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4.1. Introduction
Cheese making can be described as the process of removing water, lactose and some minerals
from milk to produce a concentrate of milk fat and protein.
The essential ingredients of cheese are milk, coagulating enzyme (rennet), bacterial cultures
and salt. Rennet causes the milk proteins to aggregate and ultimately transform fluid milk to a
semi-firm gel. When this gel is cut into small pieces (curds), the whey (mostly water and lactose)
begins to separate from the curds. Acid production by bacterial cultures is essential to aid
expulsion of whey from the curd and largely determines the final cheese moisture, flavour and
texture.
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Fig. 4.1: Flowchart of cheese making processes
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4.2.1. Clarification of cheese milk
Clarification may be as simple as filtering out debris or may include removal of microbial cells
and spores. The principal clarification procedures are as follows.
(1) Cloth filters are common to remove debris at the farm but should not be necessary at the
processing plant
(2) Centrifugal clarifiers or medium speed centrifuges, remove particles which escape
filtration. Cream separators effectively double as centrifugal clarifiers because small
particles of debris collect at the periphery of the separator bowl and are ejected as sludge.
The loss of milk solids by this process is minimal
(3) Bactofugation is a high speed centrifugal process which separates bacterial cells and
spores such as Clostridium tyrobutyricum.
Bactofugation removes 95% of the spores of milk which means the risk of late gas defect
due to germination and growth of Clostridium tyrobutyricum is much reduced.
1-2% of milk solids is transferred to the bactofugate which, in particular contains casein
along with somatic cells and bacteria. To avoid yield loss the bactofugate which contains
12-16% of dry matter is sterilized by ultrahigh temperature processing and added back to
the milk.
(4) Microfiltration is a membrane process which has been used in a few European cheese
plants since 1985. Think of microfiltration as an ultrafine sieve. Microfiltration achieves
about 99% reduction of spore forming bacteria relative to 95% by bactofugation. The
disadvantage is that microfiltration can be applied only to skim milk because the milk fat
globules are too large to pass through the microfiltration membrane.
The addition of proteins to cheese milk during standardization has the advantage that it is
possible to produce cheese quantities beyond what's possible from the available fresh milk. This
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is significant in areas where fresh milk is in short supply or where milk purchases are limited by
quotas. Several sources of milk proteins are available for cheese milk standardization.
Most jurisdictions prohibit the use of non dairy fat in cheese. That leaves a number of choices:
Milk and cream unaltered other than by pasteurization and gravity or centrifugal
creaming.
Recombined cream prepared from skim milk and butter oil. This process requires
homogenization which is generally considered undesirable with some exceptions
including Feta, Blue and cream cheese.
Altered flavour, especially the absence of short chain fatty acids such as butyric which
are found in dairy fat. The flavour problem can be addressed by dairy flavour additives.
Preparation of filled cheese milk (filled means containing fat other than dairy fat)
requires homogenization, which as noted normally creates inferior texture.
The fat should have melting properties similar to butter fat.
Legally, it is recommended that cheese be made from pasteurized milk. However some other
heat treatment alternatives are possible and are practiced as outlined below.
If the milk is not fully pasteurized the resulting cheese is considered raw milk cheese: No heat
treatment results in raw milk cheese which has more flavor and is preferred by some consumers.
Raw milk cheese by law must be "held at 20C or more for a period of 60 days or more from the
date of the beginning of the manufacturing process. The question of raw milk cheese is an
ongoing concern to consumer groups and to health authorities.
Legally, it is recommended that cheese be made from pasteurized milk. However some other
heat treatment alternatives are possible and are practiced as outlined below.
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Thermisation
Thermisation (63-65°C, short hold) results in phosphatase positive milk which must be fully
pasteurized before cheese making. The purpose is to prevent raw milk spoilage (eg. over a
weekend) due to acid or protease or lipase producing psychrotrophic bacteria.
Pasteurization
Homogenization is desirable in cream cheese because it increases fat recovery and creates
smoother texture.
Homogenization reduces syneresis which is not desirable for hard cheese types
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Homogenization results in increased cheese yield due to greater moisture retention
(reduction of syneresis) and improved fat and protein recovery.
Culture, refers to prepared inocula of bacteria, yeasts and moulds which are added to cheese milk
and cheese. In the broadest terms cultures have two purposes in cheese making:
Lactic acid cultures contribute to both of these functions, while numerous special or secondary
cultures are added to help with the second function.
