Location via proxy:   [ UP ]  
[Report a bug]   [Manage cookies]                
Scribd Logo
Upload

Welcome to Scribd!

  • 10 views

    Chemistry Project

    Uploaded by

    Aswath S

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd

    Chemistry Project

    Uploaded by

    Aswath S
    10 views12 pages

    Original Title

    chemistry project

    Copyright

    © © All Rights Reserved

    Available Formats

    PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    10 views12 pages

    Chemistry Project

    Uploaded by

    Aswath S

    Copyright:

    © All Rights Reserved
    Download as PDF, TXT or read online from Scribd
    Download as pdf or txt
    of 12

    INDEX

    1. Introduction
    2. Aim
    3. Requirements
    4. Theory
    5. Procedure
    6. Observations
    7. Conclusion
    8. Bibliography
    INTRODUCTION
    Casein is the name of related phosphor proteins. These
    proteins are commonly found in mammalian milk, making up
    80%of the proteins in cow milk and between 20% and 45% of
    the proteins in human milk. Casein has a wide variety of uses,
    from being a major component of cheese, to use as a food
    additive, to a binder for safety matches. As a food source,
    casein supplies amino acids, carbohydrates and two inorganic
    elements, calcium and phosphorus.

    Figure: Structure of Casein

    Composition of Casein :-
    Casein contains a fairly high number of proline residues,
    which do not interact. There are also no disulfide bridges. As
    a result, it is hydrophobic, making it poorly soluble in water. It
    is found in milk as a suspension of particles called “casein
    micelles' ' which have only limited resemblance with
    surfactant-type micellae in a sense that the hydrophilic parts
    reside at the surface and they are spherical. However, in sharp
    contrast to surfactant micelles, the interior of a casein micelle
    is highly hydrated. The caseins in the micelles are held
    together by calcium ions and hydrophobic interactions.Several
    models account for the special conformation of casein in the
    micelles. One of them proposes the micellar nucleus is formed
    by several sub micelles, the periphery consisting of
    microvellosites of K-casein. Another model suggests the
    nucleus is formed by casein-interlinked fibrils. Finally, the
    most recent model proposes a double link among the caseins
    for gelling to take place. All three models consider micelles as
    colloidal particles formed by casein aggregates wrapped up in
    soluble K-casein molecules.

    Uses:-

    Paint- Casein paint is a fast drying, water soluble medium


    used by artists. Casein paint has been used since ancient
    Egyptian times as a form of tempera paint, and was widely
    used by commercial illustrators as the material of choice until
    the late 1960s when, with the advent of acrylic paint, casein
    became less popular. It is still widely used by scene painters,
    although acrylic has made inroads in that field as well.

    Glue- Casein- based glues were popular for woodworking,


    including for aircraft, as late as the de Havilland Mosquito.
    Casein glue is also used in transformer manufacturing
    (specially transformer board) due to its oil permeability. While
    largely replaced by synthetic resins, casein-based glues still
    have a use in certain niche applications, such as laminating
    fireproof doors and the labelling of bottles.

    Cheese making- Cheese consists of proteins and fat from


    milk,, usually the milk of cows, buffalo, goats or sheep. It is
    produced by coagulation of casein. Typically, the milk is
    acidified and then coagu-lated by the addition of rennet,
    containing a proteolytic enzyme, typically obtained from the
    stomachs of calves. The solids are separated and pressed into
    final form. Unlike many proteins, casein is not coagulated by
    heat. During the process of clotting, milk-clotting proteases
    act on the soluble portion of the caseins, K-casein, thus
    originating an unstable micellar state that results in clot
    formation. When coagulated with chymosin(EC 3.4.23.4) is
    an aspartic protease that specially hydrolyzes the peptide bond
    in Phe105-Met106 of K-casein, and is considered to be the
    most efficient protease for the cheese-making industry(Raoet
    al., 1968). British terminology, on the other hand, uses the
    term caescinogens for the uncoagulated protein and casein for
    the coagulated protein. As it exists in milk, it is a salt of
    calcium.

    Plastics and fibre- Some of the earliest plastics were based


    on casein. In particular, galalith was well known for use in
    buttons. Fibre can be made from extruded casein. Lanital, a
    fabric made from casein fibre(known as Aralac in the United
    States), was particularly popular in Italy during the 1930s.
    Recent innovations such as QMilch are offering a more
    refined use of the fibre for modern fabrics.

    Protein Supplements­- An attractive property of the casein


    molecule is its ability to form a gel or clot in the stomach,
    which makes it very efficient in nutrient supply. The clot is
    able to provide a sustained slow release of amino acids into
    the bloodstream, sometimes lasting for several hours.

    Medical and dental uses- Casein-derived compounds are


    used in tooth remineralization products to stabilise amorphous
    calcium phosphate(ACP) and release the ACP onto tooth
    surfaces, where it can facilitate remineralization.

