ILK AND MILK PRODUCTS ilk is one food for which there seems to be no adequate substitute. All mammals produce milk sfter the birth of the young ones and man uses milk of many animals as his food. The cow is the most important of all these animals as supplier of food. Buffalo and goat milk are also used_ (ere) Vine SUELO aU PAROLES LEN =A CaN OLS ‘lk is a complex mixture of lipids, carbohydrates, proteins and many other organic compounds and inorganic salts dissolved or dispersed in water. The most variable component of milk is fat followed by protein. Milk is a compound liquid which contains fat in emulsion form, protein in colloidal state and lactose as true solution. The composition of milk varies with the species, breed, diet, Jactational period and terval between milking. There is individual variation also. at Buffalo’ ’s milk contains 6.5 per cent fat. Cow’s milk contains 4.1 per cent fat. Milk fat or itter fat is of great economical and nutritive value. The flavour of milk is due to milk fat. Milk is a true emulsion of oil-in-water. The fat globules are stabilised by a surrounding nembrane composed of proteins, phospholipids and cholesterol. Fat globules are visible ider a microscope. Each globule of fat is surrounded by a thin layer which is composed 2 lipid-protein complex and a small amount of carbohydrate. The lipid portion includes oth phospholipids and triglycerides. Fat globules vary widely in size from 2 to 10 um (micro metres) and in number 3x10? x ml.(The larger fat granules come to the surface of milk more quickly due to low specific avity and this can be observed in the transportation of milk. Milk fat is a mixture of several different glycerides, They contain about 64 per cent fatty ids ranging from 4 to 26 carbon atoms.)Milk contains considerable amount of short chain 'y acids which give the characteristi¢ favour and off flavour. Due to their low melting pint -10 to 12°C, they give soft solid consistency to butter, Saturated fatty acids account butyric and caproic acid 62 per cent and unsaturated 37 per cent. Of the unsaturated lity acids, 3.8 per cent constitute polyunsaturated fatty acids. Other lipid materials present milk are phospholipids, sterols, free fatty acids, carotenoids and fat-soluble vitamins. ine}ke Fooo SciENcE Carotenes are responsible for the yellow colour of milk fat. Gerber test is used to know, percentage of fat present in food. ‘ A th Milk fat absorbs volatile odour very readily, Milk, butter and cream shoujg exposed to strong odours. The structure of fat globule is shown in Fig. 5-a. Oy Sterol-rich raft Phospholipid Tii-layer Figure 5-a: Structure of fat globule membrane in milk. Milk fat is composed mainly of triacylglycerols which are present as an emulsion in which the fat globules are stabilised by a surrounding membrane composed of proteins, phospholipids and cholesterol. The fat globules alsp contain small amounts of cholesteryl esters and fat-soluble vitamins and provitamins mainly A, D and p-carotene. Proteins 1 ght Casein: Casein constitutes 80 per cent of the total nitrogen in milk. It is precipitated on "the acidification of milk to pH 4.6 at 20°C.,The remaining whey protein constitutes lactoglobulin and lactalbumin. Milk protein contains proteoses, peptones and milk enzymes Casein is classified as a phosphoprotein because of the phosphoric acid that is contained in its molecular structure. At the normal acidity of fresh milk (about pH 6.6), casein i largely combined through the phosphoric acid part of its structure with calcium caseinatt Hence, casein occurs in milk as a colloidal protein calcium phosphate complex. Casein is also a glycoprotein. Glutamic acid is the predominant one in casein. Prolits aspartic, leucine, lysine and valine are also present. Casein is a good source of essentil amino acids. Casein contains 8.2 per cent calcium and 5.7 per cent carbohydrates. Casein can also be separated from milk by the addition of rennin, an enzyme secrettl by the young calves. Whey proteins! Whey proteins are made up of a-lactabumin and B-lactoglobulin, semi albumin, the immunoglobulins, enzymes and proteose—peptones. f-lactoglobulin accoul for about 50 per cent of total whey proteins, These are not precipitated by acid or rennl they can be coagulated by heat. Whey also