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Food Polymers
Food Polymers
Polymers can vary in complexity depending upon the number, the kinds, and the order (or
sequence) of the monomers in the macromolecule; the manner in which the monomers are linked
together (the chain topology) also influences the polymer properties.
Number of monomers: Polymers can contain as few as 50 or as many as 108 monomers.
Large proteins in your muscles contain about 2000 amino acids; large starch (amylopectin)
molecules contain 105 to 106 sugar monomers; individual DNA molecules in your cells contain
about 2x108 nucleotide bases and are about 4 cm (about 1.5 inches!) long.
Kinds of monomers: Synthetic plastics are simple polymers made by polymerizing a
single kind of monomer. Polyethylene is polymerized ethylene (CH2=CH2) while polystyrene
(the plastic in foam cups) is polymerized styrene. Most biopolymers are more complex, typically
made of different kinds of monomers: proteins are made of twenty different amino acids; DNA is
made of four different nucleotide bases. Starch and cellulose, however, are made entirely of
glucose monomers; they differ because of differences in the specific linkage that connects them.
Order or sequence of monomers in chain: The true complexity of biopolymers becomes
apparent when considering the possible order of monomers in the linear polymer. Although
polyethylene can only vary in terms of its size (number of monomers), a polymer made from two
or more different monomers can vary in terms of its sequence. Polymer sequence is most
important when describing proteins and, of course, the DNA which codes the sequence
information for the protein. Consider a small protein containing 100 amino acid monomers.
There are actually 20100 10130 possible proteins of this size if we consider all the possible ways
that the 20 amino acids can be ordered in this protein. (Consider the first monomer in the
sequence, there are 20 possible amino acids that can be at this position. There are also 20
possible amino acids for the second monomer and 20 possible for the third, and 20 possible for
the fourth, etc. There are thus 20x20x20x20…x20 = 20100 possible proteins containing 100
amino acids.) Despite this potential complexity, each protein is a unique sequence.
Topology of polymer chain: Polymers can be linear (most synthetic plastics) or they can
be branched (starches). The extent and degree of branching can vary enormously. Most
synthetic polymers are linear; however, a new class of synthetic polymers, dendrimers, has very
extensive branching structures. Proteins are linear polymers, as is DNA. Starches have variable
topology. Amylose is primarily linear with only a very few (less than 1%) branching points
while amylopectin is more heavily branched, containing about 4% branch points.
Properties of food polymers
The physical and chemical properties of polymers are the result of the chemical
properties of the monomers (polarity, acidity, chemical reactivity), the size of the polymer, the
specific topology of the polymer chain, and in the case of proteins and some other biopolymers,
the linear sequence of monomers.
Chemical properties. All food polymers are polar because they are made up of polar
monomers (sugars, amino acids) and thus interact strongly with water. They are thus either truly
water soluble or bind water tightly. Many food polymers are also acids and/or bases. Proteins
contain many acidic (carboxyl) and basic (amino) groups and are thus charged at the pH of food
(neutral or slightly acidic). The chemical reactivity of a polymer is solely due to the reactivity of
the groups in the monomers of which it is made.
Size. The size of a polymer has a great influence on its physical properties. Large water
soluble molecules can dramatically affect the viscosity of aqueous solutions. Only a small
quantity of cornstarch, for example, can turn a thin fluid liquid into a thick viscous gravy. The
larger the polymer, the greater is its ability to modulate the flow properties of a solution. This is
because larger (longer) polymers have large effective sizes in solution (large effective
hydrodynamic volumes).
Topology. The degree of branching in a polymer influences the ways in which the
polymer can interact with water and with itself. Branched polymers also have a smaller effective
hydrodynamic volume for their mass due to their being less extended; they thus have a smaller
effect on water viscosity.
Sequence. The sequence of a protein determines the way in which this polymer folds up
in aqueous solution. Proteins contain many different kinds of amino acids. Some of these
contain side chains that are non-polar (phenylalanine, leucine, etc.) and thus not water soluble.
The protein will thus adopt a conformation, a three-dimensional shape for the polymer chain, that
segregates these non-polar groups away from water. The protein is said to fold up into a specific
shape that is determined by the sequence of amino acids in the polymer. All of the biological,
and many of the food, functionalities of the protein are influenced by the protein conformation.
Common Food Polymers (Food Hydrocolloids)
Look for these names on the labels of foods that you buy (they will usually be at or near
the end of the list, indicating that they are added in very small quantities).
Protein:
Food polymers (also called hydrocolloids) have many important functional roles in foods.
These include:
Generate and maintain foam structure in bread dough. The foam-like structure of bread
is generated by the growth of CO2 gas bubbles formed by fermentation by yeast. The surfaces of
these bubbles are formed from wheat proteins called glutens that act as elastic films to entrap the
gas. Upon heating, the walls of the gas cells are stabilized by the formation of many
intermolecular interactions that solidify the material into a stable foam.
