Journal of Food Engineering 48 (2001) 19±31

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Water sorption isotherms of foods and foodstu€s: BET or GAB

parameters?
E.O. Timmermann a, J. Chirife b,*, H.A. Iglesias b
a 
Facultad de Ingenierõa, Universidad de Buenos Aires, and PRograma de INvestigaciones en SOlidos (PRINSO), CITEFA-CONICET,
Zufriategui 4380, 1603 Villa Martelli, Provincia de Buenos Aires, Argentina
b
Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria,
1428 Buenos Aires, Argentina
Received 3 March 2000; accepted 8 August 2000

Abstract
The aim of the present work is to solve the dilemma about the di€erences between the values of the monolayer and the energy
parameters obtained by the regression of water sorption data by foods and foodstu€s using the Brunauer, Emmett and Teller (BET)
two-parameter isotherm or the Guggenheim, Anderson and de Boer (GAB) three-parameter isotherm. It is shown that the GAB
values are more general and have more physical meaning, and that the two BET parameters can be calculated in terms of the three
GAB-parameters. Furthermore, the marked dependency of the BET constants on the regression range as well as the typical upswing
at higher water activities observed in the so-called BET plots are explained. It is also shown that the rough agreement early reported
by L. Pauling, J. Am. Chem. Soc. 67 (1945) 555±557 between monolayer values and number of polar groups in the aminoacid side
chain in several proteins is enhanced if the former are evaluated by means of the GAB sorption equation. Ó 2001 Elsevier Science
Ltd. All rights reserved.

Keywords: Sorption isotherms; Monolayer values; Energy constants; BET equation; GAB equation; Proteins

