Food Chemistry

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10.3 Aroma of Milk and Dairy Products 543

characteristic sour/pungent taste, which is inten-
sified by lactic acid. The two furanones HD3F
and EHM3F probably contribute to the nutty
note. Model experiments show that lactic acid
bacteria (Lactobacillus helveticus, Lactobacillus
delbrueckii) are involved in the formation of
HD3F.
At the Emmentaler pH of 5.6, magnesium
(threshold value: 3.5 mmol/kg) and calcium
propionate (7.1 mmol/kg) taste sweet. Conse-
quently, it is assumed that these propionates
contribute to the sweet note. On the other
hand, glutamic acid is an important taste sub-
stance, which has the additional function of
neutralizing the bitter taste of amino acids
and peptides. Only if the concentrations of
these constituents climb too high on longer
ripening of Emmentaler, the effect of glutamic
acid is no longer sufficient and the bitter taste
appears. An off-flavor can also be formed if
there is a greater increase in the fatty acids
4:0–12:0.
The caseins are increasingly degraded during
longer ripening. Water-soluble peptides and
amino acids are formed which bind a part of the
ions. Thus, when chewing a cheese ripened for
a long time, the water-soluble portion of the ions
increases, possibly causing an intensification of
the salty taste.
It is probable that not only peptides, but also
other amides are responsible for the bitter taste
of cheese. For example, the presence of bitter
N-isobutyl acetamide has been detected in
Camembert cheese.


10.3.6 Aroma Defects


As already indicated, aroma defects can arise in
milk and milk products either by absorption of
aroma substances from the surroundings or by
formation of aroma substances via thermal and
enzymatic reactions.
Exogenous aroma substances from the feed or
cowshed air enter the milk primarily via the respi-
ratory or digestive tract of the cow. Direct absorp-
tion apparently plays only a minor role. Metabolic
disorders of the cow can cause aroma defects,
e. g., the acetone content of milk is increased in
ketosis.


The oxidation of lipids is involved in the endoge-
nous formation of aroma defects. While very low
concentrations of certain carbonyl compounds,
e. g., (Z)-4-heptenal (1 μg/kg), 1-octen-3-one,
and hexanal, appear to contribute to the full
creamy taste, increased concentrations of these
and other compounds produce cardboard-like,
metallic, and green aroma notes. In butter, for in-
stance, the phospholipids of the fat globule mem-
brane are especially susceptible to oxidation. The
subsequent products get distributed in the entire
fat fraction and cause taste defects which range
from metallic to fatty and from fishy to tallowy.
Light can cause the degradation of methionine to
3-methylthiopropanal via riboflavin as sensitizer.
Together with other sulfides and methanethiol,
this sulfur compound produces the aroma defect
of milk and milk products called “light taste”.
A series of aroma defects are caused by enzy-
matic reactions. These include:


  • An unclean taste due to an increased concen-
    tration of dimethylsulfide produced by psy-
    chotropic microorganisms.

  • A fruity taste due to the formation of ethyl
    esters produced by psychotropic microorgan-
    isms, e. g.,Pseudomonas fragii.

  • A malty taste due to increased formation
    of 3-methylbutanal, 2-methylbutanal, and
    methylpropanal byStrept. lactis var. malti-
    genes.

  • A metallic taste in buttermilk due to (E,Z)-2,6-
    nonadienol in concentrations> 1 .3μg/l. The
    precursor is the triglycerol-boundα-linolenic
    acid which is oxidized to 9-hydro-peroxy-
    10,12,15-octadecatrienoic acid by oxygenases
    from the starter culture. Proton catalysis lib-
    erates (E,Z)-2,6-nonadienal which is reduced
    to the corresponding alcohol by lactic acid
    bacteria.

  • A phenolic taste due to spores ofBacillus cir-
    culans.

  • A rancid taste due to the release of lower fatty
    acids (C 4 –C 12 ) by milk lipases or bacterial li-
    pases.

  • A bitter taste can occur due to proteolytic ac-
    tivity, e. g., on storage of UHT milk. The milk
    proteinase plasmin is inactivated on intensive
    heating (142◦C,>16 s). However, some bac-
    terial proteinases can still be active even after
    much longer exposure to heat (142◦C, 6 min).

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