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Subcommittees on Upper Reference Levels of Nutrients and Interpretation and Uses of Dietary Reference Intakes, and the Standing Committee on Scientific Evaluation of Dietary Reference Intakes (2000) Dietary Reference Intakes for Vitamin C, Vitamin E, Selenium and
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Carotenoids: A Report of the Panel on Dietary Antioxidants and Related Compounds. National Academy Press, Washington, D.C. Von Lintig J and Wyss A (2001) Molecular analysis of vitamin A formation: cloning and characterization of beta-carotene 15,150 -dioxygenase. Archives of Biochemistry and Biophysics 385: 4752.
Methods of Manufacture
C R Southward, Fonterra Research Centre, Palmerston North, New Zealand
This article is reproduced from Encyclopedia of Dairy Sciences, Copyright 2002, Academic Press.
Introduction
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The commercial production of casein, the principal protein in cows milk, has occurred for most of the 20th century. During the period to 1960, the major proportion of casein was used in technical (or nonfood) applications. More recently, however, there has been a significant change from technical to edible uses for casein products and this has been reflected in the introduction of requirements for pasteurization of milk intended for casein manufacture (c. 1970) and the greater number of specifications for microbial quality and freedom from impurities. At the present time, the major producers of casein include the European Community (in particular, Denmark, France, Germany, the Irish Republic, and The Netherlands) and New Zealand, with Poland, Australia, and India producing smaller quantities. World production of casein products is currently estimated at 220 000 250 000 tonnes. This article describes the manufacture of the main casein products.
(the isoelectric point of casein) whereas whey proteins remain in solution. Commercial casein is a mixture of four different caseins as1-, as2-, b- and k-casein, and may sometimes be referred to as whole casein. As a phosphoprotein, casein belongs to a relatively rare class of proteins. It contains 0.70.9% phosphorus, covalently bound to the casein by a serine ester linkage. Casein exists in milk in combination with calcium, inorganic phosphate, and citrate as a colloidal suspension of complex micelles and accounts for 2.62.9% by weight of whole milk.
Manufacture
Casein may be precipitated from skimmed milk to produce several products such as acid casein, rennet casein, or coprecipitate. All these products are insoluble in water after precipitation. However, addition of alkali to acid casein yields water-soluble caseinate.
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Acid Casein
Acidification
General
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The proteins that exist in milk can be broadly divided into two groups casein and whey proteins. Caseins may be considered as those proteins that are precipitated when unheated (raw) milk is acidified to pH 4.6
When milk (pH 6.6) is acidified, the calcium and inorganic phosphate are removed from the casein micelles, the net charge on the micelles decreases, and the micelles become less and less stable until the casein precipitates. Complete precipitation of the casein occurs at the isoelectric point, pH 4.6. Acidification of the milk may be carried out by one of the following processes: 1. Inoculation of milk with lactic acid-producing bacteria such as Lactococcus lactis subsp. lactis
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or cremoris. These bacteria, commonly known as starters, convert some of the lactose in the milk to lactic acid during the period of incubation (about 1618 h). This is the most commonly employed method of manufacture in New Zealand (Figure 1). 2. Direct addition of dilute acid to skimmed milk. Hydrochloric acid, sulfuric acid, phosphoric acid, or lactic acid (or, occasionally, other organic acids) may be used for this purpose. The most common method of producing acid casein in countries other than New Zealand is by means of hydrochloric acid. 3. Indirect acidification of skim milk. A number of alternative processes have been patented in which skimmed milk is acidified by one or more of the following: . contact by means of ion exchange resins in the acid (cation) form . addition of acidified whey . electrodialysis It is believed that these processes have relatively minor commercial significance.
Cooking/Acidulation
Following acidulation, the curds and whey are discharged by gravity to a dewheying screen above the first washing vat. The whey is removed and the curds fall into the vat. Alternatively, the curds and whey may be separated more completely using a horizontal solid-bowl centrifuge (decanter) or a caseindewatering press before the curds are transferred to the first wash. A combination of screening and decanter dewheying can be used to reduce the hydraulic load on the decanter. The purpose of washing is to remove whey (containing mainly lactose) from the curds so that the casein produced is relatively pure. The temperature of the wash water may be varied, depending upon particular requirements. Casein is usually subjected to multiple washes and these are operated in a counterflow to the direction of the curds, with the purest curd meeting the cleanest water.
