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Effect of manufacture steps on cheese structure (review)

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DOI: 10.7813/2075-4124.2012/4-6/A.11

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Enab A.K., Fatma A.M. Hassan, Mona A.M. Abd El. Gawad. Effect of manufacture steps on cheese
structure (review). International Journal of Academic Research Part A; 2012; 4(6), 79-89.
DOI: 10.7813/2075-4124.2012/4-6/A.11

EFFECT OF MANUFACTURE STEPS ON

CHEESE STRUCTURE (REVIEW)
Enab A. K., Fatma A. M. Hassan, Mona A. M. Abd El. Gawad

Dairy Science Departement of Nationa Research Center, Dokki, Giza (EGYPT)

fatmahassan98@yahoo.com

DOI: 10.7813/2075-4124.2012/4-6/A.11

ABSTRACT

Many factors influence the texture of cheese such as: manufacturing, procedure variety and composition
and bio chemical changes during ripening. Texture is the sensory and functional manifestation of the structural,
mechanical and surface properties of foods detected through the senses of vision, hearing, touch, and kinesthetic.
Cheese has a complex structure that causes differences, even within the same variety of cheese, which depend on
compositional factors and their changes during processing techniques and storage conditions. In order to be able
to fully understand what determines cheese quality and texture, it is necessary to have an understanding of the
physical and chemical mechanisms that occur during cheese processing.

Key words: cheese structure, texture, homogenization, ultrafiltration pressure

1. INTRODUCTION

All cheeses contain three major constituents—protein (casein), fat and water (brine), which contribute to the
structure and rheological properties. This structure is common to all types of cheese (Fox 1987, Luyten et al.
1991, Lucey et al. 2003, Pappa et al. 2007). The functional properties of cheese ingredients are dictated by the
structure; therefore knowledge of how cheese structure is produced and develops during ripening is a great
importance of the cheese manufacturer. The prediction and subsequent control of functional properties requires an
understanding of where the components of cheese are located in relation to each other, and how they interact and
change during ripening (McKenna 2003).
Instrumentation has been used to study the microstructure of the individual components in milk products
such as casein micelles and fat globules, casein–fat interactions, state of water (bulk, or bound), and changes
which these components undergo either alone or by interactions with each other or with additional ingredients such
as stabilizers, thickeners, starter culture, etc., during manufacture process. These include scanning and
transmission electron microscopy, confocal laser scanning microscopy, and atomic force microscopy, although,
atomic force microscopy has not largely been applied to cheese structural studies (Everett and Auty 2008).

2. TEXTURE DEFINATION

A general agreement has been reached on the definition of texture, which evolved from efforts of a number
of researchers (Lawless and Heymann, 1999, Brown 2002, Szczesniak 2002, Foegeding et al. 2003, Peleg
2006). It state that texture is the sensory and functional manifestation of the structural, mechanical and surface
properties of foods detected through the senses of vision, hearing, touch, and kinesthetic. This definition conveys
important concepts such as:

 Texture is a sensory property and, thus, only human being can perceive and describe it;
 It is a multi-parameter attribute, not just tenderness or chewiness, but a gamut of characteristics;
 It derives from structure of the food (texture depend upon the relative amounts and extents of
interaction between cheese structural units); and it is detected by several senses, the most important ones
being the senses of touch and pressure.

3. TEXTURE GENERATION IN CHEESE

Cheese has a complex structure that causes differences, even within the same variety of cheese, which
depend on compositional factors and their changes during processing techniques and storage conditions
(Lawrence et al. 1987, Prasad and Alvarez 1999, Kandarakis et al. 2001, Watkinson et al. 2001, Tsigkros et
al.2003).
The physical properties of cheese (i.e., body/texture, melt/stretch, and color) are influenced by initial cheese
milk composition, manufacturing procedures, and ripening conditions (Lucey et al. 2003). In order to be able to

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fully understand what determines cheese quality and texture, it is necessary to have an understanding of the
physical and chemical mechanisms that occur during cheese processing.