1. Introduction Weisser, 1985; Maroulis, Tsami, Marinos-Kouris, &

In the past, the well-known Brunauer, Emmett and
Teller (BET) sorption isotherm was the model that had
the greatest application to water sorption by foods and
foodstu€s (Labuza, 1968; Iglesias & Chirife, 1976a),
although it was known to hold only for a limited range
of water activity (aw ), up to only 0.3±0.4. Two familiar
constants are obtained from the BET model, namely the
monolayer moisture content, xmB , and the energy con-
stant, cB . Despite the theoretical limitations of the BET
adsorption analysis, the BET monolayer concept was
found to be a reasonable guide with respect to various
aspect of interest in dried foods (Karel, 1973; Iglesias &
Chirife, 1982).
In more recent years, the Guggenheim, Anderson and
de Boer (GAB) isotherm equation has been widely used
to describe the sorption behavior of foods (Bizot, 1983;
*
Corresponding author. Fax: +54-1-7943344.
E-mail addresses: etimmer@citefa.gov.ar (E.O. Timmermann),
jchirife@satlink.com (J. Chirife).
0260-8774/01/$ - see front matter Ó 2001 Elsevier Science Ltd. All rights reserved.
PII: S 0 2 6 0 - 8 7 7 4 ( 0 0 ) 0 0 1 3 9 - 4
Saravacos, 1988; Iglesias & Chirife, 1995). Having a
reasonable small number of parameters (three), the
GAB equation has been found to represent adequately
the experimental data in the range of water activity of
most practical interest in foods, i.e., 0.10±0.90. The
GAB equation has been recommended by the European
Project Group COST 90 on Physical Properties of
Foods (Wolf, Spiess, & Jung, 1985) as the fundamental
equation for the characterisation of water sorption of
food materials.
Both isotherms (BET and GAB) are closely related as
they follow from the same statistical model (Timmer-
mann, 1989). By postulating that the states of water
molecules in the second and higher layers are the same
as each other but di€erent from that in the liquid state,
the GAB model introduced a second well-di€erentiated
sorption stage for water molecules. This assumption
introduces an additional degree of freedom (an addi-
tional constant, k) by which the GAB model gains its
greater versatility. One of the three GAB constants is, as
in the BET equation, the monolayer capacity now de-
noted by xmG . The other two GAB constants, denoted
20 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31
by cG and k, are energy constants as the BET constant
cB , but with slighly di€erent physical meanings. The
BET constant cB is related logarithmically to the dif-
ference between the chemical potential of the sorbate
molecules in the pure liquid state and in the ®rst sorp-
tion layer. On the other hand, the GAB constant cG is
related to the di€erence of this magnitude in the upper
layers and in the monolayer, while the constant k is
related to this di€erence in the sorbate's pure liquid state
and in the upper layers, and the product of both
(cG k ˆ cB…G† ) represents the equivalent to cB of BET. It is
to be mentioned that the third GAB constant k is,
practically without exception, near to but less than unity
(Chirife, Timmermann, Iglesias, & Boquet, 1992), a fact
which constitutes a de®nitive characteristic of this iso-
therm (Timmermann, 1989).
Now, if both isotherms (BET and GAB) are used
for regression analysis of sorption data, two sets of
values of the monolayer capacity and of the energy
constant are obtained, which should be comparable.
However, it has been observed by several authors (van
den Berg, 1981; Kim, Song, & Yam, 1991; Duras &
Hiver, 1993; Lagoudaki, Demertzis, & Kontominas,
1993) that
xmB …BET† < xmG …GAB†; cB …BET† > cB …GAB†: …
That is, the monolayer capacity by BET is always less
than the GAB value, while the energy constant cB by BET
is always larger than the GAB value. These inequalities
set up the dilemma, about which values resemble a better
physical reality, a dilemma not solved so far.
Following a general approach given elsewhere by one
of us (Timmermann, 2000), it will be shown here that
there exits mathematical (and physical) reasons for the
inequalities set by Eq. (1) and that the GAB values are
the values of better physical reality. For this purpose,
several experimental data for water sorption in foods
and foodstu€s are analysed and in each case, the in-
equalities (Eq. (1)) are qualitatively and quantitatively
explained. Hydration of proteins, in terms of the at-
tachment of one water molecule to each polar group of
the side chains of the aminoacids (Pauling, 1945), is also
discussed in terms of the BET and GAB monolayer
values.
2. BET regression vs GAB regression
2.1. The BET isotherm
The classical BET equation, giving the amount of
water x(aw ) sorbed by a unitary amount of sorbant in
terms of the water activity aw , is the following:
BET : x…aw † ˆ xmB cB aw =‰…1 ÿ aw †…1 ‡ …cB ÿ 1†aw †Š: …
It is well known that the two constants, the monolayer
value xmB and the energy constant cB , are obtained from
the so-called BET plots (Iglesias & Chirife, 1976a). In
synthesis, in these plots, the linearised form, F(BET), of
this isotherm
F…BET†  aw =‰…1 ÿ aw †x…aw †Š
ˆ 1=cB xmB ‡ ‰…cB ÿ 1†=cB xmB Šaw …3†
is drawn in terms of aw . This function should be linear if
the BET assumptions apply, and within the linear range,
using a linear least-square analysis, F(BET) is adjusted
by a linear polynomial
P…BET†i ˆ a0 ‡ a1 xi …4†
by minimising the squares sum over the n experimental
points (index i)
X
iˆn
 2
F…BET†i ÿ …a0 ‡ a1 xi † ˆ minimum; …5†
iˆ1
where xi stands for aw at the point i. The coecients a0
and a1 are given by the solutions of the system of normal
equations associated to the extremum condition (5).
According to Eqs. (3) and (4), the least-squares esti-
mates of a0 and a1 , a^0 and a^1 , are related to the BET
1†
constants by
a^0  1=cB xmB ; a^1  …cB ÿ 1†=cB xmB …6†
and herefrom
   
