Five Interesting Food Systems

Objectives:
To introduce the four basic food molecules which have a

profound effect on the way we perceive and enjoy food, namely:

1. 2. 3. 4.

Water Carbohydrate Lipids Protein

To demonstrate by suitable examples, how these 4 basic

molecules are manipulated and fashioned into unique and peculiar chemical food systems which we have come to accept in our daily lives;

1. Water
An inorganic molecule essential to (organic) life. Water

acts as a:

Body temperature regulator; Solvent; Carrier of nutrients & waste; Reactant & reaction medium; Lubricant & plasticizer; Stabilizer of macromolecules & catalytic (enzymatic) properties; Structure, Appearance & Taste; Susceptibility to spoilage & method of preservation used;

Water is a major component on many foods affecting

Removal of water (as in dehydrated foods) greatly alters

foods native properties.

Water Content of various Foods

extracted from: Food Chemistry, Fennema (3rd ed.), p19.
Food Meat: Raw pork (lean) Raw Beef (retail) Raw chicken (less skin) Fish (fillet) Fruit: Cherries, Pears Apples, peaches, oranges Tomatoes, strawberries Vegetables: Peas Broccoli, carrots, potatoes Cabbage, lettuce, beans Water content (%) 53 -60 50 -70 74 65 81 80 -85 90 90 95 74-80 85-90 90-95

Physical Properties of Water & Ice

Extracted from: Food Chemistry, Fennema (3rd edition), p20.
Properties 20 oC O oC (water) O oC (ice) - 20 oC (ice)

Density (g/cm3)
Viscosity (pa.sec) (103) Vapour pressure (k.Pa) Heat capacity (J/g. K) Thermal conductivity (W/m.K)

0.99821
1.002 2.3388 4.1818 0.5984

0.99984
1.793 0.6113 4.2176 0.5610

0.9168
0 0.6113 2.1009 2.240

0.9193
0 0.103 1.9544 2.433

Structure, Properties & Interactions

The structure of water

Association of water molecules (H-bonding)

The structure of Ice

Association of water molecules (H-bonding)

The structure of Ice

Interactions
Water solute interactions Macroscopic: water binding, hydration & holding capacity; Molecular: Bound water Interactions with Ions & ionic groups; Hydrophilic solutes; Hydrophobic solutes; Ampiphilic molecules.

Hydrophilic solutes

Hydrophobic solutes

Ampiphilic molecules

Relative Vapour Pressure & Food Stability

Food stability is affected by Vapour Pressure (p/po (Microbial growth / Enzymic hydrolysis/ Oxidation reactions /Maillard reactions)

Interesting Food System

Carbohydrates Confectionery
Caramelisation & Caramels Gelling agents Jelly Beans, Gummy bears & Cotton Candy

Fats & Oils Types of Creams

Ice Cream; Italian Gelato Whipped cream

Fermented Milk Yoghurt Mayonnaise

Food Proteins
Cheese Sausages

Carbohydrates
Basic structure & nomenclature
Types:

Mono-, oligo- and polysaccharides; Starch

Common Molecules

Confectionary

Effect of Temperature on Sucrose

Caramelization & Caramels

Caramelization: the cooking of plain sugar (syrup) until it turns brown

and aromatic. It leads to the development of a brown colour (browning) but does not require the presence of amino acids and proteins. It requires higher temperatures than Maillard reactions and produces a different mixture of aromatic compounds (and flavour); Caramels: the brown, sweet, aromatic syrup produced in caramelization used as colouring & flavouring agents in many dishes. It may also refer to the combination of caramelized sugar to which milk products (cream) has been added to generate colour & aroma. Sugar Work: molten sucrose with a large proportion of glucose and fructose (as corn syrup HFCS, or by adding acid citric/tartaric) to help prevent crystallisation of sucrose. The sugar mixture is heated until it reaches ca. 160 oC (no water present) but not yet caramelised (>165 oC). When cooled to 50-55oC, it is pliable like dough, and can be formed or blown into hollow spheres. It can be pulled, twisted & folded unto itself. Colour & air can be incorporated to form an attractive fabric.