1. Milk constituents and preparation

Milk is composed of water, proteins, lipid, lactose, and minerals. The goal of making cheese is to form a
network from the casein that entraps the fat, bacterial cell, minerals and some of the water, and concentrate this by
removing excess whey (Everett and Auty 2008). The first stage in the processing of cheese is milk
standardization. Milk standardization gives the producer the ability to manipulate the composition of the final
cheese by controlling the composition of the starting milk in order to meet the legal definition of the specific variety
and to improve yields (Lucey and Kelly 1994, Scott 1998). Other considerations of the initial milk that affect
cheese texture;
 The source of the milk: Milk coming from mastitic cows has higher somatic cell counts, indicating
an increase in plasmin activity. Plasmins degrade β-caseins, (Fox 1989) which initially results in less
network formation and lower yields. Pappa et al. (2007) found that Goats’ milk resulted in harder Teleme
cheese than that made from cows' and ewes' milk, regardless of the culture used and the age examined. In
addition, the values of force and compression at the point of fracture of cheeses made with goats’ milk were
higher than those found of cheeses made with the other two types of milk.
 Standardization of milk: Milk standardization gives the producer the ability to manipulate the
composition of the final cheese by controlling the composition of the starting milk in order to meet the legal
definition of the specific variety and to improve yields. In addition, however, the use of standardized milk
avoids the manufacture of cheese containing excess fat and minimizes fat and casein losses into the whey
(Lucey and Kelly 1994, Scott 1998). The three main methods for standardizing milk for cheese making: the
addition of skimmed milk powder, the addition of liquid skim milk and the removal of cream. In the first two
cases the quality and temperature history of the skimmed milk powder or liquid are important, particularly in
the manufacture of high quality Cheddar cheese. When Cheddar cheese was made from milk showing the
normal seasonal trends in composition and from milk that had been standardized to a crude protein-to-fat
ratio of 0.9 (by the addition of skimmed milk), standardization resulted in a small loss of yield from a
standard volume of milk (averaged over a complete year). This loss was compensated for by an almost
equal gain in the efficiency of fat retention (Banks et al. 1989).
 Homogenization is the process in which fat globules in the milk are broken up into smaller
globules with a greater total fat–water interfacial surface area. The casein component of the new interfacial
area is capable of interacting with the surrounding casein matrix to participate in the structure (Zamora et
al. 2011). The outcome is a firmer cheese with less free oil formation compared to non-homogenised
cheese with the same fat content (Rowney et al. 2003). Everett and Auty (2008) reported that
homogenisation of milk prior to the manufacture of cream cheese allows the fat globules to interact with the
casein matrix and produce a more elastic cheese with less free oil formation. In addition, use of
homogenized milk for cheese-making will produce higher yields since more moisture will ultimately be
retained in the protein network. However, such milk produces a finer network of protein, which impairs curd-
matting properties and results in cheese with decreased end-use functionality such as stretch and melt
(Rowney et al.1999, Abd El- Gawad et al. 2012).
 Ultrafiltration: It is used to concentrate the milk which adverse affects on texture and rate of
maturation. Ultrafiltered (UF) milk affects the composition, structure, and maturation of cheese, which then
affects the texture. From a sensory perspective, firmness, crumbliness, granularity, and dryness increased
as the concentration factor of the milk increased. However, elasticity was affected little by the concentration.
Since structurally, the UF and the control milk were similar, they hypothesized that structural differences
seen between the curds of each were probably due to differences in the concentration of milk components
rather than the structural differences in the initial milk. They hypothesized that the basic structure of the
protein network is established during the initial curd formation and is not altered much during later stages of
ripening (Brown 2002). Karlsson et al. (2007) indicated that the aggregates formed in the UF concentrate
were much smaller and could not be detected with confocal laser scanning micrographs prior to coagulation
point. Due to the higher volume fraction of casein micelles in the UF concentrate than in unconcentrated
skim milk, the bonds between casein strands will strengthen rapidly preventing further rearrangements in
the gel microstructure. Thus, the casein network was less coarse in gels made from UF concentrate and the
microstructure was preserved during storage at 13 °C for 60 days.
 High pressure treatment of milk increases the rate of firming of renneted milk, consistent with a
greater casein cross-link density, and with increased gel strength (Hayes and Kelly 2003), (Huppertz et
al.2005). Buffa et al., (2001) found that treatment of milk at high pressures of around 500MPa reduces the
size of milk fat globules and disperses these more evenly in a more compact protein matrix, producing a
cheese that is firmer and more elastic. In addition, Pressure treatment of immature Mozzarella cheese
increased meltability and hardness, and increased the swelling of the casein matrix concomitant with greater
water retention (O’Reilly et al. 2002, Abd El- Gawad et al. 2012). The application of HP for the
acceleration of cheese ripening has been suggested. Exposure to HP increases cell membrane permeability
(Cheftel 1995, Malone et al. 2002, Wouters et al. 1998), favouring the release of intracellular material such
as peptidases to the medium and, subsequently, the access of enzymes to their substrates (Trujillo et al.
2000). On the other hand, HP treatment causes the release of Ca, P and αs1- and αs2-caseins and the
destabilization of micelles (Huppertz et al. 2004, Regnault et al. 2006), which might render caseins more
susceptible to the action of proteolytic enzymes. Young Cheddar cheese treated at 50MPa for 72 hr at 25