xmB ˆ 1= a^0 ‡ a^1 ; cB ˆ a^0 ‡ a^1 =^
a0 …7†
relations by which the BET constants are calculated. It
should be noted that the energy constant cB is in-
versely proportional to the intercept a^0 of the linear
regression polynomial P(BET) of Eq. (3) and, there-
fore, cB is very sensitive to the value of a^0 , which is
usually very low.
Usually, and this was observed by many workers, the
BET plots give only an apparent linear plot at low
water activities (0.05 < aw < 0.3±0.4) and over this range
the BET regression is performed (Iglesias & Chirife,
1976a). For aw > 0.3±0.4, always deviation from linear-
ity is observed with an upswing of F(BET) indicating
that at higher water activities less water is sorbed than
that predicted by the BET equation as shown in Fig. 1
for the BET plots of water sorption for various food
materials.
2.2. The GAB isotherm
On the other hand, the GAB equation is
GAB :
2† x…aw † ˆ xmG cG kaw =‰…1 ÿ kaw †…1 ‡ …cG ÿ 1†kaw †Š; …8†
 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31
where
cB…G†  cG k: …9†
To determine the three constants of the GAB equation,
several methods can be employed. In the present con-
text, a linearisation method of the GAB isotherm ana-
logue to that of the BET model (Eq. (3)) is the most
adequate; the other methods will be examined latter. To
linearise the GAB isotherm, the following function
F(GAB) applies:
F…GAB†  aw =‰…1 ÿ kaw †x…aw †Š
ˆ 1=‰cG kxmG Š ‡ ‰…cG ÿ 1†=cG xmG Šaw : …10†
Thus the so-called GAB plots ± i.e., F(GAB) vs aw
(Anderson, 1946; Gascoyne & Pethig, 1977; Timmer-
mann, 1989) ± should be linear in aw , if the correct k-
value is used for the experimental F(GAB). In practice,
one looks for the k-value which best linearises F(GAB)
vs aw ; a too high k-value determines an upward curva-
Fig. 1. (a) Fish ¯our; (b) corn barn; (c) wheat starch BET and GAB
plots for food materials. Note that GAB plots are displaced 0.02 units
downwards to avoid overlapping. Values of the k-constant for ®sh
¯our, corn bran and wheat starch are 0.81, 0.76 and 0.68, respectively.
21
ture in these plots as in the BET plots and a too low k-
value determines a downward curvature. Analytically,
the minimum of the sum of the least squares of the linear
regression of Eq. (10) in terms of variable k determines
the best k-value. Moreover, from the two linear regres-
sion coecients of F(GAB), the other constants ± xmG
and cG ± can be obtained.
The corresponding representation of F(GAB) vs aw is
also given in Fig. 1 (corresponding values of k have been
taken from Table 1). The linearisation of experimental
data through Eq. (10) is possible within the range
0.05 < aw < 0.8, which represents a much broader appli-
cability range of the GAB isotherm compared with the
BET equation. Furthermore, at higher water activities,
these GAB plots present a downward deviation due to
the appearance of the third sorption stage (Timmer-
mann & Chirife, 1991), an e€ect, which determines the
upper limit of application of the GAB isotherm.
2.3. The relation between F(BET) and F(GAB)
As already stated, the results of both regressions for
the same set of experimental data lead to the inequalities
stated by Eq. (1). This dilemma may be tackled in the
following way. F(GAB) is related to F(BET) by
F…BET† ˆ aw =‰…1 ÿ aw †x…aw †Š
ˆ ‰…1 ÿ kaw †=…1 ÿ aw †ŠF…GAB† …11†
and by introducing here the expression (10) of F(GAB)
and multiplying out the resulting expression, a second
relationship for F(BET), named F (BET), is obtained,
now in terms of the three constants of the GAB iso-
therm. It results
F …BET†  ‰…1 ÿ kaw †=…1 ÿ aw †Š‰1=…kcG xmG †
‡ ……cG ÿ 1†=cG xmG †aw Š
ÿ

ˆ 1=cB…G† xmG ‡ cB…G† ÿ 1 ‡ 2…1 ÿ k†

=cB…G† xmG aw
 ÿ

‡ …1 ÿ k† cB…G† ‡ 1 ÿ k

=cB…G† xmG ‰aw =…1 ÿ aw †Š; …12†
where Eq. (9) has been used to introduce cB…G† . This
second expression for F(BET) shows that, if k < 1,
F(BET) will not be linear in aw , but will present an hy-
perbolic behaviour
F …BET† ˆ A ‡ Baw ‡ C ‰aw =…1 ÿ aw †Š
ˆ …A ÿ C† ‡ …B ÿ C†aw ‡ C=…1 ÿ aw †; …13†
where
A  1=cB…G† xmG ;
ÿ

B  cB…G† ÿ 1 ‡ 2…1 ÿ k† =cB…G† xmG ;
ÿ

C  …1 ÿ k† cB…G† ‡ 1 ÿ k =cB…G† xmG : …14†
 22

Table 1
BET and GAB constants for water sorption in foods and foodstu€sa

BET (range: 0:05 6 aw 6 0:4) GAB (range: 0:05 6 aw 6 0:8)

nB xmB (exp) cB (exp) xmB (calc) cB (calc) nG xmG cG k cG k

Tomato (A) 4 14.5 ‹ 1.1 61.8 ‹ 67.5 14.3 ‹ 0.5 68.8 ‹ 39.5 9 16.6 ‹ 0.6 31.4 ‹ 9.3 0.83 ‹ 0.06 26.1 ‹ 9.6
30°C/NEF 5.49 (0.113±0.432)b 2.48 2.38 (0.113±0.836)b

Corn bran (A) 6 6.12 ‹ 0.36 9.5 ‹ 1.3 5.92 ‹ 0.14 10.3 ‹ 0.6 9 7.21 ‹ 0.75 9.8 ‹ 4.5 0.76 ‹ 0.20 7.5 ‹ 5.4
25°C/NEF 3.10 (0.063±0.379)b 1.36 3.38 (0.063±0.716)b