Dewatering
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In the manufacture of acid casein, acidification of the milk is followed, or occasionally preceded, by heating of the mixture. Heating promotes agglomeration of the casein curd particles which subsequently shrink (syneresis) to expel whey. At the same time, the curds become firmer and are able to withstand the mechanical processing that follows. Heating of the acidified milk is sometimes termed cooking (as used in cheese manufacture) and may be carried out, usually in the temperature range 4555 C, by: 1. injection of steam into the pipeline carrying the acidified milk 2. indirect heating by means of a heat exchanger 3. a combination of both preheating through a heat exchanger with steam injection to complete the heating process (Figure 1) In each case, the cooked curds and whey are held in a cooking pipe for a period of about 1020 s before they emerge into an acidulation vat. The curds and whey may remain here for a period varying from 30 s to about 15 min, during which time the curds are agitated gently in the whey until equilibrium between the calcium in the curds and that in the whey is attained. Alternative processes may use a syneresis tube; the cooked curds and whey are held in a large-diameter tube for a period of several minutes (also undergoing acidulation or equilibration).
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After washing, the curds are mechanically dewatered to remove excess water before drying. As drying is a relatively expensive operation, it is worthwhile removing as much water as possible from the curd before transferring the casein to the drier. The texture of the curd is affected by temperature; as the temperature of the wash water is increased, the curd releases more water during dewatering but becomes firm and more plastic and is consequently harder to break up and dry. Therefore, it is necessary to regulate carefully the temperature of the last wash to optimize the conflicting requirements of minimum water content and maximum friability of the curd. Equipment for dewatering casein curd consists of roller or belt presses, decanters, and screen-bowl centrifuges. The roller press, used for many years, is designed to reduce the moisture content of curd to about 55%. The belt press will do a similar duty. Solid-bowl decanters or screen-bowl centrifuges are capable of reducing the moisture content of acid casein curd to about 52%.
Drying
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Drying of casein curd is most commonly carried out using horizontal vibrating fluid-bed driers. These driers have two or more perforated stainless-steel decks (Figure 1). The combined effect of vibration of the decks and the flow of hot air (typical temperature range 75115 C) up through the holes in the decks causes the casein curd to become fluidized and materially helps in the removal of moisture from the particles. Most of the water is removed during the early stages of drying of the casein as it is evaporated from the surface of the particles. The later stages
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Co
Preheater
Flow control Co
Sm
Starter vessels
Steam injector
Tempering Cas Washing and separation by screening Acidulation Screen Whey Exhaust Roller mill Oversize particles Fines recovery cyclone Cas Sifter 30 mesh 60 mesh Press Casein drier Metal removal Cas Storage silos Bag-filling hopper Bag sewing Cas Blending 80 mesh
Weighing
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Figure 1 Outline of the manufacturing steps involved in producing lactic acid casein from skim milk. Wm, whole milk; Sm, skimmed milk; Co, coagulum; Cas, casein.
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of drying require the transfer of moisture from the center to the surface of the particle, and this is a much slower process. Pneumatic-conveying ring driers and attrition driers are also used for drying casein. These employ inline milling and tend to produce finer casein products than those dried in fluid-bed driers.
Cooling, Tempering, Milling, Sifting, Blending, Packing
stable in the presence of calcium ions and form a three-dimensional gel. This process is essential in the production of most types of cheese.
Clotting of Skimmed Milk
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Casein that is produced using fluid-bed driers is warm and soft and unsuitable for grinding immediately in some mills such as roller mills. Consequently, the casein may be cooled and then transferred to tempering bins where equilibration of moisture can occur in and between all the particles during a period of 824 h. The casein may then be ground and sieved, using multideck, gyrating screens, into various particle sizes, usually < 600 mm. Very fine casein (e.g. < 150 mm) is generally produced using pin mills. Following blending of the ground casein, it is packed into multiwall paper bags equipped with plastic liners and stored. The typical composition of acid casein is shown in Table 1.
Pasteurized skimmed milk at a temperature of 29 C (or lower) is mixed with calf rennet (or other milkclotting enzyme) in the approximate ratio (by volume) of 1:7500 rennet to the milk. If a lower setting temperature is used, renneting time must be correspondingly increased. It is also possible to reduce the quantity of rennet added under these conditions and consequently allow a longer time for rennet action to occur.