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±1ºC showed similar free amino acid (FAA) levels and taste than 6-month-old control cheese (Yokoyama et
al.1992). A faster as1-casein degradation and an increase in pH 4.6-soluble nitrogen and FAA levels was
reported for Cheddar cheese treated at 2 days of age under the same conditions (O’Reilly et al. 2000).
Garrotxa cheese, a semi-hard goat’s milk variety, treated on the day after manufacture at 50MPa for 72 h at
25 ±1C showed lower residual as-casein contents and higher pH 4.6-soluble nitrogen values than untreated
cheese (Saldo et al. 2001) and when treated at 400MPa for 5 min at 14 ±1C the content of free amino acids
samples (FAAs) increased with respect to untreated cheese (Saldo et al. 2002). Juan et al.(2004) reported
higher FAA levels for semi-hard ewes’ milk cheese treated on the day after manufacture at 300MPa for 10
min at 12 ±1C than for untreated cheese and for cheeses treated at 400 or 500MPa. However, FAA levels
were lower in Cheddar cheese treated by HP within 12 h of production than in untreated cheese (O’Reilly et
al. 2003) and Cheddar cheese pressurized at 1 month of age at 400, 500 or 800MPa also evolved FAAs at
a lower rate than control cheese (Wick et al. 2004).
 Starter cultures: The starter cultures digest the lactose in the milk and produce lactic acid, which
aids in lowering the pH of the milk creating the ideal environment for coagulation. The pH affects the
reactivity of the binding sites on the casein molecules and therefore, influences the structure of the matrix.
Second, starter cultures produce enzymes that affect cheese flavor and texture (Rowney et al.1999,
Ahmed et al. 2011).

2. Cheese-making process
Cheese manufacture is essentially for the dehydration of milk in combination with other preservative effects
such culturing, acidification, salting, packaging, and refrigeration. The rennet induced milk coagulum is cut and
heated to expel moisture in a process termed syneresis. Curds are later drained, salted, and packaged into fresh
cheese. The pH continually drops throughout the process to a value between 4.6 and 6.0 for most varieties of
cheese. An additional step is added during curd draining for Cheddar-like cheese varieties. In this process, called
cheddaring, the pH is allowed to drop over a period of 1–2 h with frequent turning and stacking of curd blocks, after
which the curd develops a chicken breast texture that flows under the weight of the curd blocks. Electron
microscopy has shown quite clearly how the various components in cheese, such as protein fibres, fat, water
channels, microbial cells and precipitated minerals interact (Kalab 1979, Kalab and Harwalkar 1973), although the
sample preparation techniques can introduce artefacts, primarily through the removal of water.