contains small amounts of lactoferrin and Sé! transferrin. By a process involving ultrafiltration, whey protein concentrate is pI Whey protein isolates are also produced, It can be given in lactose intolerance.tn ’ Mik ano Mix Prooucts — BIULA arbohydrate jik contains 4-5 per cent carbohydrate, The disaccharide, although trace amounts of gl yesent. Lactose gives on hydrolysis glucose a: Byeetness of sucrose and one third-one fourth ose reacts with protein and develops a bro fs due to nonenzymatic browning. It is calle ed in making butter, cheese and curd, chief carbohydrate present in milk is lactose, lucose, galactose and other sugars are also ind galactose, Lactose has only one sixth the of its solubility in water. When milk is heated, wn colour. The development of brown colour d Maillard reaction. The acid fermentation is Minerals lorides, phosphates, citrates, sulphates and bicarbonates of sodium, potassium, calcium xi magnesium are present. These salts influence the condition and stabilit ry of the proteins, specially the casein fraction. Copper and iron are important in the development of off Bayours in milk and milk products. In addition to this, milk contains trace elements like gnc, aluminium, molybdenum and iodine. nzymes ee enzymes found in milk can ori wntaminating bacteria. Alkaline phosphatase exists as lipoprotein and is queous phases. This enzyme is inactivated by normal tivity is tested to determine the effectiveness of paste More than one type of lipase occur in milk. Mi rancid flavours in milk, Bacterial lipase is very fects. Lipases may be important in the develo, iginate from the mammary glands or may be released by distributed between the lipid and pasteurisation procedures and its urisation. ilk lipase is responsible for the development Tesistant to heat and can cause serious quality pment of desirable flavours in some cheeses. Xanthin oxidase occurs in the fat globule membrane. It is a Conjugated protein complexed. fith flavin adenine dinucleotide, iron and molybdenum. The enzyme degradation of flavin Kdenine dinucleotide gives flavin mono nucleotide and riboflavin. The riboflavin content of may thus be due to xanthin oxidase. Xanthine oxidase can catalyse the oxidation of ichydes which are some of the aroma constituents in fermented dairy products. The ie is not destroyed by pasteurisation. four ite colour of milk is caused by the reflection of light by the colloidally-dispersed casein, Icium and phosphorus. Yellowish colour of milk is due to the Presence of carotene and oflavin. Fat-soluble carotenes are found in milk fat; riboflavin is water soluble which can Visible clearly in whey water, Ke roan Vour and aroma ilk is slightly sweet because of its lactose content, Flavour sensation in mouth is due to Protein and some of the salts such as calcium phosphate, The slight aroma of fresh milk roduced by a number of low molecular weight compounds such as acetone, acetaldehyde, yl sulphide and short chain fatty acids, Some of the volatile compounds to the Our of milk are unique to the fat portion of milk, Boiling changes the flavour of fresh More than pasteurisation. : ae idised flavour can result from the oxidation of phospholipids in the milk, Since traces Copper accelerate the development of oxidised flavour, copper containing equipment isacids are particularly suscepti le poly-unsaturated fatty foxygen and unpleasant flavour substances are prog, ed by the health ‘of the cow or the feeds thar’ y in milk, or the absorption C ries, Some of t he n the presence o be influenc f bacteria, chemical changes 1! ot used in dat qutooxidation if Off flavour in milk may consumed by U foreign flavours a! silk is exposed to ight, In this reaction, tryp ‘ecreases when the off-flavour dee t of the lipases with the fate val ed when and their content brane and permits contac COfrflavours are also produce and riboflavin may be involved Anything that alters the mem! promote rancidity and off flavour. NUTRITIVE VALUE Table 5.1 gives the nutritive value of milk a1 Milk has good quality protein and the biological va only 3-4 per cent protein, due to the quality of protein and the amount that can be ing and the presence of other nutrients makes it indispensable. Lysine is one of the essen, amino acids which is abundant in milk