Development of Acidity
Raw milk at warm temperature will support a variety of micro-organisms in succession as the pH
changes over time. In controlled conversion of milk to fermented dairy products, a primary
component of fermentation is development of acidity by lactic acid bacteria. Acid development
in cheese making is absolutely essential to cheese flavour, cheese texture and cheese safety. Acid
is required to:
Assist coagulation: Lower pH results in faster coagulation (faster action of rennet) and in
acid coagulated cheese is the only factor which induces coagulation.
Promote syneresis: This is a most critical means of controlling moisture content. Acidity
(specifically reduced pH) causes the protein matrix in the curd to contract and squeeze
out moisture. That process of contraction is called syneresis.
Prevent growth of pathogenic and spoilage bacteria: Proper rate and extent of acid
development is the most important principle with respect to quality and safety of natural
cheese.
Develop cheese texture, flavor and colour
Assisting in ripening/curing
Growth factors produced by lactic cultures are required for other non-starter
microorganisms which contribute to the desired flavour and body of cheese
Enzymes (both lipases and proteases) produced by lactic cultures contribute to interior
ripening of cheese and are important to both flavour and texture development.
Lactic acid cultures used in cheese making are shown in the table below (Table 4.1).
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Table 4.1: Old and new Latin names for some common lactic cultures used in cheese making.
Mesophilic Cultures
Streptococcus Lactococcus lactis ssp As a mixed blend these two form the most
cremoris cremoris common mesophilic and homofermtative
culture.
Streptococcus Lactococcus lactis ssp Used for many low temperature varieties; fresh
lactis lactis cheese, Cheddar, American varieties etc.
Streptococcus Lactococcus lactis ssp Hetero culture; ferments citrate; produces both
diacetylactis lactis biovar diacetylactis CO2 and diacetyl
Mixed with homofermentative lactococci for
cheese with small holes
Thermophilic Cultures
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Addition of starter cultures to cheese milk: Inoculation
Cultures can be carried and prepared for cheese milk inoculation in one of three general formats:
Traditional starters which need several scale up transfers. This system requires some
microbiological facilities and expertise and is only feasible for very large plants or
perhaps for smaller plants which use mixed strain cultures.
Bulk set culture. In this system, the culture supplier does all the purification and transfer
work, and delivers a bulk set culture which is used to inoculate a bulk culture, which in
turn is used to inoculate the cheese milk. Bulk cultures are the norm in medium to large
plants because the cost savings are significant.
Direct to the vat cultures require no scale up at the cheese plant. Concentrated cultures
ready to inoculate the cheese milk are supplied directly by the culture supplier.
In addition to lactic acid cultures (primary starter cultures) many special or secondary cultures
are used to promote specific ripening (both flavour and texture) characteristics.
(1) Calcium Chloride is frequently added at a level of about 0.02% to aid coagulation and
reduce amount of rennet required.
(2) Nitrate (sodium or potassium nitrate) is added at levels of about 200 ppm to Edam,
Gouda, Swiss to inhibit growth of gas forming Clostridium tyrobutyricum.
(3) Annatto cheese color is added to some cheese to standardize seasonal changes in color or
to create orange cheese such as Cheddar, Gouda and Cheshire.
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(4) Decolorants: Goats' and sheeps' milk are flat white in color because they lack carotene.
Cows' milk may be whitened to mimic goats' or sheeps' milk. Legal whitening agents
include:
Titanium dioxide
Chlorophyll based products which mask the natural yellow colour. Excess chlorophyll
makes green cheese.
(5) Ripening Agents: A wide range of products are available to accelerate cheese ripening or
to develop a broader flavour profile.
Lipases (lipolytic enzymes) are traditionally added to cows' milk to produce cheese such
as Feta, Romano, Kefalotyri, and Parmesan which are traditionally made from goats' or
sheeps' milk. That's because goats' and sheep's milk, especially goats' milk, have more
natural lipase than cows' milk. Commercial lipases are commonly extracted from kid
goats.
Enzyme Cocktails: Mixtures of enzymes from various sources added to the milk to
accelerate ripening of aged cheese such as Cheddar. These cocktails include both lipases
and proteases, with a predominance of proteases for Cheddar. Bacterial enzyme extracts
from lactic acid bacteria have also been used.
Coagulation is what happens when the casein micelles precipitate and stick together. Because
casein particles are hydrophobic (they hate water) their natural tendency is to aggregate (clump
together). In normal milk, aggregation is prevented by two factors. If one of these factors is
eliminated, the casein micelles will aggregate and form a gel.
