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Reactivity and Interaction of Carrageenan

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Reactivity and Interaction of Carrageenan

Let us learn more about Carrageenan, which is the most popular food additive present in most dairy products that you use every day. This article will brief you on the reactivity of Carrageenan with proteins and interactions with many other gums.

Reactivity- With proteins

It is the most important property of many other properties of this food additive (carrageenan) that makes it different from certain hydrocolloids is its efficiency to respond to milk proteins. Its high reactivity with milk is because of solid electrostatic interaction among the estate sulphate group that is negatively charged in its molecule with high positive charges of the milk casein micelle.

Another interaction is via the links build between its ester sulphate groups with the carboxylic remains of different amino acids that form the protein. Its reactivity with proteins is based on many factors like its concentration, protein type, pH, temperature and protein’s isoelectric point. Its ability to compound with milk proteins blend with its properties like water gelling, making it a perfect ingredient for gelling and stabilizing milk products.

Interaction- With many other gums

Kappa form shows an uncommon synergism with LBG (locust bean gum) in watery gel systems. The interactions is noticeable by a significant increase in the strength of the gel, enhancement in binding capacity of water, transformation in texture of the gel from brittle to elastic and decrease in the level of syneresis.

The Iota form shows a synergism with many starches. A system that includes of starch and carrageenan shows a rapid growth in viscosity.

Thixotropy  

Carrageenan water gels show thixotropic rheological properties at low concentrations. These gels go through liquefaction by whipping and form gels when allowed to cool. This property is quite helpful to hang insoluble particles like spices used in salad sauces. Some water gels, made with kappa carrageenan don’t have thixotropy property at all.

 

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