proteins. Cheese, hoya and dehydrated milk pe are concentrated forms hence contain high amount of nutrients per unit. — Milk is the only substance that contains lactose, which has galactose which is essen, for the synthesis of myelin sheath. Lactose, not being easily a bie vouts eae hhich decreases the pH. This drop in pH favour cal lactic acid bacilli in the intestine, wl Se Lactose also increases the permeability of the small intestine for calcium { ilk sugar due to its controlled glycaemic effect, is preferred as a source of. carbokyiall nd milk products. lue is over 90. Though milk conta, in Nutrient content of Aavin Toned* milk (100 ml) Energy kcal 6 Carbohydrate g ae Protein g 32 Fat g 3.0 Calcium mg 125 Sodium mg a Magnesium mg in Potassium mg He Phosphates mg 710 Citrate mg 500 Chloride mg 100 Bicarbonate mg a Sulphate mg ra Vitamin A TU Bt * Aavin toned Sra milk contains skim milk powder, buffaloe’s milk. | Nadu Co -operati i eee etaimysu] TRUONN ‘S21qe} uon|sodusos poo Ue}pUL “tog wePAUEA “ puE AseyDENUASC “pequiophH ‘ueyjueuy “Y “L Yeaduoy ‘eamnos “doREIMN JO: & 3 g a = = 110 06T g 2 S = oro ¥61 110 002 £10 8°08 CEC: 060 sto 910 09 oly sir Tl Ole 8ST gol rT or €8 90 Lye vy 59 €or SH ssl 61s ce 998 OS 908 ou sooueg 2 MOD 2OUA TAL opeyng, 9}oUN YT. (wopuod aiqype Jo # OT 30d) syonpord YMA pue YW Jo anjea oanENN :1S IdeL EN eeeBee Food Science The fat of milk is easily digestible. It contains linoleic acid Qu per cent) linoleni (0.5 per cent) and arachidonic acid (0.14 per cent). Skimmed milk does not contain any Buffalo milk contains high amount of fat. fe Daity foods are a major source of calcitn ee minerals present, The calcium-phosphonis ratio (1.2:1) in milk is regarded a8 most favo for bone development. In addition, dairy products contain other nutrients sich as vita! D and lactose which favour calcium absorption. The calcium requirement cannot be me easily without taking milk. ae) Milk is a poor source of iron, But whatever little iron is present, it is utilised in the bog, Khoya contains more amount of iron because during the process it gets from the Containes Milk has been an important dietary source of preformed vitamin A but many urban regi de consume dairy milk from which much of the vitamin A has been removed with the fat, Aaj milk produced by Government of Tamil Nadu is fortified with 1000 IU for every 500 mil of mig¢ Thiamine occurs in only fair concentration in milk, but is relatively constant in am, Riboflavin is present in a higher concentration in milk than the other B-vitamins ang jg stability to heat makes milk a dependable source of this vitamin. In cheese maki riboflavin is present in whey water. Since it is sensitive to light, when milk is exposed i sunlight 50 per cent of riboflavin is lost. Milk is not a good source of niacin but it is an excellent source of tryptophan. Milk is a very poor source of vitamin C. The amount of vitamin A and D depends poy the feed of the animal. PHYSICAL PROPERTIES Physically, milk is a dilute emulsion, colloidal dispersion and true solution. Acidity Fresh milk has a pH of about 6.5-6.7 at 25°C. As milk stands exposed to air, its acic decreases slightly because of the loss of carbon dioxide. Raw milk, which normally contai some lactic acid producing bacteria gradually increase in acidity on storage. Pasteuris destroys lactic acid bacteria. m because of the significant amount o Viscosity Factors affecting viscosity of milk are state and concentration of the protein and fat, tel of milk, age of milk. Conditions and treatments that affect the stability of casein are in in the viscosity of milk such as acidity, salt balance, heat treatment and the action of va extent of clustering of the globules. Homogenisation and ageing increase the viscosity. Freezing point constituents, lactose and ash which are constant. This fact makes it possible to dete! whether or not milk is diluted, Addition point by —0.0055°C. 3 Boiling point : Milk boils at 100.2°C at value of boiled milk isMILK AND MiLK Prooucts 424 MMccoentsind FFECT OF HEAT protein heating, lactalbumin and lactoglobulin become insoluble or precipitated. Lactalbumin begins to coagulate at a temperature of 66°C and almost total when whey proteins are peated to 90°C for Sminutes. For whey proteins, heat denaturation