The first stabilizing factor is a 'hairy' layer of surface active protein, called kappa-casein
(κ-casein), on the surface of the casein micelle. This layer (which is also hydrophilic)
helps prevent the micelles from getting close enough to stick together.
The second factor is a negative charge on the micelles. At the normal pH of milk (6.6 –
6.8) the micelles are negatively charged so they repel each other.
So, basically there are two ways to coagulate milk: one is to remove the hairy layer from the
casein micelles: That's called enzymatic coagulation. The other is to neutralize the negative
charge on the micelle: That can be accomplished by acidification (already discussed in
“Fermented milks”) or a combination of high temperature and acidification.
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A. Enzymatic milk coagulation
In the first stage, the enzyme (rennet/chymosin) cuts off a specific fragment of one of the
caseins, namely, κ-casein. Specifically the enzyme, rennet/chymosin, cuts κ-casein between
Phe(105)-Met(106) (Fig. 4.2).
The next stage is the physical process of aggregation of casein particles (micelles) to form a gel
(Fig. 2.3). After losing its water soluble tail, κ-casein can no longer keep the casein particles
separated, so they begin to form chains and clusters. The clusters continue to grow until they
form a continuous, three dimensional network which traps water inside, and forms a gel.
Fig. 4.2: The first stage of coagulation whereby Rennet/chymosin cuts κ-casein exactly and
specifically between Phe(105)-Met(106). The results are two fragments: para- κ-casein which is
hydrophobic and will form the coagulate and caseino-macropeptide or glycomacropeptide
which is hydrophilic and will be lost with whey.
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Fig. 4.3: Highlighted with a yellow rectangle is the physical process of aggregation of casein
particles (micelles) to form a gel.
Because rennet coagulation takes place in stages, it is necessary to understand the effect of
processing on each stage (the first and second stages of milk coagulation).
Effect of pH. Lower pH increases enzyme (rennet) activity and neutralizes charge repulsion
between casein micelles. Therefore, both primary and secondary stages of coagulation proceed
more quickly at lower pHs.
Effect of Calcium. Calcium is not required for the primary stage (i.e., enzyme hydrolysis of κ-
casein) but is essential to aggregation of the casein micelles. At low levels of calcium the
primary phase goes to completion. Subsequently, instantaneous coagulation can be induced by
adding sufficient calcium chloride.
Effect of temperature. The optimum coagulation temperature for most cheese types is 30-32°C,
the exception is Swiss cheese type which is set at 37°C.
At temperature less than 30°C the gel is weak and difficult to cut without excessive yield
loss due to fines.
At temperatures less than 20°C coagulation does not occur, but the primary stage goes to
completion and the milk will then coagulate quickly when warmed.
Heat treatment in excess of pasteurization results in increased clotting time and a weak gel. High
heat treatments cause absorption of whey proteins onto the casein particles. The casein particles
are then unable to form a strong gel.
Effects of Homogenization. The following effects occur if the cheese milk is homogenized in its
entirety. Some of these results may be different if only the cream is homogenized and then added
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back to the skim milk. Homogenization primarily affects the secondary phase of aggregation.
Some cheese quality effects are also noted.
Coagulating enzymes
The traditional enzyme for cheese making is rennet (specifically, chymosin) which is derived
from the abomasum of the milk fed calf. The practice of cheese making probably began when
somebody discovered that milk stored in bags made from calf stomachs formed a sweet curd.
Other proteases (known as milk clotting enzymes or coagulants) have been or are being used for
cheese making (Table 4.2). Because there are now several different types and sources of milk
clotting enzymes on the market, the International Dairy Federation (IDF/FIL) official definitions
decree that the name 'rennet' be reserved for enzyme preparations from ruminant stomachs, and
other milk clotting enzymes (mainly the microbial ones) should be named 'coagulants'.
Table 4.2: Main types and sources of milk-clotting enzymes (rennets and coagulants) used in
cheese making
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Animal rennets: Of the animal rennets, calf rennet is widely regarded as the ideal milk-clotting
enzyme for cheese making. This preference arises partly through traditional familiarity with the
product through long use, but also has a sound scientific basis in that calf rennet is typically 80-
90% chymosin (EC 3.4.23.4). This means that most of the casein breakdown in the cheese vat is
directed very specifically at kappa-casein to clot the milk, and not at the other caseins. Non-
specific proteolysis of alpha- and beta-casein during curd formation can result in the loss of
casein nitrogen in the whey, reducing the yield of the cheese process.
