KIIT INT T INTERNATIONAL SCHOOL HEMISTRY INVESTIGATORY PROJECT ON STUDY OF QUANTITY OF ASEIN PRESENT IN IFFERENT MILK SAMPLES” SUBMITTED BY:PRAYASH PATEL GRADE 112-1 SCHOOL NO 75564CERTIFICATE This és to cortiy hat SD rays Datel ofelass 12 Nees sucossaly completed the projeet works on STUDY OF AMOUNT OF CASEIN PRESENT IN DIFFERENT MILK SAMPLES fer das XN SCIENCE pradical examination of the central board f Secondary education tn the year 2023 / 2024 IT IS FURTHER CERTIFIED THAT THIS PROJECT IS INDIVIDUAL WORK OF THE CANDIDATE. Pe INTERNALS SIGNATURE EXTERNAL'S SIGNATURE&CKNOWLEDGEMENT T would like to thank chemi: in men pada Rout for giving me this opportunity to make this project and guiding me throughout the Project, which also helped me in a lot of research and I came to know about so mary new things. Without his help, cooperation and. guidance, this Project wouldn’t have been what it evolved to be. Twould also like to extend my sincere gratitude to my parents and friends for supporting and encouraging me unconditionally throughout this project. The suggestions and criticism on the improvement of this project will be highly appreciated. EXTERNAL S SIGNATURE“7 To study the quantity of Casein present in different samples of milk.Milk is a complete diet as it contains proteins, carl ‘ bohydrates, fats, minerals, vitamins and water. The avera ABE COMposition of milk from different sources is given + below: : \ SOURCEOF | WATER [MINERALS | PROTEINS | FATS [CARBONVORATES | ! MILK 1 i © «© @) (9) @& i | Cow 87.4 07 34 13.9 49 ! 1 !"Human [87.4 02 7% 40 49 : i { i ;, Goat |87 07 33 42 48 : Sheep | 82.6 0.9 55 [es 45 Casein is the most predominant phosphoprote is found in milk an cheese. When coagulated with rennet, casein is sometimes called Paracasein. British terminology, on the other hand, uses the term caseinogen for the uncoagulated protein and casein for coagulated protein. As it exists in milk, it is a salt of calcium. acids and by rennet enzymes, a proteolytic enzyme typically obtained from the stomachs of calves. The enzyme trypsin 1 i 1 1 1 i i 1 i i Casein is not coagulated by heat. It is precipitated by i i ! can hydrolyze off a phosphate-containing peptone. 1 1sein con: sts of a fairly high number of praline » which do not interact. There are also no disulphide a result, it has relatively little secondary structure iary structure. Because of this, it cannot denature. Iti tively hy 1ydrophobic, making it poorly soluble in water. tt ‘ound in milk as a suspension of particles called casein les which show some resemblance with surfactant-typ¢ lae in a sense that the hydrophilic parts reside at the sether by elles >, The casei ace. The caseins in the micelles are held t¢ calcium ions and hydrophobic interactions. These tr lave negative charge and on adding acid to milk the negative es are neutralized. lar The isoelectric point of casein is 4.7. The purified protein water insoluble. While it is also insoluble in neutr al sz ersible in dilute alkalis and in salt alt solutions, it is readily disp’ 1s such as sodium oxalate and sodium acetate, solutiorApplicationsTo study quantity of casein in different samples of milk. Milk contains 3 to 4% casein suspended in water in the colloidal form. It is precipitated in a weakly acidic medium.Fu inne funnel stand, glass rod , filter paper, weight box , test tubes, pestle and mortar. (i) Different samples of milk. (ii) Saturated ammonium sulphate solution. (iii) 1 % acetic acid solution.Ww. 2 be: ‘ash the beaker ( 250 ml) with the distilled water and dry it >. Take 20 ml of buffalo’s milk in 250 ml beaker ani fin its weight 3. Add 20 mi saturated solution of ammonium sulphate slowly with stirring. Fat and casein will separate out as precipitate 4. Filter the above solution and transfer the precipitate in another beaker. 5. Treat the above precipitate with 30 ml distilled water. Casein dissolves forming milky solution whereas fat remains as such. 6. Warm the above contents of the beaker to 40 - 45°C ona low flame. Now, add 1% acetic acid solution drop wise with stirring when casein gets precipitated. 7. Filter the precipitated casein and wash with distilled water and dry it. 8. Find the weight of dry precipitate. g. Repeat the whole experiment with cow’s milk, goat’s milk and sheep’s milk.Volume of milk taken in each case =20 ml Weight of milk taken = W, g Weight of Casein isolated = w, g Percentage of casein = Weight of Casein x 100 Weight of milk milk taken | of milk | Casein (ml) | (Mg) (eg) 1. Buffalo’s 20 | 23.09 ) 0.632 milk 2. Cow's milk 20 i i i i i i ' i i { 3. Goat's milk { ' 35.66. 0.55 casein 2.73% 1.64% 3.67%£ot Samples of milk contains different percentage Percentage of casein is present in milk. Handle apparatus and chemicals carefully Add ammonium sulphate solution very slowly. tir milk while adding chemicals lot disturb milk after adding ammonium e solution and wait some time for fat and ein to precipitate out. ske the amount readings carefully with digita 1achine only.www.wikipedia.com www.encyclopedia.com www.caesine-pro.com www.sciencejournals.com www. icar.nic.in www.zetascience.com www.scribd.com