3. Structure formation via coagulation

Coagulation has been described as a two-phase process. In the first phase, para-caseins are formed by
enzymatic reactions. Chymosin, an enzyme in rennet, acts upon the casein micelle in the milk to form the para-
caseins (Richardson et al. 1992). Chymosin cleaves off the κ-casein between the Phe105-Met106 bonds, releasing
glycomacropeptide into solution; this makes the micelle less sterically and electrostatically stable (Fox 1989,
Dalgleish, 1997). The bare micelle is now composed of primarily α, β, and para κ−caseins. When approximately
85% of the κ-casein has been hydrolyzed, the second phase of coagulation begins (Fox 1989). The para-caseins
start to aggregate. Phosphoseryl groups, contained in the casein, react with the calcium in the cheese to form
bridges, connecting the caseins. Over time, many connections form a three-dimensional network of casein; this
network entraps fat and moisture, forming a multi-components gel. The structure of cheese fits a filled gel model. A
filled gel is described as a multi-components material in which one of the components is a gelling agent that forms
a continuous network and the other component(s) acts to fill in the network (Swaisgood 1992). Cheese is
composed of a continuous, three-dimensional network of primarily casein. When this protein network forms during
coagulation, it entraps fat globules and moisture contained in the milk forming the filler component. It is thought that
since the fat is highly hydrophobic, water in this system can associate with the protein; it exists in both free and
bound states (Prentice 1987, Ahmed et al. 2011).
Gel formation is greatly influenced by pH, Ca concentration, protein content, and temperature (Lomholt and
Qvist 1999, Lucey 2002). In cheese making, gelation pH varies due to the action of starter culture, pre-ripening of
the cheese milk, or addition of acid or acidulants. Lucey et al. (2003) reported that Gel stiffness increases with a
reduction in pH up to a maximum at pH 6.0 to 6.2; at lower pH values the stiffness decreases. Calcium
concentration varies in practice due to changes in milk composition, acid development, and the addition of CaCl2.
Gelation temperature is selected by the cheese-makers based on cheese type and experience (Lucey et al. 2003).
Madadlou et al. (2006) showed that milk coagulation temperature had important effects on chemical composition,
opacity, microstructure, and rheological behavior of Iranian white cheese. As the coagulation temperature
increased, the moisture content and whiteness index decreased, and protein and fat contents increased.
In Ricotta and queso blanco style cheeses, milk is heated to ~80 to 85°C. Acidulants (e.g., acetic, lactic, or
citric acid) are added to the hot milk to bring the pH to ~5.9 to 5.4. Flocculation of casein occurs rapidly under these
conditions, before it is mechanically dewheyed. In these cheeses, both casein and β-lactoglobulin jointly precipitate
(forming the curd structure). Cheeses made by acid coagulation have very high moisture contents, e.g., quarg,
possibly due to less protein rearrangements of the gel network (Lucey et al. 2003).

4. Post-coagulation procedures
After the curd has coagulated, it is cut into smaller, cube-shaped pieces in order to expel excess moisture
and whey from the protein network. When fresh curd is cut, the curd particles are easily deformed, improving
syneresis. The curd particles can then fuse together after expelling some water due to the protein in the curd (Vliet
andWalstra 1983). In practice, if the curd is cut when it is very soft, the network will shatter and fat will be lost,
decreasing yields, and altering. Conversely, if the curd is too firm when cut, the protein network will break and there

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will be high loss of casein, again, altering texture. Presumably, the change in the moisture content is a reflection of
the extent of bonding between and within casein particles, which increases with time texture (Johnson and Law
1999, Johnson et al. 2001).
After cutting, the curd is left alone for a short period known as a healing period. During the healing period, a
"skin" forms on the outside of the curd, which prevents further losses of fat and moisture. The curds are then stirred
and cooked in order to expel moisture and to promote shrinkage of the protein network (Brown, 2002).
After cooking, whey is drained from the curds. The pH of the whey determines the proportions of chymosin
and plasmin retained in the cheese (Fox, 1989). Both of these have the capability to cause breakdown of the
protein network during storage, which greatly affects the final texture of the cheese (Brown et al. 2003).
A number of steps may now occur depending upon the variety of cheese being made. For example, curds
are salted and matted together in a process known as cheddaring when making Cheddar cheese. This process
makes the protein network denser, resulting in a characteristic texture (Brown et al.2003).
In pasta-filata type cheeses, e.g., Mozzarella cheese, the curd is subjected to a stretching process in hot
water (>70°C). Cheese makers subjectively decide when the curd is suitable for stretching. This point depends on
many factors including the composition of the cheese and method used for acidification. The cooking and
stretching process helps to confer a plastic appearance to the curd and promotes the formation of a fibrous
structure. The heat treatment reduces the amount of residual rennet activity in the curd, which decreases the
amount of primary proteolysis that occurs during ripening (Taneya et al. 1992).
It is at this point that the altered curds are typically pressed into molds. If the curds are not salted, the molds
may be soaked in brine. Salt influences textural changes as the cheeses age. Such changes are most apparent in
brined cheeses, where immediately following molding; cheeses are immersed in a sodium chloride solution.
Osmotic pressure differences exist between the cheese and the brine, causing the sodium chloride to migrate into
the block; simultaneously, in order to maintain equilibrium osmotic pressure, moisture from the cheese block exits
into the brine (Guinee and Fox 1987). Madadlou et al. (2007) indicated that a higher brine concentration
increased the fracture stress and storage modulus of Iranian white cheese. It also modified the casein network
arrangement providing more homogenous protein aggregates.