The second enzyme in calf rennet, pepsin (EC 3.4.23.1), is thought by traditional cheesemakers
to add to the ripening qualities of rennet in maturing cheese, but there is no hard evidence for
this. Indeed, cheesemakers now make excellent quality long-hold cheeses (especially Cheddar)
using pure chymosin from genetically modified yeasts and fungi expressing cloned copies of the
calf pro-chymosin gene.
Sheep, goats and pigs can provide rennet preparations that are enzymatically similar to calf
rennet, but not ideally suited to clotting cows' milk. Rennet 'paste' is a crude form of rennet made
from the macerated stomachs of suckling calf, lamb or kid, and containing pregastric lipase to
add piquancy to the flavor of the cheese. It is mainly used in traditional Italian cheeses.
Plant coagulants: Many plants produce proteinases that clot milk. However, plant coagulants
are not produced on a commercial scale, but made locally (mainly in Portugal) for artisanal
cheesemaking.
Microbial coagulants: The best-known and most widely used microbial coagulant is that
produced (naturally and not genetically produced) from Rhizomucor miehei (table 4.2). The
commercial preparation is a mixture of aspartyl proteinases (EC 3.4.23.23).
Although this has been used successfully to make soft, short-hold cheese varieties, its non-
specific proteolytic action reduces yields of cheeses whose curd spends a long time in the whey
(hard and semihard cheese), and caused bitterness in long-hold cheeses. The heat resistance of
the enzyme is also a potential drawback in cheese plant from which the whey is processed as a
food ingredient. The heat treatment and processing does not eliminate the activity of the
coagulant and it can cause protein breakdown in other food products in which whey protein is a
supplementary ingredient (e.g. sausages, meat pies, soups).
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Also the flavour profile of hard cheese made with fungal rennet is not the same as that of
chymosin-made cheese. The most widely used alternative to calf rennet in the cheese industry
worldwide is fermentation-produced chymosin (FPC). It is produced by large-scale
fermentation of genetically modified Kluyveromyces lactis orAspergillus niger. In both cases the
microorganism has been modified using gene technology by the incorporation of the pro-
chymosin gene from the calf into the host organism with a suitable promoter to ensure its
efficient secretion into the growth medium. The enzyme is relatively easy to harvest and purify
from the culture.
B. Acid coagulation
As it can be observed from Fig. 4.1, some cheese types are acid-coagulated with little or no
addition at all of rennet. Acid milk gels can be formed solely by lactic acid bacteria or the use of
acidifying agents such as glucono-delta-lactone (Fig. 4.4) (GDL is slowly hydrolysed to gluconic
acid in the presence of water).
Acid coagulation is used for example in the production of cottage cheese (Fig. 4.5) and quark
cheese (Fig. 4.5) as well as other fermented milk products such as yoghurt, commercial butter
milk, kefir etc. In the case of cottage cheese and quark a small amount of chymosin may be used
(2 ml/1,000 hl) to make the curd more elastic and less subject to breakage.
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Fig. 4.5: Cottage cheese (left) and Quark cheese (right)
C. Heat-acid coagulation
For another group of cheese, coagulation is not realized with rennet or acid, but by a combination
of heat and acidification. This process permits recovery of caseins and whey proteins in a single
step. The basic principle is that whey proteins which are normally acid stable, become sensitive
to acid coagulation after heat treatment. This principle is exploited in the manufacture of ricotta
cheese (Fig. 4.6), Paneer and Channa, and in the manufacture of "co-precipitated" milk protein
concentrates. The basic process for heat-acid coagulation is:
Heat milk or milk-whey blends to at least 80°C for at least 5 minutes to completely
denature (unfold) the whey proteins and encourage association of whey proteins with
casein micelles.
Continue heating and acidify slowly with gentle agitation. The caseins and whey proteins
will coagulate together and form either sinking or floating curds.
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4.2.8. Cutting the cheese curd (after coagulation)
Proper cutting of the curd is extremely important to both quality and yield. Improper cutting and
improper handling of the curd result in the loss of fines, that is, small curd particles which are not
recovered in the cheese.
Both early cutting when the curd is fragile and late cutting when the curd is brittle cause losses of
fines. Several means are used to determine cutting time.