is an irreversible action. The randomly coiled proteins ‘open up’ and f-lactoglobulin in particular is bound fo the alpha casein fraction by sulphur bridges. The amount of coagulum increases with increasing temperature and time of heating. The coagulum that forms appear as small particles rather than a firm mass and collects on the bottom of the pan in which the milk s heated. The protein found in largest amount in milk, casein, does not coagulate at the usual ¥ temperatures and times used in food preparation. Casein coagulates at 100°C heated at SW 12 hours or at 135°C to one hour or at 155°C to 3 minutes. The resistance of casein to heat Wis because it is in combination with a definite amounts of calcium, magnesium, phosphorus d citrate in milk. Heating periods that produce casein coagulation are shorter when the concentration of asein is increased aboye the regular fluid milk. For example in the sterilisation of canned aporated milk, it is necessary to take certain measures to prevent coagulation of the tasein. One such measure is to prewarm the milk prior to its sterilisation. When milk is heated the albumin forms a flocculant precipitate that settles on the sides of the container. The coagulation of milk proteins by heat is accelerated by an increase in acidity. It is io influenced by the kind and concentration of salts present. The reaction of salts and fannins on coagulation of casein is enhanced by heat. of emulsifying agents permits the coalescence of fat globules. iugar-protein mixtures id reducing sugars, The maximum effect is with lysine, followed by tryptophan and ginine. Glucose reacts more strongly with lysine than lactose or fructose, while lactose ‘acts most readily with tryptophan. : The steps involyed in the Maillard reaction between reducing sugars and amino acids or oteins are as follo (2) Condensation of the aldehyde or ketone group with the amino group. () Rearrangement of condensation products, (¢) Dehydration of the rearranged products. (a isation tc igments. Si mot react oy set it has no reacting group but the hydrolytic products cI lucose and fructose react with amino acids, If proline is involved in the reaction luct may become bitter.Bye Foo SCIENCE ‘The rate of brown increases with increasing PH 6.0 with glucose—o-amino available. cent in a dehydrated iron and copper and Concentrated milk products such contain substantial amou! colour on heating. This react The reaction rate ¢ materials will react. The optim ng increases rapidly with a rise in above 6.8 for glucose—c being decreased at low or very nal moisture levels fo product. The reaction is cata by phosphate ions as evap nts of both protein and the sug tion may also occur in drie temperat acids. The involved amino ac high water levels although the q, ge from 10 to 15 or the reaction ran, / f metals: SUCH ag Iysed by the presence 0: ure. The colour developme, “amino acid solutions and aboye ids are no longer biologicay, orated milk and s\ yeetened condensed mig ar lactose and develop some bri .d milk stored for long periods, H H i | | (H.COH), (H.COH), (H.COH), | { | Brown and HCOH a iH: COH May © = 0 > polymeric | | Amadori | compound H.C =0 H.COH rearrangements _H.CH + \ via schifis bases i protein protein protein Hexose Addition 1-Deoxy, + compound 2-Ketosyl free amino compound group of protein Figure 5-b: Simplified outline of the Maillard reaction. Source:Passmore R., M.A. Eastwood, 1987, Davidson and Passmore Human Nutrition and Dietetics, English Language Book Society/Churchill Livingstone. Acid Whien milk is heated, its acidity decreases at fist owing to the release of dissolved carbon dixie and then neeses Because drogen ons ae Hoerated when cael and phosphate forms insoluble compounds. A balance between these opposing factors prevents I changes of pH during heating. a aa Minerals ‘The dispersion of calcium phosphate in milk is decreased by heati its i c yy heating and part of its precipitated, Some of it collects on the bottomtn hetaeAtaE eee MnPSG Inia Elam some is probably entangled in the scum on the top surface of the milk Iodine is a volatile substance and when heated tends to be lost from milk. Vitamins The fat soluble vitamins like A and D are therm mind I i ostable, The loss of vitamii ii 8 importance as milk is not an