5. Pasta filata process

Some varieties of cheese, most notably Mozzarella, are manufactured for functional properties rather than
for flavour. These types of cheese are commonly used by the food service sector as ingredients. Low-moisture
Mozzarella cheese is manufactured as a cheese ingredient, and is commonly known as pizza cheese. The freshly
made curd is stretched under hot water (typically between 55 and 80ºC) in a pasta filata (stretched curd) process to
impart desirable stretch and melting characteristics. The elongation of protein fibres and aggregated fat globules
and pools of fat in the direction of stretching can be seen by duallabelled CLSM (Rowney, et al., 2004, Ahmed et
al. 2011, Abd El- Gawad et al. 2012) Fig 1.

Fig. 1. Confocal micrograph of Mozzarella cheese showing the protein phase as red, the fat phase as blue,
and the serum phase as black; scale bar 25 mm (Everett and Auty 2008).

6. Cheese melting
Cheese meltability is improved by enhanced casein solvation, increased temperature, age, proteolysis, fat
and moisture levels. Sufficient casein hydration to promote interaction between caseins and the water phase is a
requirement for cheese to melt. Any factor that decreases casein–casein interactions will increase cheese
meltability. These include reducing the pH to around 5.2, maintaining a higher ratio of soluble to insoluble calcium,
and reducing total calcium by chelation, washing of the curd, preacidification of milk, or draining the curd at a lower
pH. Directly acidifying cheese milk rather than culturing will decrease the amount of bound calcium at the same pH.
Mozzarella cheese melts poorly below pH 5 due to incomplete fusion of casein aggregates (Kindstedt, et al.
2001). The effect on meltability and the proportion of soluble calcium is reversible over the pH range of 4.8–6.5
(Ge, et al. 2002). Although pH is known to affect meltability, this may be through the mechanism of altering the

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ratio of bound to soluble calcium. Total calcium is probably not as important as the bound calcium to casein ratio in
dictating melting characteristics (Lucey et al. 2003).
Casein solvation improves the meltability of Mozzarella cheese by enhancing casein–water interactions.
This interaction increases as the cheese ages due to a transfer of water from the bulk phase to the entrapped
phase. The casein phase has been argued to be more important than the fat in dictating melting behavior (Guinee
et al.1999, McMahon and Oberg1998).
Other factors that increase meltability include greater proteolysis (longer ripening time), higher levels of fat
and water (Tunick et al. 1993), using emulsifying salts in the case of process cheese, and increasing the level of
free oil (McMahon et al. 1999) which perhaps provides a lubricating role. Concentrating milk prior to cheese
manufacture or homogenising cheese milk will have an adverse effect on cheese melting. Fat globules coalesce in
cheese above about 60 ±1ºC, as observed by CLSM, and this coincides with an increase in the value of tand from
dynamic rheological measurements, concomitant with increased fluidity (Auty et al. 1999).

7. Free oil formation

The manufacture of pizza-style cheeses requires the application of heating and stretching, a process that is
likely to exacerbate unwanted formation of free oil when the cheese is heated on a pizza base. Although a certain
amount of free oil is necessary to prevent localised dehydration of the surface of cheese blisters, with associated
browning of the surface (Rudan and Barbano 1998), large amounts of oil on the cheese surface are unappealing
to the pizza aficionado.
A study by (Rowney et al. 2003) examined the effects of curd deformation and temperature on free oil
formation. Stretching curd to a greater extent in the pasta filata process increases the propensity for free oil
forming, whereas increasing the rate of stretching has a much smaller effect on free oil. Compression of curd has
little effect. Higher temperatures increase free oil, perhaps by promoting fat globule coalescence and rupture. In
conjunction with the salt-induced swelling of the casein matrix, the apparent viscosity of Mozzarella cheese
increases at higher salt levels due to partially inhibited proteolysis (Everett et al. 2004, Ahmed et al. 2011). This
might be expected to increase the propensity for fat globules to rupture as the casein matrix expands, however this
is not the case. The increase in viscosity is a much smaller effect than the swelling of the casein matrix during the
early stages of ripening, thus globules are protected against rupture by embedding into the soft casein fibers.