Manual testing. The curd is ready to be cut if it breaks cleanly when a flat blade is
inserted at 45o angle to the surface and then raised slowly (Fig. 4.7).
Some plants cut by the clock. This may be OK as long as all conditions are uniform from
day to day (which is not easy) and adjustments are made for any change in milk
composition or properties.
If setting temperature is high as for Swiss cheese types, the curd firms rapidly and cutting
must begin early when curd is still somewhat soft to prevent over setting. Agitation
should begin immediately to prevent matting.
Fig. 4.7: The manual test that can be carried out to determine whether it is the right time to cut
the formed curd. The curd is ready to cut if it breaks cleanly when a flat blade is inserted at 45 o
angle to the surface and then raised slowly.
Curd size
Curd size has a great influence on moisture retention. Hence, there is an obvious relationship
between cheese moisture and the prescribed curd size:
High temperature and low moisture varieties such as Italian hard cheese require the
smallest curd. Cutting continues until the curd cutting is the size of rice grains.
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Medium moisture cheeses like most washed varieties and Cheddar are cut into small
cubes.
High moisture varieties like soft ripened cheese are cut with 2 cm knives or the curd is
simply broken sufficiently to be dipped into forms.
Small curd size will result in greater fat and SNF recovery because large curds tend to get
crushed resulting in the loss of 'fines'. Smaller curds will also dry out faster and, therefore, other
factors such as cooking temperature and stirring out may have to be adjusted according to curd
size.
Cutting
Curd cutting can be done either manually (with cutting harps, made by stretching stainless steel
wire over a stainless steel frame, Fig. 4.8) or mechanically (with mechanical knives, Fig. 4.8).
Total cutting time should not exceed 10 minutes (preferably less than 5 minutes) because the
curd is continually changing (becoming overset) during cutting.
Fig. 4.8: Mechanical curd cutting (left) and manual curd cutting (right)
The combination of heat and the developing acidity (decreasing pH) causes syneresis with
resulting expulsion of moisture, lactose, acid, soluble minerals and salts, and whey proteins. It is
important to follow the cooking schedule, closely. Cooking too quickly causes the curd to shatter
more easily and forms a tough exterior on the curd particles which prevents moisture release and
hinders development of a smooth texture during pressing. Cooking is combined with stirring
(Fig. 4.9).
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Fig. 4.9: Cooking and stirring of the curds
Most cheese is drained in the range of whey pH 6.1-6.4 (curd pH 6.0 - 6.3). Draining time should
be uniform at about 20 min to prevent variation from vat to vat. Cheddar cheese types may be
stirred out 1 to 3 times as required to obtain required curd moisture. Whey drainage is carried out
in a variety of ways (Fig 4.10).
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Fig. 4.10: Different ways that are used to drain whey out from the curds.
Lactose content can be adjusted by moisture removal (syneresis), fermentation, or leaching with
water (=washing).
By leaching lactose with water it is possible to make a high moisture cheese (such as brine brick
cheese or Muenster cheese) and still achieve a final pH of about 5.0 - 5.2. The temperature of the
wash water will determine the moisture content of the curd. Sometimes relatively hot water (eg.,
Gouda cheese) is used to dry the curd and develop its texture.
Traditionally washing was accomplished by removing about 2/3 of the whey and replacing it
with water and agitating for about 15 min.
4.2.12. Salting
Almost all cheese types is salted by one of three methods: before pressing (Fig. 4.11) as in
Cheddar and American varieties, surface salting after pressing (Fig. 4.11), or brine salting by
dipping cheese in a brine solution (Fig. 4.11).
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Purposes of Salting
Fig. 4.11: Cheese salting: Dry salting or salting before pressing (left); surface salting after
pressing (middle) and Brine salting (right).
4.2.13. Pressing
Pressing varies from little or none for soft cheese up to 172 kPa for firm Cheddar cheese. The
warmer the curd, the less pressure required. Mechanical openings may be reduced by vacuum
treatment before, during or after pressing. Pressing can be carried out in a variety of ways (Fig.
4.12)
Fig. 4.12: Different ways that are used to press cheese: removing the remaining moisture and
giving shape to the cheese.
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4.2.14. Ripening
Cheese ripening is basically about the breakdown of proteins, lipids and carbohydrates (acids and
sugars) which releases flavour compounds and modifies cheese texture. Here we include a few
practical principles behind the biochemical processes of ripening.