Gelling Agents
Pectins:
large CHO molecule (which is found in plant cell walls) bound together into a

continuous sponge like network that traps water in many several different pockets; Extracted from fruits by boiling in water but are negatively charged; Bonding is encouraged by

Reducing available water (add sugar @ 55% w/w and boil to final sugar of 60 65%); Add acid (at 0.5% citric) to a pH of between 2.8 3.5, thus neutralizing the ve charge & allowing the bonding of pectin molecules network;

Gelatin extracted from bone & animal skin, comingled with collagen as

helix:
Large molecules of coiled protein which uncoil when heated and recoil when

cooled; Most protein behave in an opposite way: egg solidifies, milk curdles; meat stiffens; At 1% gelatin, a sufficiently rigid network of molecules is formed (transition temperature = 40 C); Desert Jellies are at 3% gelatin;

Jelly Beans, Gummy bears & Cotton Candy

Composition: Gummy Bears:
Equal wts. Of Sucrose & corn syrup, and a mixture of gelatin (5 15%) &

pectins (1%); The gelatin provides a rubbery texture while the pectin a crumbly texture; Because gelatin is degraded at high temperature, a concentrated solution is added to the sugar syrup after it has been cooled; Water content is about 15%;

Cotton Candy: 1904 World Fair, St. Louis:

Hard candy, filaments of sugar glass which is very fine & with the

consistency of cotton balls, dissolving in the mouth at exposure to moisture in the mouth; Melted sugar is forced through spinnerettes into air where it instantly solidifies into threads;

Lipids, Fats & Oils

Nomenclature & classification: # of C & unsaturation;
Physical aspects: Fats vs Oils Chemical aspects

Lipolysis: Thermal decomposition & Frying: Smoke points & free fatty acids; Vegetable oils @ 230 oC & Fats @ 190 oC; Hydrogenation: cis to trans fats.

Linoleic & Eicosa-pentaenoic acids

1. Types of Cream:
Cream is a special portion of milk (with 3.5% fat) that is greatly enriched with fat (> 20%) and is layer of fat which separates from fresh milk left to stand.
Single Cream (20%) Cream with a low fat-content, which does not thicken when beaten. Used in both sweet and savory dishes. Also know as light cream. Light Cream (20% fat - range 18-30%) Pretty much the same as half and half. Also know as coffee cream or table cream. Will whip if it contains 30% butterfat but will not be very stable. Generally contains only 20% butterfat. Also know as single cream. Light cream is not available everywhere. Whipping Cream (30%) Cream with enough butterfat in it to allow it to thicken when whipped. Does not whip as well as heavy cream but works well for toppings and fillings. Almost all whipping cream is now ultra-pasteurized, a process of heating that considerably extends its shelf life by killing bacteria and enzymes. Heavy Cream / or Heavy Whipping Cream (36 to 38%) This cream whips denser than whipping cream. Whips up well and holds its shape. Doubles in volume when whipped.

ICE CREAM STRUCTURE

Ice cream:
ice crystal, conc. cream, sugar, air: Water (60%), sugar (15%), milk fat (10 -20%)
Ice cream: 1. Ice crystal form (the backbone) from water molecules as they freeze the size determines its texture; 2. Concentrated cream remains as the ice crystal forms. The hydrophilic solutes (sugar) retain some water into which the milk fat & proteins are dissolved; 3. With constant stirring, this mixture coats each ice crystal and allows them to stick together; 4. Air cells are trapped in the ice cream when agitated, inflating the volume by as much as 100%! (ie. doubling the initial liquid volume); Achieving the right balance of ice, cream & air is critical to good ice cream. Good ice cream should be creamy, smooth and firm. Less water small ice xstals & smooth texture: High sugar & milk solids heavy, syrupy product; Too much fat buttery product. Premium quality ice cream more cream (high fat) and egg yolk. 3 Steps of making Ice Cream: Preparing the Mix, freezing it rapidly & hardening it (in small containers).

Italian Gelato
A variation of the French /custard ice cream containing the additional

ingredient of egg yolk (up to 12 yolks per litre), low in milk fat and higher in water content; Gelato is high in both egg yolk and butterfat, and is frozen with little incorporation of air; How can Liquid Nitrogen be used to make ice cream?