    Controversies

    Autism­- Although research has shown high rates of use of


    complementary and alternative therapies for children with
    autism, including gluten and/or casein exclusion diets, as of
    2008 there is a lack of evidence for the efficacy of these diets.
    A 2006 review of seven studies indicated that, although all
    reported benefits of exclusive diets in reducing autism
    symptoms, all suffered design flaws, and there was not
    enough evidence overall to justify recommending exclusion
    diets to patients.

    A1/A2 beta caseins in milk- According to Food Standards


    Australia New Zealand(FSANZ), “Milk contains many
    types of proteins can be quite different in the milk from
    different breeds of cows and in the milk from other animals.
    Of the six major protein types in cow’s milk, four are casein
    proteins and the other two are whey proteins. The caseins
    usually make up about 80% of the protein in cow’s milk. One
    of the major caseins is beta-casein. There are different beta
    casein types, but the most common are beta casein A1(milk
    high in this type is known as A2 milk). Certain breeds of
    cows, such as Friesians, produce mostly A1 milk, whereas
    other breeds, such as Guernseys, as well as sheep and goat,
    produce mostly A2 milk. Milk produced in Australia and New
    Zealand is normally a mix of A1 and A2 milks. The European
    Food Safety Authority carried out a literature review in 2009
    concluding “a cause and effect relationship is not es-
    tablished between the dietary intake BCM7, related peptides
    or their possible protein precursors and non-communicable
    diseases” . Studies supporting these claims have had
    significant flaws, and the data are in-adequate to guide autism
    treatment recommendations.

    Cancer- T.Colin Campbell’s The China Study(2005), a book,


    describes a direct correlation between casein administered to
    rats and the promotion of cancer cell growth when exposed to
    carcinogens. Aflatoxin( a potent carcinogen) was
    administered to these rats over a 2 week dosing period. The
    rats were given a 1 week post dosing period before beginning
    the test (promotion period). During the promotion period, one
    group of rats was put on a 5% casein protein diet and another
    group on a 20% casein protein diet. None of the rats on 5%
    casein protein developed foci, precur-sors to cancerous cell
    growth, and every rate on 20% casein protein developed the
    pre-cancer foci. It should be noted that all test groups were fed
    a 20% casein diet for a total of 5 weeks(2-wk acclimation,
    2-wk dosing, 1-wk post-dosing)prior to the 12 week
    promotion period in order to survive the initial aflatoxin
    B1(AFB1) dosing, regardless of whether they were in the 5%
    or 20% test groups. Campbell has performed additional
    studies using a range of different carcinogens and other
    experimental animals, and claims to have found a consistent
    correlation between cancer growth and the amount of casein
    protein in diet. A 2001 study suggests another milk protein,
    when protein may play a protective role against colon tumours
    in rats. According to a study from the Australian Dairy
    Council, casein has antimutagenic effects.
    AIM
    To determine the amount of CASEIN present In different
    samples of Milk .

    REQUIREMENTS

    APPARATUS

    ● 250ML BEAKERS
    ● FUNNEL, GLASS ROD
    ● PORCELAIN DISH
    ● CHEMICAL BALANCES
    ● TEST TUBES
    ● FILTRATION FLASK
    ● BURNER

    CHEMICALS
    ● DIFFERENT SAMPLES OF MILK
    ● 1% OF ACETIC ACID SOLUTION
    ● SATURATED AMMONIUM SULPHATE SOLUTION
    THEORY
    Natural milk is an opaque white fluid secreted by the
    mammary glands of female mammals. The main constituents
    of natural milk are protein, carbohydrate, mineral vitamins,
    fats and water and are a complete balanced diet. Fresh milk is
    sweetish in taste. However, when it is kept for a long time at a
    temperature of 5 degrees it becomes sour because of bacteria
    present in air. These bacteria convert lactose of milk into
    lactic acid which is sour in taste. In acidic conditions casein of
    milk starts separating out as a precipitate. When the acidity in
    milk is sufficient and temperature is around 36 degrees, it
    forms a semi-solid mass, called curd.
    PROCEDURE
    1. A clean dry beaker has been taken, followed by putting 20
    ml of cow’s milk into it and adding 20 ml of saturated
    ammonium sulphate slowly and with stirring. Fat along with
    casein was precipitated out.

    2. The solution was filtered and transferred to another beaker.


    Added about 30 ml of water to the precipitate. Only casein
    dissolves in water forming milky solution leaving fat
    undissolved.

    3. The milky solution was heated to about 40° C and 1%


    acetic acid solution dropwise, when casein got precipitated.

    4. Filtered the precipitate, washed with water and the


    precipitate was allowed to dry.

    5. Weighed the dry solid mass in a previously weighed watch


    glass.

    6. The experiment was repeated with other samples of milk.


    OBSERVATION
    TABLE

    Serial Organism from Weight of Weight of


    No. which Milk Casein present Casein present
    sample was in heated Milk in normal Milk
    taken

    1. Cow - 1 gram
    2. Buffalo - 0.8 gram
    3. Goat 1.4gram 1.2 gram
    4. Sheep - 1.15 gram

    CONCLUSION
    Different samples of milk contain different
    percentages of Casein.

    You might also like