Fine-stranded gels

For gels of finer dimensions, such as transparent fine-stranded gels, the capillary pressures are too high for water to be pressed out. Such gels can also release water, but this is mostly due to syneresis, which is related to aggregation of the network beyond the gel point and subsequent shrinkage. The water will be squeezed out because of the decrease in volume of the gel network and there will simply be less space available. 

Type of protein. For example, fine-stranded gels are far more readily formed from myosin (an elongated molecule) or x-lactalbumin (a small molecule that does not form —S—S— bridges) than from (3-lactoglobulin or soya protein. 

Lefevre, T., Subirade, M. (2000). Molecular differences in the formation and structure of fine-stranded and particulate p-lactoglobulin gels. Biopolymers, 54, 578-586. 

Fine-stranded at neutral pH gels are formed at or close to pH 7.0 and contain little, if any, added salts,... 

Langton, M., and Hermansson, A.M. (1992). Fine-stranded and particulate gels of beta-lactoglobulin and whey protein at varying pH. Food Hydrocolloids 5, 523-539. 

Fine-stranded. These are clear gels, consisting of relatively fine strands, that are branched to form a network. Strand thickness generally is between 20 and 50 nm, i.e., clearly larger than molecular size (4-8 nm). These gels typically form at a pH far away from the isoelectric point (pi) at low ionic strength. 

The number and type of bonds between the basic building imits, i.e., aggregates, within a strand the smaller the number and the weaker these bonds, the more susceptible the strand is to deformation. In fine gel structures, there are probably fewer intra- and interaggregate attractions/ bonds than in coarser gels. Hence, products with finer gel structures may be considered to exhibit less elastic, and more viscous, behavior than those with coarser networks. 

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