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Essential Amino Acids
Cannot be made by the body and must be taken from the food we eat. E.g. Valine
Non-essential amino acids
Can be made in the body so not essential in our food. E.g. Alanine
Sources of protein
Animal; Meat (Actin) Egg (Ablumin) cheese (Casein). Plant; Wheat (Gluten)
Primary Protein Structure
The sequence or order of amino acids in the polypeptide chains. These amino acids are linked together by peptide links. Primary structure also refers to the number of amino acids in each polypeptide chain, E.g. Insulin is a simple protein with 51 amino acids arranged in a specific order
Secondary protein structure
Involves further linking of amino acids in the polypeptide chain/s to give the protein a definite shape which is often the form of a spiral. This structure is caused by cross links that form between different chains or within the one
Disulphide links
Type of cross link, happens when 2 sulphur atoms join within one polypeptide chain or between two different polypeptide chains. The amino acid cysteine has sulphur and so two cysteine amino acids can join together by disulphide links
Hydrogen bonds
Type of cross link, Where a hydrogen atom in one chain bonds with an oxygen atom in another chain, occurs in collagen. These bonds are formed with one polypeptide chain or between two different polypeptide chains
Tertiary protein structure
Involves pattern of folding of the polypeptide chains to give a three dimensional compressed unit. The protein chains cross link forming either a fibrous or a globular protein structure.
Fibrous proteins
Polypeptide chains are straight, coiled or zigzag. These proteins are insoluble in water and not easily denatured. Example keratin, hair. Gluten, wheat. Elastin and collagen, meat
Globular proteins
Polypeptide chains are spherical. These proteins are soluble in water and easily denatured. Example, Ovalbium, egg white. Lactalbumin, milk
Denaturation
A change in the nature of the protein, unfolding of protein chains resulted in irreversible loss in both structure and shape
Heat
Most proteins coagulate when heated, heat causes protein chains to unfold and bond together, which results in hardening or setting of the protein food e.g. fried egg
Chemicals
Acids lower the Ph, e.g. lemon juice added to milk cause the milk protein caseinogen to curdle. The enzyme rennin, coagulates the milk protein caseinogen in the stomach.
Mechanical action (agitation)
Whisking an egg white causes the protein chains to unfold resulting in partial coagulation and foam forms. Moist heat(boiling) converts collagen to gelatine, tenderising meat. Dry heat(grilling) causes meat to become tougher as the meat fibres shrink and lose water. Whisking egg white(mechanical action)
Elasticity
Some proteins such a gluten in flour, are very elastic. Presence of gluten allows bread to rise during cooking by making yeast dough elastic so it can trap Co2
Solubility
Proteins are generally soluble in water except egg white ( only in cold water) and collagen( only in warm water). Moist heat (stewing) converts collagen in meat to gelatine, more tender
Maillard reaction
The non enzymic browning of food when dry heat is applied. Occurs when food is roasted, baked or grilled. Under dry heat a reaction occurs between amino acids and carbohydrates resulting in browning of food e.g. roast beef, roast potatoes, toast
Brown colour
Amino acid, carbohydrate, dry heat
Gel formation
The heat collagen presents in the bones and skin of meat is converted to gelatine on heating. Gelatine has the ability to absorb large amounts of water when heated, as protein chains uncoil and waste becomes trapped.
Sol
A Sol (a solution with evenly dispersed particles) is formed, which on cooling, forms a gel
Foam formation
Whisking an egg white causes protein chains to unfold and air bubbles form, which entrap air creating temporary foam. Heat is generated due which coagulates the egg albumin so the egg white slightly sets. The foam will collapse in time, unless heated so it sets to form a permanent foam e.g. making meringues
Biological value
A measure of the quantity of a protein in food and is determined by the number of essential amino acids present
High biological value
A complete protein, contains all essential amino acids required, generally sourced from animals apart from soya beans
Low biological value
Incomplete protein, lack some essential amino acids, generally plant sourced apart from gelatine
Supplementary value/ complimentary rate
When lbv foods are eaten together they can provide all essential amino acids, only if the deficiency of the amino acid missing in one food can be made up for by being present in the other food e.g. Beans on toast
Beans on toast
Bread is lacking lysine but is high in methionine. Beans are lacking methionine but is high in lysine. By eating beans on toast both essential amino acids are included in the meal