Fish ¯our 4 4.91 ‹ 0.65 5.00 ‹ 1.1 4.56 ‹ 0.19 5.8 ‹ 0.5 8 5.80 ‹ 1.23 5.1 ‹ 3.7 0.81 ‹ 0.33 4.1 ‹ 4.7
(25°C)/NEF 4.17 (0.115±0.443)b 1.32 5.58 (0.115±0.848)b
E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31

Potato starch (native) (A) 10 8.07 ‹ 0.24 26.9 ‹ 4.8 8.22 ‹ 0.45 25.0 ‹ 7.5 16 9.79 ‹ 0.27 20.4 ‹ 3.4 0.75 ‹ 0.05 15.4 ‹ 3.6
20°C/NEF 3.84 (0.0399±0.4027)b 2.52 3.11 (0.0399±0.8887)b

Wheat starch (native) (A) 5 7.93 ‹ 0.17 32.8 ‹ 4.7 7.95 ‹ 0.54 38.0 ‹ 20.9 11 9.89 ‹ 0.21 26.7 ‹ 3.8 0.68 ‹ 0.04 18.1 ‹ 2.2
20°C/NEF 2.57 (0.0404±0.4013)b 3.64 1.94 (0.0404±0.8663)b

Wheat (D) 5 7.64 ‹ 0.41 21.7 ‹ 5.7 7.73 ‹ 0.59 22.7 ‹ 8.9 9 10.24 ‹ 0.1 18.6 ‹ 1.0 0.62 ‹ 0.02 11.4 ‹ 0.9
25°C/NEF 5.50 3.04 5.40

Chicken (cooked) (D) 5 6.81 ‹ 0.06 22.6 ‹ 1.1 7.0 ‹ 0.2 21.5 ‹ 3.5 9 7.75 ‹ 0.31 18.7 ‹ 0.8 0.86 ‹ 0.07 16.1 ‹ 1.9
19.5°C/NEF 0.88 1.31 1.76
Turkey (cooked) (A) 5 5.36 ‹ 0.31 7.7 ‹ 0.9 5.35 ‹ 0.21 7.8 ‹ 0.7 10 6.29 ‹ 0.26 7.41 ‹ 1.22 0.82 ‹ 0.07 6.1 ‹ 1.7
22°C/NEF 3.49 0.37 3.87 (0.05±0.9)b

Turkey (cooked) (D) 5 6.24 ‹ 0.44 7.0 ‹ 1.0 6.20 ‹ 0.30 7.2 ‹ 0.7 10 6.92 ‹ 1.59 7.50 ‹ 0.45 0.79 ‹ 0.10 5.9 ‹ 1.0
22°C/NEF 3.99 0.95 3.74 (0.05±0.9)b

Corn ¯our (degermed) 5 7.93 ‹ 0.38 79 ‹ 61.4 7.91 ‹ 0.64 138 ‹ 314 9 10.27 ‹ 0.16 42.4 ‹ 5.4 0.59 ‹ 0.03 25.1 ‹ 4.3
25°C/NEF 7.47 5.80 1.07

Rice (A) 4 7.74 ‹ 0.23 32.9 ‹ 7.4 7.94 ‹ 0.60 31.1 ‹ 16.6 8 11.0 ‹ 0.53 19.2 ‹ 5.3 0.58 ‹ 0.08 11.2 ‹ 4.6
25°C/NEF 2.38 (0.1±0.4)b 2.83 2.04 (0.1±0.8)b

Corn (D) 5 7.39 ‹ 0.26 22.6 ‹ 4.0 7.49 ‹ 0.55 23.3 ‹ 8.9 9 9.78 ‹ 0.21 18.8 ‹ 2.3 0.633 ‹ 0.037 11.9 ‹ 2.1
30°C/NEF 3.67 2.96 1.27 7

Wheat gluten (A) 4 5.33 ‹ 0.68 21.9 ‹ 14.8 5.36 ‹ 0.24 21.7 ‹ 4.9 8 6.38 ‹ 0.54 16.4 ‹ 7.6 0.78 ‹ 0.15 12.9 ‹ 8.5
3°C/NEF 1.02 (0.1±0.4)b 1.52 4.40 (0.1±0.8)b