4. Cheese composition
Cheese composition also affects final texture. Cheeses having a higher fat content are less firm and more
elastic; the recently popular low fat cheeses are firmer and less smooth due to the increase in the amount of
protein matrix (and lack of lipid filler) (Mistry 2001). Beal and Mittal (2000) reported that hardness, gumminess,
and chewiness increased linearly, and cohesiveness and springiness decreased nonlinearly with fat content
decrease in Cheddar cheese. In UF-Feta cheeses, Fat globules are breakers of texture and hydrolysis of them
results in a uniform and homogenous texture. Wium et al. (2003) stated that the amount of fat distributed within the
cells of the protein matrix determines the ability of the cheese undergo deformation in response to stress, such that
an increase in the fat-to-protein ratio weakens the protein structure, thus increasing cheese flexibility.
The level of protein directly affects the firmness of the cheese; the more protein the cheese has initially, the
firmer the cheese is. The size of the protein aggregates seems more important in the matrices with the highest dry
matter content. The microstructure of the proteinic networks is much branched, denser and exhibits a higher
degree of cross-linking in the products containing the highest protein concentration (440 g/kg dry matter and/or
high fat/dry matter ratio). The microstructure of the matrices made with lower dry matter contents and fat (dry basis)
is coarser and fluffier (Fig 2).

(a) (b)

Fig. 2. Con focal microscopic observations of protein matrices:

(a) high dry matter content; (b) low dry matter content

Water exists in three main phases in cheese: bulk water in the serum channels, entrapped water in close
proximity to the casein matrix, or as bound water tightly associated adsorbed to the caseins and therefore
unavailable as a solvent. Heating and stretching fresh curd increases the proportion of mobile water molecules in
Mozzarella cheese (Kuo et al. 2003) and this is thought to represent the bulk water phase. In the first few weeks of

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ripening the proportion of entrapped water increases at the expense of bulk water, brought about by casein
swelling and hydration (McMahon et al. 1999). In addition, small variations in water content greatly affect firmness;
water content is affected by cheese making conditions and by surface evaporation during ripening (Adda et al.
1982). Lucey et al. (2003)reported that increasing the moisture content or increasing the ratio of moisture to
protein (nonfat substances) in cheese weakens the rigidity as the volume fraction of protein decreases and this
influences a wide range of textural characteristics. Visser (1996) stated that the stress at fracture decrease with
increasing moisture content at a given age of the cheese. In addition, Cheese functionality, i.e. melting temperature
and hardness, was associated with the mobility of water within the cheese matrix. Matrices in which the water was
more mobile, produced good melting, softer cheeses, while cheeses in which the water was more tightly bound
were brittle and non-melting (Noronha et al. 2008).
In proceed cheeses, the all textural properties, except adhesiveness and stringiness, are increased when
the moisture and fat content are reduced and when the protein content is increased. High levels of moisture and fat
content may be the cause for increased values of adhesiveness and stringiness when the protein content is low
(Dimitreli and Thomareis 2007).