Cooking
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Rennet Casein
Action of Chymosin
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Casein may also be precipitated from milk by the action of a proteolytic enzyme, such as chymosin, which is present in calf rennet. Chymosin (and other enzymes from animal or microbial sources that cause milk to clot) splits off a portion of the k-casein (referred to as glycomacropeptide or GMP) from the micelles. As a result, the micelles are no longer
The usual technique for cooking rennet casein involves the injection of steam into a cooking line of clotted milk pumped from a vat. However, the vat cooking technique (similar to that used in cheese manufacture) is also practiced in some countries. The cooking temperature used in making rennet casein usually varies from about 50 to 60 C. Dewheying, washing, dewatering, and drying of the curd then proceed in a manner similar to that used for acid casein, and the dried casein is also treated as outlined previously. Where indirect cooking of rennet casein is used, a tubular heat exchanger may be used to cook the curds and whey to a temperature similar to that used in the direct cook (steam injection) process. Other processing steps are similar to those described above but no acidulation step is required after cooking of the rennet casein. The typical composition of rennet casein is shown in Table 1.
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Table 1 Typical composition and properties of casein products Component Composition Moisture (g) Fat (g) Protein (g) (nitrogen 6.38) Ash (g) Lactose (g) Copper (mg) Lead (mg) Iron (mg) Physical properties Color Flavor Solubility in water Acid casein Amount per 100 g 11.5 1.1 86.2 1.8 0.1 Amount per 1 kg 2 <1 520 Creamy white Bland, clean Insoluble Rennet casein Sodium caseinate (spray dried)
11.5 0.4 81.3 8.2 0.1 2 <1 5 Creamy white Bland, clean Insoluble
4.5 1.0 92.0 3.6 0.1 2 <1 510 White Bland, clean Soluble
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Coprecipitates
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Coprecipitates are combinations of casein and whey proteins that are coprecipitated from heated (skimmed) milk. When milk is heated to a temperature greater than 70 C, some of the whey proteins are heatdenatured and may interact with some of the caseins. When a casein precipitant (such as acid or calcium chloride) is added to the heated milk, the casein and whey proteins coprecipitate together. Depending on the pH of precipitation (which may vary from 6.6 to 4.5), the coprecipitate will contain different quantities of calcium (high-calcium at pH 6.6 to low-calcium at pH 4.5). As whey proteins have a higher nutritional value than casein (as measured by several different biological and chemical techniques), coprecipitates also have an enhanced nutritional value compared with casein. The yield of coprecipitate from skimmed milk is usually 520% greater than that of acid casein.
Caseinates
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Caseinates are produced by the neutralization of acid casein with alkali. All caseinates are substantially
Casein dewatering
water-soluble and are typically prepared as a solution of about 20% solids prior to spray drying. Roller-dried caseinates may be prepared from more concentrated solutions. It is also possible to prepare granular, partly soluble, or semidispersible forms of caseinate in which the casein and alkali have only partly reacted. Sodium caseinate is the most common form of this class of product and is prepared by mixing a solution of sodium hydroxide, bicarbonate, or carbonate with acid casein curd or dry acid casein that has been suspended in water and then drying the resultant solution (Figure 2). The dried powder dissolves completely in water to produce a viscous, sticky, straw-colored solution. Calcium caseinate, on the other hand, produces a thin, opaque, white colloidal dispersion in water, similar in appearance to milk. Other caseinates, such as those of potassium and ammonium, are similar in general properties to sodium caseinate. Magnesium caseinate has properties that are intermediate between those of sodium and calcium caseinates. However, relatively insignificant commercial quantities of these products are manufactured at the present time.
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C Colloid mill
F1
pH
F2
Heat exchanger
Jacketed vats
Balance tank
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Figure 2 Suggested plant layout for dissolving casein for sodium caseinate manufacture. Dewatered casein curd is minced, mixed with water, and finely milled in a colloid mill (C). The curdwater slurry is then mixed (D) with dilute sodium hydroxide solution and transferred to the first of two jacketed dissolving vats (F1), each equipped with an agitator. The sodium caseinate solution is subsequently pumped from the second dissolving vat (F2) and extra alkali is added, if necessary. The solution is heated by means of a tubular heat exchanger (H) and then pumped via a balance tank to the spray (or roller) drier for drying. The viscosity of the solution may be monitored and reduced, if necessary, by addition of hot water. From Southward CR (1985) Manufacture and applications of edible casein products. I. Manufacture and properties. New Zealand Journal of Dairy Science and Technology 20: 79101, with permission.
