512 10 Milk and Dairy Products
Hence, the monomer is stable only at a pH
less than 3.5 or above 7.5. The octamer oc-
curs with variant A, but not with variants B
and C. Irreversible denaturation occurs at a pH
above 8.6aswellasbyheatingorathigherlevels
of Ca^2 + ions. β-lactoglobulin has 5 cysteine
residues, one (Cys^121 , Table 10.8) of which
being free. In the native protein, however, this
cysteine is buried within the structure. This SH
group is exposed on partial denaturation and
can participate either in protein dimerization via
disulfide bridge formation or in reactions with
other milk proteins, especially withκ-casein and
α-lactalbumin, which proceed during the heating
of milk.
α-Lactalbumin(Mr 14 ,200). This protein exists
in two genetic forms, A and B (Gln→Arg).
It has 8 cysteine residues. Its amino acid se-
quence (Table 10.8), which is similar to that of
lysozyme, has been elucidated. Disulfide bonds
and a Ca^2 ⊕ion participate in the stabilization
of the tertiary structure. α-Lactalbumin has
a biological function since it is the B subunit
of the enzyme lactose synthetase. The enzyme
subunit A is a nonspecific UDP-galactosyl trans-
ferase; the subunit B makes sure that the transfer
of the galactose residue can occur at the low
glucose concentration present in mammals. The
affinity of the transferase alone for glucose is too
low (Km=2mol/l). It is increased 1000 fold by
cooperation withα-lactalbumin.
10.1.2.2 Carbohydrates
The main sugar in milk is lactose, an O-β-
D-galactopyranosyl-( 1 → 4 )-D-glucopyranose,
which is 4–6% of milk.
The most stable form isα-lactose monohydrate,
C 12 H 22 O 11 ·H 2 O. Lactose crystallizes in this
form from a supersaturated aqueous solution at
T< 93. 5 ◦C. The crystals may have a prism-
or pyramid-like form, depending on conditions.
Vacuum drying at T> 100 ◦C yields a hy-
groscopic α-anhydride. Crystallization from
aqueous solutions above 93. 5 ◦C provides water-
freeβ-lactose (β-anhydride, cf. Formula 10.10).
Rapid drying of a lactose solution, as in milk
powder production, gives a hygroscopic and
amorphous equilibrium mixture of α-and
β-lactose.
(10.10)Some physical data of lactose are summarized in
Table 10.15. The ratio of anomers is temperature
dependent. As temperature increases, theβ-form
decreases. The mutarotation rate is temperature
(Q 10 = 2. 8 )and pH dependent (Fig. 10.12). The
rise in mutarotation rate at pH<2 and pH> 7
originates from the rate-determining step of ring
opening, which is catalyzed by both H+and OH−
ions:(10.11)Fig. 10.12.Mutarotation rate of lactose as affected by
pH