1. Cheese ripening
Cheese ripening has a profound effect on texture and structure. Two phases of texture development during
storage have been identified. Phase one occurs within the first 7 to 14 days after production. During this time, the
rubbery texture of the young cheese is converted into the more smooth characteristic texture of the specific variety.
In this phase, hydrolysis of about 20% of the αs1-casien by residual coagulant occurs, as well as a redistribution of
water within the cheese network (Lawrence et al. 1987, McMahon et al. 1999, Brown et al. 2003). A more
gradual change in cheese texture occurs during phase two of ripening. It is during this period that the rest of the
αs1-casein and the other caseins are hydrolyzed. Unlike phase one, which takes only days, phase two occurs over
a period of months (Lawrence et al. 1987).
However, it has been shown that the β-casein does not change as much during ripening as αs1-casein
(Creamer and Olson 1982). It should be noted that in very old cheeses, some varieties (i.e. Cheddar) show highly
brittle texture. Several factors could explain such a change; as the cheeses age, evaporation of available water on
the surface occurs, causing a “drier”, more fragile cheese.
As proteolysis occurs, more and more “new” ionic peptides are created; as each “new” group is created,
competition for available water increases. Less water is available to solvate the protein chains and the resulting
cheese is harder and less deformable (Creamer & Olson, 1982). Changes in the texture of cheese can be related
to the rate at which proteolysis occurs; these reactions are affected by many things:
 Amount of residual coagulant: though most coagulant is lost in the whey when drained, some is
retained in the curd. If no active coagulant is present in the curd, then no αs1-casein degradation can occur,
and therefore, cheese softening will not happen (i.e. the cheese will maintain the young, rubbery texture)
(Lawrence et al. 1987). The amount of residual coagulant depends upon the pH of the system. Lower curd
pH at draining encourages retention of more rennet resulting in increased hydrolysis of αs1-casein.
 The pH at drain determines the amount of plasmin in the curd. Plasmin is associated with the
casein micelle in fresh milk, but as the pH decreases, they dissociate from the caseins. O’Mahony et al.
(2005) reported that proteolysis from residual chymosin, indigenous milk enzymes such as plasmin, and
proteases from starter bacterial cells and other microorganisms undoubtedly contribute to a softening of
cheese (Floury et al. 2009).
 The salt to moist. ratio (S:M): Sodium chloride (salt) is added to freshly made curd to limit the
action of starter bacteria from reducing the pH to unacceptably low values, and assisting in whey expulsion
immediately after curd milling (in the case of dry-salted cheeses), as well as the secondary effect of flavour
enhancement. A review of the effects of salt induce a swelling of the casein phase with subsequent
adsorption and absorption of moisture by the casein matrix, up to at least 1.6% NaCl in Mozzarella, as
shown by (Rowney et al. 2004). This has been observed with Mozzarella cheese and with Muenster
cheese (Pastorino, et al. 2003). The protein phase in unsalted cheese will swell at a slower rate compared
to salted cheese, and this explains the slower rate of reduction of expressible serum over time (Guo, et al.
1997). Such unsalted cheese has larger pockets of serum phase. Unsalted directly acidified Mozzarella
cheese contains a more porous protein matrix as a consequence of enhanced casein–casein interactions,
thus impaired meltability (Paulson, et al. 1998). The salt to moisture (S:M) affects the amount of intact
casein; at lower ratios, there is less intact casein than at higher ratios. Lawrence et al. (1987), Hort et al.
(1997) reported that after ripening at 10°C for 28 days, only 5% of the ά sl-casein but 50% of the β-casein
was still intact in that part of cheese with a S:M of 4.0%. At 6% S: M, 30% άsl-casein and 80% β-casein
remained intact. At 8% S: M, 60% of the άsl-casein and 95% of the β -casein was unhydrolyzed. The
relationship between the rate of degradation of both caseins and the S:M level was almost linear. In
addition, the salt to moisture ratio in the molded cheese also controls the activity of the residual rennet and
plasmin in the cheese [Brown 2002]. The compression modulus linearly increases with increasing salt
content. These results correlated with the chalky and brittle appearance of a high salt cheese and the more
smooth character of low salt in water cheese [Visser 1996].
 Ripening temperature affects the rate of proteolysis, though the impact on textural characteristics
depends upon the type of protein being proteolyzed. It is believed that αs1-casein hydrolysis contributes
more structurally to the cheese than the other caseins. At temperatures below 6°C, the amount of β-casein
hydrolyzed decreases significantly, but the amount of αs1-casein hydrolyzed only slightly decreases.
Therefore, cheeses of the same variety ripened at different temperatures below 6°C are not very different

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texturally. However, ripening temperatures above 10°C have significant effects on creating textural
differences since more αs1-casein is hydrolyzed as the temperature is increased. Cheese proteolysis is
negatively correlated with firmness, indicating softening of the cheese as the protein matrix is broken down
(Brown 2002).
 pH of cheese: Changes in pH during storage affect the rate of proteolysis. Cheeses having a low
pH (near the isoelectric point of casein) show a granular texture and shatter when deformed; higher pH
cheeses are more plastic and elastic. At low pH, strong ionic and hydrophobic intra aggregate forces hold
the casein aggregates in a compact formation. At higher pH, casein molecules have a net negative charge.
Though the hydrophobic interactions still exist, the ionic interactions change to a repulsive nature (Creamer
and Olson, 1982, Pastorino et al. 2003). Lawrence et al. (1987) reported that as the pH of cheese curd
decreases there is a concomitant loss of colloidal calcium phosphate from the casein sub-micelles and,
below about pH 5.5, a progressive dissociation of the sub-micelles into smaller casein aggregates (Fig. 3).
When the pH of the cheese curd approaches that of the isoelectric point of casein, the protein assumes an
increasingly more compact conformation and the cheese becomes shorter in texture. At pH below about 4.8,
the aggregates appear to exist only as nonlinear strands. These are 3 to 4 nm in width, roughly the diameter
of a spherical casein molecule, and up to 15 nm in length.