Protein degradation during cheese ripening is a directed process resulting in protein fragments
with desirable flavours.
Some off flavours associated with undesirable or excessive protein breakdown in cheese
are bitter, stringent, putrid and brothy.
Protein breakdown causes shorter body which is less rubbery, less elastic, more meltable.
For example, flavour and texture development in Cheddar are mainly dependent on
protein breakdown and much less dependent on fat breakdown.
Protein breakdown involves three general types of processes:
o Proteases break proteins into smaller peptides, some of which are flavour
compounds. For example, bitter and brothy flavoured peptides are well known to
occur in cheese.
o Peptidases further break down peptides to amino acids.
o Further catabolism of amino acids by cheese microorganisms produces aldehydes,
alchohols, carboxlic acids and sulfur compounds, many of which are flavourful.
The amino acid, tyrosine, forms crystals in aged cheese such as Parmaggiano regiano,
which are readily detected on the palate.
Dairy fat is a wonderfully rich source of flavours, because it contains an extremely diverse
selection of fatty acids. In particular, butter fat is the only natural fat which is rich in short chain
fatty acids. Butyric acid for example is a potent flavour compound. As with all potent flavours
the trick is to add just the right amounts in balance with other flavours. Here are a few principles:
Dairy fat without any ripening during cheese making is an important contributor to
cheese flavour and texture:
o Fresh dairy fat has the well-known 'buttery' flavour associated with extremely low
levels of free fatty acids.
o Fat also acts as a flavour reservoir, so hydrophobic (fat soluble) flavours derived
from protein breakdown are stored in the fat and released during mastication in
the mouth.
o Finally, fat is an important component of cheese softening and melting.
The fat derived flavours associated with cheese ripening result from the release of fatty
acids by lipolysis and further modification of fatty acids by microorganisms to other
compounds.
Varieties traditionally made from goats' milk have higher levels of lipolysis.
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Blue moulds are generally quite lipolytic
Lactose
Milk contains no starch or fibre or any sugar other than lactose so all carbohydrate compounds in
cheese are derived from lactose or produced by microorganisms. Relative to fat and protein
lactose contributions to flavour are minimal.
Milk Enzymes
Plasmin: A milk protease which survives pasteurization and breaks down caseins during
cheese ripening.
o Particularly important in Swiss type cheese.
o Inhibited by Beta-lactoglobulin, so it has minimal activity in cheese made from
ultrafiltered milk.
Lipoprotein lipase is the principal milk lipase
o Inactivated by low heat treatment but is important to flavour development in raw
milk cheese
Milk Coagulant
Each milk coagulant has its own proteolytic profile (see section on coagulants).
Purified extracts produce more consistent flavours but lack character.
For aged cheese no enzyme other than calf rennet and recombinant calf rennet has proven
fully acceptable.
Rennet and recombinant rennet actively break down alpha-casein but do not break down
beta-casein in cheese.
Lactic Cultures
During the early days and weeks of ripening, LAB numbers decrease while the numbers
of non-starter bacteria decrease. For example, in Cheddar cheese, LAB counts reach a
maximum (up to 500 million per gram) within 3-4 days and then decrease to about 20
million at 4 weeks. However, the dying cells release enzymes which continue to ripen the
cheese.
Lactic cultures contribute to proteolysed flavours but are minimally lipolytic
Heterofermentative cultures ferment citrate as well as lactose and contribute both flavour
(diacetyl) and carbon dioxide for small eye development
Secondary Cultures
Non-starter Microorganisms
Bulk cooling and storage of raw milk selects for cold tolerant (psychrotrophic) bacteria
Heat treatment selects for thermal stable spore forming bacteria
Non-starter bacteria commonly present in heat-treat Cheddar include Lactobacillus sp.
and Pediococci sp.
Many other bacteria and yeasts may be present and may or not grow depending on
complex symbiotic relationships with other bacteria.
Heat treat is really a process of standardizing the nonstarter microorgansims, namely,
eliminate proteolytic psychrotrophic bacteria but retain a range of useful ripening
microbial agents.
Non-starter bacteria in cheese milk can be reduced by microfiltration.
Addition of lipases as noted earlier is common for Italian and other cheese varieties. The
principal areas of continuing development are:
There are many different ways of classifying cheese types. Table 4.3 gives one such
classification.
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Table 4.3: Cheese families. For each cheese family, an example, the type of coagulation, the
moisture range, the pH range and the ripening period length are given.
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