Modulate solution viscosity and texture. Long linear polar polymers bind water tightly
and impede its flow by forcing the water to move with the polymer. A good model for this is a
bowl of cooked pasta noodles in water. Quick set puddings and pie fillings are examples of the
extent to which polysaccharide polymers can modulate the texture of liquids.
Stabilize foams and emulsions. Polymers can bind to the air/water interface in foams or
the oil/water interface in emulsions and stabilize these interfaces. The polymers can do this
because they have many different groups, some of which can interact with the non-polar air or
oil phase and some of which can interact with the polar water phase. The polymers become
entangled and form a felt-like layer or film on the surface that is strong and elastic and thus
stable. Interfaces stabilized by polymers are thus more stable than those stabilized by small
molecules.
Form elastic gels. Many food polymers have the remarkable ability to interact in three
dimensions to generate elastic solids called gels. Gelatin is the best known hydrocolloid with
this ability. Hot gelatin solutions will slowly set into to soft elastic solids at temperatures below
about 30C even at concentrations below 1% by weight of the solution (solid gelatin can thus be
99% water and 1% gelatin). Gelation is the result of non-covalent crosslinks between two or
more individual strands of the gelatin protein polymer. These crosslinks, which form
spontaneous due to specific interactions among the gelatin polypeptides, weave the gelatin
polymers into a three-dimensional random network that binds water tightly and confers solidity
to the largely aqueous solution.
Gelation & the Sol-to-Gel Transition
Long polymers such as proteins and carbohydrates can form thick solutions upon
dissolution in water. Gelatin and starch are well known examples. We refer to these viscous
solutions as sols. Under specific conditions of temperature, pH, and the presence of certain ions,
however, these sols will form solid solutions known as gels. This sol to gel transition can occur
slowly or rapidly and can be initiated by a small change in solution conditions. The underlying
molecular changes (and corresponding macroscopic changes) are complex, however, and reflect
specific molecular interactions among the polymers.
Gelatin: Gelatin is made by extracting the protein collagen from the skin and bones
remaining after butchering pigs and cattle. The process generally involves solubilizing the
proteins using acid or base for long periods, followed by several cycles of purification. The
resulting solution is pure collagen with a range of molecular weights. The strength of the jelly
formed from the collagen is affected by the purity of the gelatin (higher purity makes better jelly)
and the molecular weight distribution (larger molecular weight makes more rigid gel).
In gelatin, the crosslinks probably result from the formation of regions in which 3
individual “gelatin” polymers (individual polypeptide chains made from collagen) form a triple
helical region much like a three-stranded piece of rope. The formation of these triple helical
regions is spontaneous at temperatures below about 30C. Only small regions of the polymers
can form triple helical junctions, however, due to the many possible interactions that occur
among all of the many different polymer chains (about 3x1018 per gram of gelatin). The end
result is the spontaneous formation of a 3D polymer network that completely fills the aqueous
solution giving it the solidity and elasticity of a true solid. The gel forming abilities of gelatin
are remarkable: an aqueous solution containing about 1% gelatin is a solid at room temperature.
Collagen gels form slowly due to the complex nature of the crosslinks that hold the gel
together. Since each crosslink involves the entangling of three chains (each of which may be
involved in other crosslinks), the formation of the gel is a complex process involving the
movement of many polymer chains; crosslinks are thus slow to initiate (nucleate) and grow in
size slowly.
Materials:
Gelatin (Knox or Jello)
Two 500 mL beakers (1-2 cup measuring cups)
Heat source (to dissolve gelatin)
Large container for ice water bath
Thermometer (to measure near 30C)
Food Coloring
Eye droppers or squirt bottles
Gelatin preparation:
Dissolve gelatin as described on package, except make the gelatin at least three times the
recommended concentration (for example, dissolve two packages of Knox gelatin in 1.5 rather
than four cups water).
Color the gelatin solution with a few drops of food coloring. Your choice of colors.
Cool the gelatin solution to about 35C.
Purpose:
This exercise demonstrates gel formation in alginate, a natural biopolymer that undergoes
a sol to gel transition induced by binding calcium ions.
Materials:
Sodium Alginate (Keltone LV)
Two 500 mL beakers (1-2 cup measuring cups)
Calcium Chloride
Food Coloring
Eye droppers or squirt bottles
Alginate preparation:
Materials for the alginate experiment can be acquired from Tic Gums
(www.ticgums.com); ask for the University Kit.
Dissolve alginate in water to make a 2% solution (2 g into 100 mL). Preparation of an
alginate solution is quite tricky because the alginate will readily form nearly insoluble clumps.
The best method is to slowly pour the alginate powder into a rapidly stirring liquid. A blender
works fine. If you have a stir plate, use the highest possible spin setting. The first time you do
this on your own, make the alginate solution the day before. This will let you stir overnight if
clumps develop.
Color the alginate solution with a few drops of food coloring. Your choice of colors.
Materials:
Cornstarch
Small bowls
Water
Food Coloring (optional)