Whipped cream:
An intimate mixture of liquid cream and air a key feature being the fat concentration of the cream being used, which must be > 30%;

2. Fresh(ly) Fermented Milk: Yoghurt

Lactic acid bacteria (Genus: Lactococcus & Lactobacillus): responsible for transforming (fermenting) milk sugar (lactose) to sour lactic acid, which in turn retards the growth of other microbes self preserving. The accumulation of acid causes the milk protein (casein) to form curds and thicken milk in 2 -3 hrs! Yoghurt turkish for milk that has been fermented into a tart, semi-solid mass. For commercial applications, symbiotic species Lactobacillus delbrueckii sbsp. bulgaricus and Streptococous salivarius sbsp. thermophilus are used to develop acidity at 1% lactic acid and acetaldehyde to give the characteristic fresh flavour & aroma. Ingredients: milk (cow, goat, sheep), bacteria, flavour; Milk is first heated (90 C/10 min) to sterilise batch & denature whey protein lactoglobulin, and disperse casein molecules. It is then cooled to 40 45 C and fermented by adding bacteria and held until it sets in about 2-3 hrs; Rapid gel formation coarse casein network structure & weeping of whey; Slow gel formation fine casein network structure & retention of whey proteins.

3. Cold Egg Sauce: Mayonnaise:

An emulsion of oil droplets (80%) suspended in water based ingredients (egg yolk, lemon juice or vinegar, water and mustard (for flavour / CHO); Dense and cannot be poured.
Egg Yolk as protein thickeners: 16% protein/50% water/ Salt causes the yolk to separate into its component granules (salting out) increasing surface area;

Making Mayonnaise (room temperature): 1. Mix egg yolk, lemon juice, salt, mustard 2. Whisk in oil slowly at first, and then more rapidly as emulsion thickens. Notes: 3. What is critical is the ratio of (oil: water) there must be enough (water) for the population of oil droplets to fit into; 4. The Volume of (Oil to water based) ingredient = 3: 1 ie- egg yolk & salt, lemon juice, vinegar, and other water soluble ingredient. 5. Sensitivity: extremes of cold, heat and agitation will damage the emulsion. Adding stabilisers (CHO or proteins) can fill spaces between oil droplets. PROBLEM: Mayonnaise becomes hard: how would you restore structure? Explain.

Food Proteins
Structure & Units Functional Properties Denaturation Emulsification Enzymes Foaming Gelation Water Holding capacity Hydrolysis Protein Solubility
APPLICATIONS:

Milk Protein & Cheese Whey Protein Caseins

Iso-electric point Micelle structure Cheese making

Plain Cheese Mozzarella

Structure & Units

Proteins are:
Polymers of amino acid (polypeptides); All amino acids have a common

Amino acid unit

Amine group 2. Acid group 3. Central carbon 4. Side chain The side chain allows for 5 classes i.e. - acidic, basic, neutral, aromatic & sulfur-containing;
1.

structure; Proteins are composed of chains of amino acids joined by peptide bonds; Most proteins (polypeptides) are made of several dozen to hundreds of amino acids units; Most proteins exist as non-conjugated Example of conjugated protein are: Egg white proteins are glycoproteins (not bound) molecules while some are i.e. conjugated with sugar conjugated (bound) to other non molecules called ovomucoid and protein molecules to form complex ovalbumin; molecules; In egg yolk, the protein is conjugated 1o, 2o, 3o & Quaternary Structures form with lipids to form a low density increasingly complex molecules and lipoprotein; are stabilised by hydrogen and disulfide bonds between amino acids. The milk protein, casein, contains phosphate in its structure.

Peptide Bond

1o, 2o, 3o & Quaternary Structures

Food Protein shape

Food Protein Egg Albumin Meat & legume globulins Collagen & Elastin Glycoprotein & Lipoprotein (ovomucoid & ovalbumin) Phospho-protein & metalloproteins (myoglobin) Protein Structure Globular Globular Fibrous Conjugated Conjugated Protein Shape Spherical Spherical Elongated Protein bound to sugars & lipids Protein bound to P & metals (Fe)

Functional Properties
Denaturation
Unfolding of protein structure

Emulsification
Proteins stabilise emulsions by

changing original properties & occurs when roasting meat (actin, myosin & myoglobin) or cooking eggs (ovalbumin), or even whipping egg white to form a foam; Unique to proteins & is the relaxation of protein 3o structure with decreased functional properties & solubility; Coagulation is distinct from denaturation and is the precipitation of protein as individual molecule aggregates.

acting at the oil-water interface; This gives stability to oil-water emulsions (mixtures) as seen in common food products such as salad dressing, sauces & frankfurters/sausages; Proteins are isolated from foods (meat, milk, eggs, soy) for use as emulsifiers;

Proteins as Enzymes
Enzymes are
proteins used to speed up chemical

reactions; They are used to produce various products in the food industry;

Applications
Production of HFCS a major

sweetener in the food industry via

AMYLASE Corn starch to Dextrins; FUNGAL ENZYMES Dextrins to Glucoe, & GLUCOSE ISOMERASE Glucose to 42% Fructose.

