Sunday, 16 June 2013

Biology E-learning : Bread and Ice cream - Protein


The food we have chosen are bread and ice cream. 
To achieve at least 100% RDI, at least 50g of proteins, 65g of lipids (fat) and 300g of carbohydrates are needed.
350g of bread and 200g of can ice cream would provide at least 100% RDI for all three nutrients (51.8g of proteins, 68.3g of lipids (fat) and 318g of carbohydrates).
Combined mass of both food products = 350g + 200g = 550g 

Protein in bread: Gluten 
Protein (enzyme) present in ice cream: Amylase

Gluten: 
Gluten is a protein composite found in foods processed from wheat and related grain species. Gluten gives elasticity through dough, helping it rise and keep its shape and often gives the final product a chewy texture. Gluten may also be found in some cosmetics, hair products, and other dermatological preparations.
Primary structure: linear sequence and number of amino acid residues which make up the polypeptide chain. The bond involved at this level is the peptide bond.
Secondary structure: The repetitive folding or coiling of the polypeptide chain. As a result of hydrogen bonds formed at regular intervals between the -C=O and -NG groups of neighbouring amino acid residues on the backbone of the polypeptide chains. 


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β-Amylase
Amylase
β-Amylase
Another form of amylase, β-amylase is also synthesized by plants. Working from the non-reducing end, β-amylase catalyzes the hydrolysis of the second α-1,4 glycosidic bond, cleaving off two glucose units (maltose) at a time. 
Both α-amylase and β-amylase are present in seeds; β-amylase is present in an inactive form prior to germination, whereas α-amylase and proteases appear once germination has begun. cereal grain amylase is key to the production of malt. Many microbes  also produce amylase to degrade extracellular starches. Animal tissues do not contain β-amylase, although it may be present in microorganisms contained within the digestive tract. The optimum pH for β-amylase is 4.0-5.0
Being a β-amylase,
Primary structure: Linear sequence and number of amino acid residues which make up the polypeptide chain
Secondary structure: Its has beta pleated sheet. it is formed when a single polypeptide chain folds back and forth, or when two regions of the polypeptide chain lie parallel to each other, to form sheets. The structure is stabilized by large numbers of hydrogen bonds form between the C=O and NH groups of one part of the backbone and adjacent part in the parallel regions that hold the structure together. Tertiary structure: 3 Dimensional shape a protein which is formed from extensive bending and folding of the polypetide. 



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