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The typical composition of sodium caseinate is shown in Table 1. Acid (low-calcium) coprecipitates can be dissolved in alkali in a similar manner to that used for acid casein. Both rennet casein and highcalcium coprecipitate (precipitated at a pH of 6 or greater) are usually rendered soluble by means of complex phosphates, such as sodium tripolyphosphate, to produce translucent solutions with a viscosity somewhat higher than that of the corresponding caseinates. In the great majority of applications, in both edible and technical (nonfood) uses, casein must first be made soluble before it can be used in its final application. Although some users convert the dry casein to caseinate themselves, others tend to purchase the caseinate directly from the producer (often as a freshcurd caseinate). For applications in foods. (See Casein and Caseinates: Uses in the Food Industry.)
See also: Casein and Caseinates: Uses in the Food Industry; Cheeses: Starter Cultures Employed in Cheesemaking; Chemistry of Gel Formation; Drying: Fluidizedbed Drying; Lactic Acid Bacteria; Pasteurization: Principles; Starter Cultures; Whey and Whey Powders: Production and Uses; Protein Concentrates and Fractions; Fermentation of Whey
Southward CR and Walker NJ (1980) The manufacture and industrial use of casein. New Zealand Journal of Dairy Science and Technology 15: 201217. Spellacy JR (1953) Casein, Dried and Condensed Whey. San Francisco, California: Lithotype Process. Whitney RMcL (1988) Proteins of milk. In: Wong NP, Jenness R, Keeney M and Marth EH (eds) Fundamentals of Dairy Chemistry, 3rd edn, pp. 81169. New York: Van Nostrand Reinhold.
Introduction
Although casein, as it exists in milk, has been consumed as food for thousands of years, the extracted form of casein had very little application in foods prior to 1960. Instead, from early in the 20th century, and in some cases before then, it was used as an adhesive in wood glues and paper coating, and in paints, fibers, plastics, and leather finishing. The introduction of coffee whiteners and whipped toppings, in particular, by the food industry in the USA during the 1960s played a significant part in the establishment of casein products in foods. These two product groups were based on vegetable fat and contained casein in a water-soluble form (usually sodium caseinate), together with carbohydrate, emulsifiers, and stabilizers. They were promoted as nondairy foods. (As casein was derived from milk, it was not considered to be a dairy product. Furthermore, it had been classified as a chemical because of its longestablished use in nonfood technical applications in adhesives, paints, etc., as described above.) Nondairy coffee whiteners and whipped toppings were thus presented as alternatives to the traditional dairy products of milk, cream, and whipping cream. They offered advantages of lower price (because the (imported) raw materials from which they were made were cheaper than the domestic milk solids they were replacing), convenience, and shelf stability (several of the products were sold in powder form). Other nondairy products followed, many of them containing casein, e.g., so-called imitation milks, imitation cheese, and salad dressings. Food supplements and dietary products were also produced and a number of these were based on casein. This article reviews the use and function of casein products in food.
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Further Reading
Australian Society of Dairy Technology (1972) Casein Manual. Parkville, Melbourne: Australian Society of Dairy Technology. Farrell HM Jr (1988) Physical equilibria: proteins. In: Wong NP, Jenness R, Keeney M and Marth EH (eds) Fundamentals of Dairy Chemistry, 3rd edn, pp. 461510. New York: Van Nostrand Reinhold. Muller LL (1971) Manufacture and uses of casein and coprecipitates: a review. Dairy Science Abstracts 33: 659674. Muller LL (1982) Manufacture of casein, caseinates and coprecipitates. In: Fox PF (ed) Developments in Dairy Chemistry, vol. 1. Proteins, pp. 315337. London: Applied Science. Mulvihill DM (1989) Caseins and caseinates: manufacture. In: Fox PF (ed) Developments in Dairy Chemistry, vol. 4, Functional Milk Proteins, pp. 97130. London: Elsevier Applied Science. Mulvihill DM (1992) Production, functional properties and utilization of milk protein products. In: Fox PF (ed) Advanced Dairy Chemistry, vol. 1, Proteins, pp. 369404. London: Elsevier Applied Science. Southward CR (1985) Manufacture and applications of edible casein products. I. Manufacture and properties. New Zealand Journal of Dairy Science and Technology 20: 79101. Southward CR (1994) Utilization of milk components: casein. In: Robinson RK (ed) Modern Dairy Technology, 2nd edn, vol. 1, Advances in Milk Processing, pp. 375432. London: Chapman and Hall.