Fig. 3. Effect of pH on cheese texture (Lawrence et al. 1987)

 Calcium content: Both dissolved calcium in the cheese serum and calcium bound to the protein
network have been shown to affect the rate of proteolysis. Joshi et al. (2004) found that increasing the
amount of total (ionic plus insoluble) calcium in cheese enhances casein–casein interactions, thereby
reducing meltability and increasing cheese firmness.
 Mineral equilibrium: The mineral equilibrium within the cheese influences the texture. Calcium
acts to cement the casein micelles together. During maturation, calcium is transported from the center to the
outside of the cheese causing the core to have lower calcium content (Adda et al. 1982), leaving a softer
texture in the interior. The increase in pH in the cheese during ripening facilitates the action of plasmin,
contributing further to cheese softening. Thus, this type of cheese is said to ripen from the outside in
(Noomen 1983, Karahadian and Lindsay 1987) (Fig. 4). Sodium chloride affects both the matrix and the
serum phases of the cheese, which, in turn, affects the overall texture. It has been determined that sodium
chloride in the serum phase of Mozzarella cheese promotes the microstructural swelling of the para-casein
matrix resulting in an increased water-holding capacity and formation of a hydrated gel (Rowney et al.
2004). Simultaneously, the sodium
chloride promotes the solubilization of
intact caseins from the para-casein
matrix; it is hypothesized that these
proteins are able to freely migrate
between the matrix and the serum
phase (Guo and Kindstedt 1995, Guo
et al. 1997). The calcium phosphate
bridges that connect the bare casein
micelles in the protein matrix are affec-
ted in a process called demineraliza-
tion. The sodium ions are able to dis-
place the calcium ions in the calcium
phosphate bridge. This allows for
water in the system to be able to bind
to the complex, either increasing the
water holding capacity of the matrix, or
promoting the protein to become so-
luble in the serum (Paulson et al.
1998). Fig 4. Physical and chemical reactions during ripening of
Camembert and Brie cheese (Everett and Auty 2008)

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2. Freezing of cheese
Slow freezing of cheese produces large ice crystals, whereas rapid freezing produces smaller crystals.
Large crystals of ice candisrupt the cheese protein matrix, as shown by scan electro microscopic (SEM), and
increase the meltability of Mozzarella cheese (Oberg, et al. 1992). Large ice crystals can create serum pockets
within the protein matrix, as shown by the increase in water mobility by NMR measurements (Kuo et al. 2003).
Frozen Mozzarella cheese has a more porous protein structure, as shown by SEM, due to ice crystal formation
(Graiver et al.2004). The effect on frozen and thawed non-pasta filata cheese is similar to non-frozen pasta filata
cheese, in that both contain large pockets of trapped water. If the freezing rate is sufficiently fast to produce small
crystals, the impact upon protein matrix disruption may be minimal (Cervantes et al. 1983). Freezing has also
been shown to decrease ewes’ milk cheese firmness, presumably by reducing the density of casein cross-linkages
and creating a more porous cheese (Fontecha et al.1994) and quantified by a smaller value of G0.

4. CONCLUSION
 Many factors influence the texture of cheese including:
1. Manufacturing.
2. Procedure variety.
3. Composition and biochemical changes during ripening.
 The parameters have a major influence on the degree of hydration or aggregation, of the para-
casein matrix which is the major structural element controlling deformation on the application of a stress.
 Texture profile analysis is useful for examining general aspects of cheese texture.
 The functional properties of cheese ingredients are detected by the structure therefore knowledge
of how cheese structure is produced and develops during ripening is a great importent to cularly for Pizza-
style cheese, and included stretching, melting, browning, free oil development and expressible moisture,
amongst other attributes. The prediction and subsequent control of these properties an understanding
where the components of cheese are located in relation to each other, and how they interact and change
during ripening.

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