important source of this vitamin. neEas . Mix AND Mik Proouets feu flavour nor the Raat f er the avout appearance of milk is appreciably cha astetiriea pet avout of boiled milk is due to loss of dissolved gases Brean diets tha OREN ped As : i * s like carbon dioxide and oxygen ye changes that occu" in protein. The cooked flavour has been shown to be due to the goction CS ey high giiugestines Sulphhydryl compounds are readily oxidised Foe a a aan pea Unt ther reat heated to high temperatures. Oxidised flavour fk do not usves appear until the sulphhydryls are oxidised and the cooked flavour has xored. Digestibility may be slightly improved. Heated aller a fear curs inthe stomach Compared to raw milk, Sereenentnieee fjoro-organisms pesnetion of micro-organisms takes place at higher temperature. avour and digestibilit an eum formation eum is formed when milk is heated in an uncovered pan on the surface due to drying out The scum gets toughened as the temperature is increased, The insoluble scum can be moved from the surface but another one forms. It contains a small amount of coagulated poiein, minerals and fat globules. A tenacious layer of fat that forms on the milk when jgoted is due to the breaking of the film of the protein that surrounds the fat globules in ihcated milk resulting in coalescence of fat globules. Scum formation can be prevented syheating or stirring the milk while heating it. Use of a milk boiler helps to prevent it. It fan be prevented by covering the pan or by diluting the milk. Figure 5-c: Milk cookers, by filing Over The surface tension of milk is related to proteins, fat, phospholipids and Ei jt present in milk. When milk is heated up to its boiling point, it gets agitated Be Mf ensity also decreases which results in foaming, This can be prevented by pouring e ‘aler on its foaming surface which helps to increase the surface tension to some ie formation during the heating of milk is the principle reason for its behaviour of © Over, A certain amount of pressure develops under the scum which later forces thissctitn upwards and the milk flows over the sides of the pan. Stirring breaks the se the presstire and prevents spilling over. un m, fle, Scorching of milk Scorching is due in part to the film of coagulated albumin and other whey 3 gollect on the bottom and sides of the pan. Non-enzymatic browning may yer otein for the brown colour of scorched milk, Heating milk over hot water like milk ee prevent this. Stirring to some extent can also prevent this. Homogenised milk kee more readily than non-homogenised milk. This is due to increased amount of m16taig surface of the uniform fat globules and due to the variations in the temnrpe rag pressures used for homogenisation. Figure 5-d shows the effect of heat on milk. isan Fat Sugdr Casein Balts 70 2 eee g 2 é 8 Be Tuberbulosis Typho faptecoce! Diphtheria eo 20 40 Time-Minutes Figure 5-d: Effect of heat on milk. Source: Hall and Trout, 1968, Milk Pasteurisation, AVI Publication Company. EFFECT OF ACID At pH 6.6, casein is present largely as calcium caseinate. When the acidity of milk increased either by the addition of acid or by natural souring, the acid removes calcium: phosphate from calcium caseinate changing it into casein. Casein coagulates when the nas been reduced to about 5.2 and is least soluble at its iso-electric point pH 4.6. When! pH reaches about 4.6, the colloidally dispersed casein particles become unstable. adhere together and form a coagulm or curd, This probably occurs because the negative charge on the casein particles, which causes them to repel each other and fe! apart, is neutralised by acidic hydrogen ion. ‘d casein can be rendered soluble by additional acid or alkali eithet The precipitate which shifis the pH away from the iso-electric point. Bacterial action in milk can also the pH of the milk and precipitate casein as curd. Tn making curd and cheese thiseins hence changes the Belat, clots the milk and digests i sient concentration to ways in sufficient tion to ca before combining the fruit with ni lanching oF by using canned fruits ests prot bromelin Fruit enzymes proteolyti .dg that do not ntain some Ore’ na i nilk, Destroyini the curdling of m key the en ». from pineapple dig je ens gel, The enzyme organic acids but not al f the enzymes