Other Functional Properties

Foaming
Foams are colloidal

Gelation
Protein can form a well

dispersions of gas in liquids; Foods that are good foaming agents are

Egg, Milk, Soy Protein;

ordered gel matrix which can hold together water, fat and other ingredients; Examples are

Examples of foam foods are

Ice cream; Whipped toppings Beer froth

Bread Dough Gelatin desserts; Tofu Yoghurt

 Water holding Capacity

Food Protein interaction with H2O

Hydrolysis
By protease enzymes (papain)

The presence of hydrophilic groups

and charged groups is responsible for this characteristic, & Influenced by pH, salt content & temperature; Protein: protein interactions Strong interactions when the protein molecule is electrically neutral; Protein: water association Strong interactions when the protein molecule is polar; Increasing salt content, protein polarisation is increased facilitating increased binding with water; Increasing temperature to 80 oC causes gelation of proteins which traps water inside the 3D gel network.

Protein + H2O amino acid;

Non-enzymic hydrolysis (heat/pH)

Protein + H2O amino acid Occurs during cooking and food processing.

Protein Solubility
Affected by pH & temperature Function in foods related to

hydrated proteins; Soluble proteins used to produce whipped creams products, protein films and emulsions.

Milk Protein & Cheese

Milk Protein & Cheese

Excellent source of high quality

protein; Important proteins are

Casein 80% of all milk proteins and

Caseins
Exists in a disordered 3o state as

are comprised of 2 alpha caseins (1 & 2), -casein, -casein & -casein. Whey 20% of milk proteins;

Functional Properties Whey proteins

have an ordered globular structure with disulfide (S-S) linkages;

randomly coiled molecules; Caseins are resistant to heat denaturation due to their structure; Addition of rennin (enzyme) causes the formation of gels; When milk is acidified to pH 4.6, the caseins become insoluble; Precipitate on addition of acids;

remain colloidally dispersed in

solution; Denatured by heat to form gels;

Casein
Iso-electric Point (pH = pI)
A critical pH for proteins when

the H+ & OH- are equal; Net charge of protein is zero; At pI, protein is unstable & insoluble; This instability causes protein bond to each other by H- bonds (protein: protein interactions) clumping proteins and casuing them to precipitate (fall out of solutions); Phenomenon used is cheese making by forming a solid protein cheese curd due to the clumping of casein;

Micelle Structure
Casein Micelles
In milk, case exists within micelles

each with thousands of casein polypeptide molecules; Ca-phosphate are complexed to casein forming colloidal particles; Sub-micelles are composed of alpha, beta & kappa caseins, Alpha & beta reacts with Ca & precipitates while kappa remains free to stabilise the colloidal suspension by binding to H2O; The P group of alpha & kappa react with Ca to form crosslinks between submicelles; The kappa form dominates the micelle structure by aggregating to form a hydrophilic cap where no cross-linking occurs;

Cheese Making
Casein micelles are stable in milk

as colloids; To make cheese, the casein micelles must be destabilised by disrupting the stabilising effect of kappa casein; Rennin, catalyses the splitting of kappa-casein into
a micelle remnant called

para -casein, and - casein macropeptide, which is lost in the whey liquid;

In the presence of Ca, para--

casein is insoluble; The casein micelles remnants aggregate to form the cheese curd (gel);

Plain cheese vs Mozzarella

Comparison of proteins

5. Sausage
Sausage: from Latin salt & names a mixture of chopped meat and salt stuffed in an edible casing. The salt i) controls growth of microbes, and ii) dissolves the protein fiber (myosin) out of the meat and makes it available to act as a glue, binding the pieces together. Emulsified sausages: Frankfurters/wieners /bologna- very fine textured, homogenous, tender interior with relatively mild flavour. They contain pork/beef/chicken meat, fat, salt, sodium nitrite, flavouring & water homogenised together to form a smooth meat batter similar to an emulsified sauce (like mayonaise). The fat is evenly dispersed in very small droplets, surrounded by muscle cell & dissolved muscle protein (myosin) network. Emulsion stability is highly dependent on temperature (16 21 C) & after batter is prepared, it is stuffed into casings & cooked (smoked) at 70 C. Heat coagulates the meat proteins and turns the batter into a solid mass from which the casings can be removed. The high water content (55%) makes sausages perishable and they must be refrigerated.

Breakfast Meats:

Yoghurt & Cheese:

Alpha - casein