregation depended on the potassium ion concentration. In the weakest gel formed in 0·01 m KCl, the superstrands did not form a network but were rather dispersed in the fine network structure. In 0·1 and 0·2 m KCl the superstrands formed a three-dimensional network, where aligned superstrands formed the junction zones and branching occurred when superstrands deviated from each other and aligned with new superstrands. In 0·1 m KCl the supermolecular network dominated but in 0·2 m KCl a mixed gel was formed of the fine network and the coarse supermolecular network. The mixed gel gave rise to the firmest gel. © 1989.
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- Hermansson, Ann-Marie
(author)
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Soy protein gelation
- 1986
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In: Journal of the American Oil Chemists Society. - 0003-021X .- 1558-9331. ; 63:5, s. 658-666
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Journal article (peer-reviewed)abstract
- Heat-induced protein gels are of importance for the structure and properties of many food products. Gel formation is a complex process which often involves several reactions such as denaturation, dissociation-association, and aggregation. The kinetics of the reactions involved will determine the type of structure formed. Protein gels can be divided into two types: gels formed by random aggregation and gels formed by association of molecules into strands in a more ordered way. The two soy proteins glycinin and conglycinin both have the ability to form ordered structures consisting of strands 10-15 nm thick. The glycinin gel strands formed in distilled water are regular, and cross sections of strands showed a hollow cylindrical structure. In the presence of sodium chloride, glycinin forms an aggregated gel structure at 85 C, but at 95 C a regular structure similar to that found in distilled water was formed. The aggregated structure was interpreted as a transient state similar to the soluble aggregate formed on heating dilute solutions prior to dissociation into subunits. Conglycinin gels are more irregular and more cross-linked than gels of glycinin. Also, the strands of conglycinin showed a complex mode of aggregation possibly in the form of double spirals. The addition of salt does not affect the microstructure of conglycinin gels as dramatically as in the case of glycinin gels. Commercially produced soy protein isolates may behave quite differently from native soy proteins, due to processing conditions causing denaturation and various states of aggregation. © 1986 American Oil Chemists' Society.
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- Hermansson, Ann-Marie, et al.
(author)
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The Structure of gluten gels.
- 1986
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In: Food Microstructure. ; 5, s. 233-239
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Journal article (peer-reviewed)
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