yme action, by bl Bromelin, @ to compoun' clot. All fruits co” prevents curdling ©@ COMPOUNDS (TANNINS) AND SALTS en stages. Curdling of milk may ocey, din the milk. Tannins are also Preseny EFFECT OF PHENOLIC 5 contain tannins chiefly in gre ne ToOR such as potatoes are cooket oa products. Fruits and vegetal if tannin containin in brown sugar and coct Saved ci ficant a veds and stems may contain signil t ; the oe pods, some seeds and woody stems are likely to conti than other parts of the plant, although distribution is general Salts present in milk or food or addition of sodium chlori MICROBIAL SPOILAGE Milk is an excellent medium for the growth of micro-organisms. The odour of milk is due to the activity of the micro-organisms. Milk can be contaminated from the udders to the vessels. Good hygienic conditions are to be used at all levels of milk handling to keep the bacterial count level low. Freshly drawn milk is cooled immediately to 4°C to arrest micorbial growth or heated to boiling to destroy them. If raw milk is placed at room temperature a number of fermentative changes take place. Curdling may occur due to lactic acid produced by bacteria. Some bacteria produce in addition to acid some gaseous products while oth bring about proteolysis of casein resulting in off flavour and unpleasant od The a also bacteria which bring about ropiness in milk. oan ount of phenolic substances. Among vegetables ain more phenolic compound | throughout the plant. ide can curdle the milk, Steps involved in spoilage of milk Milk undergoes predictable changes in ste] steps involved in spoilage of milk. P succession during spoilage. Figure 5-e showsMux AND. Mine PRODUCTS lation ation of casein coal nig can be prevented BY fe. Higher temperature he precipitated curd sirable: Cream of tomato soup is a product in which the preven jsdesiing is needed. Fruit milk shakes may also curdle and curs, the temperature of the ingredients, eg. mango milk shak jowernt .¢ action of acid coagulation. If the heat or acid is excessive, ¢ is tl eS tnd becomes tough and rubbery. s eprecT OF ENZYMES chymosin) rennin ( i , Rennin, a” enzyme secreted by the young calves, brings about the coagulation of ee inf is due to the change in the physico-chemical status of casein, asa result OF teavage of 2 particular peptide bond (between phenylalanine and_methoionine) ff K-casein fraction. This results in the release of a peptide. The remaining protein 1s no pee insolul soluble and it cannot act as a stabilising agent for micellar proteins. Hence, an i gel is formed. Next rennin acts as a general proteolytic enzyme on all the protein casein components: ee ‘When casein is precipitated by the action of rennet, the calcium is not released to the remains attached to the casein. Therefore, cheese made with rennet is a much ree of calcium than cheese made by acid precipitation alone. Cottage cheese 1S by acid precipitation. whey but petter sow often made Casein —22"_, Paracasein —S*_, Calcium paracaseinate (gel) + glycopeptide. Factors affecting rennin coagulation: Temperature: The optimum temperature is 40-42°C. Low temperature retards the reaction and produces a more tender coagulum. Higher temperature within the ange of activity tends to toughen the coagulum, No action occurs below 10°C or above 65°C. . Heating milk before enzyme action: Heating milk to temperature over 65°C prior to the addition of rennin retard or may entirely prevent the formation of firm clot. By heating, the casein is made more resistant to coagulation by rennin. Pasteurisation temperatures do not affect the action of rennin. + pH of the milk: Rennin acts best in a faintly acid medium at 5.8 pH but milk that is acidic enough to curdle is not coagulated by rennin. Rennin action does not occur in an alkaline medium. + Concentration of constituents: Diluting milk, dilutes the casein and calcium. Rennin reacts with diluted milk to form less firm clots and the reaction is noticeably retarded. ‘An excess of sugar may tend to prevent the formation. of clot by rennin. + Salts; Monovalent ions reduce clotting tendencies and divalent and trivalent cations hasten coagulation. + Agitation: The clot formed by rennin is easily broken by stirring and cause sineresis or separation of the watery portion of the milk.