Skimmilk (A) 4 3.92 ‹ 0.20 52.6 ‹ 31.7 3.87 ‹ 0.11 67.3 ‹ 28.9 9 4.27 ‹ 0.11 38.0 ‹ 10.2 0.876 ‹ 0.05 33.0 ‹ 13.1
34°C/NEF 4.68 (0.1±0.4)b 1.32 2.98 (0.1±0.9)b
a
A: adsorption, D: desorption; xm : in g H2 O/100 g dry matter; nB , nG : number of experimental points; (exp): obtained using the direct regression by F(BET); (calc): calculated in terms of the GAB
constants using F (BET); NEF: normalized error function (Eq. (21)). Source of sorption data: Tomato: Kiranoudis, Maroulis, Tsami, and Marinos-Kouris (1993); Corn bran: Duras and Hiver
(1993); Fish ¯our: Labuza, Kaanane, and Chen (1985); Potato starch (native): van den Berg (1981); Wheat starch (native): idem; Wheat: Hubbard, Earle, and Senti (1957); Chicken (cooked): Taylor
(1961); Turkey (cooked): King, Lam, and Sandall (1968); Corn ¯our (degermed): Kumar (1974); Rice: Nemitz (1963); Corn: Hubbard et al. (1957); Wheat gluten: Bushuk and Winkler (1957);
Skimmilk: Berlin, Anderson, and Pallanach (1970).
b
Other evaluation range than that stated in the headings.
E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31
23
24 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31
Conversely, if k ˆ 1, Eqs. (3), (13) and (14) become
identical as C (k ˆ 1) ˆ 0.
Eq. (13) readily explains qualitatively and quantita-
tively (Eq. (14)) the usually observed upswing in the
BET plots at aw > 0.4±0.5, if k < 1. In the graphs of
Fig. 1, F (BET) has been represented in terms of the
corresponding GAB constants taken from Table 1. It is
shown that this function reproduces quite well the (non-
linear) experimental F(BET) within the whole GAB
applicability range 0.05 < aw <0.8.
Furthermore, it is evident that, if F(BET) responds to
Eq. (13) but analysed using Eq. (3), the so-obtained (and
associated to the BET isotherm) values of xmB and cB
will certainly be functions of the three GAB constants
xmG , cG and k through Eqs. (12)±(14) and of the aw in-
terval over which the regression is performed. And this
functional dependence determines the di€erence between
the BET and the GAB sets for the monolayer capacity
(xm ) and the principal energy constant (cB ) and, there-
fore, the inequalities stated by Eq. (1).

2.4. BET regression by F (BET)
The second expression (13) of F(BET) may also be
adjusted by the same linear polynomial (4), but now
using an analytical formulation as F (BET) is known as
a function of aw and not by a set of numerical data. The
calculation implies the adjustment of a function of a
known functional dependence of a higher degree than
one to a straight line. This regression of F (BET) can be
made either in a discrete form or in a continuous form,
as it is shown elsewhere (Timmermann, 2000).
In the discrete procedure, F (BET) given by Eq. (13)
is explicited into condition (5), which becomes
X
iˆn
f‰ A ÿ C ‡ …B ÿ C†xi ‡ C=…1 ÿ xi †Š ÿ …a0 ‡ a1 xi †g
iˆ1
ˆ minimum
and this expression can now be solved analytically for a0
and a1 in the usual way of least squares. As it is to be
expected, it results (Timmermann, 2000) that a0 and a1
become functions of the constants A, B and C of Eq.
(13) on one side, and of regression sums over the values
of the independent variable xi on the other.
The ®nal expressions are the following:
a0 ˆ …A ÿ C† ‡ C…d0 =d†; …
a1 ˆ …B ÿ C† ‡ C…d1 =d†; …
where a0 and a1 are the minimum squares estimates in
terms of F (BET). The functions d, d0 and d1 contain
only the regression sums of aw over the employed re-
gression interval with the following signs: d0 /d < 0, d1 /
d > 0 and d0 /d + d1 /d > 0 for aw < 1 (Timmermann, 2000).
The corresponding relations are, where Gaussian
brackets have been used,
 
d0  ‰1=…1 ÿ aw †Š a2w ÿ ‰aw =…1 ÿ aw †Š‰aw Š; …17a†
d1  ‰aw =…1 ÿ aw †Šn ÿ ‰1=…1 ÿ aw †Š‰aw Š; …17b†
 
d  n a2w ÿ ‰aw Š2 : …17c†
n is the number of data included in the regression.
As the Eqs. (6) and (7) remain valid, the BET con-
stants are now given by
xmB ˆ 1=…a0 ‡ a1 †
ˆ 1=f A ‡ B ‡ C ‰…d0 ‡ d1 †=d ÿ 2Šg …18a†
and
ÿ

cB ˆ a0 ‡ a1 =a0
ˆ f A ‡ B ‡ C ‰…d0 ‡ d1 †=d ÿ 2Šg=f A ‡ C ‰d0 =d ÿ 1Šg:
…18b†
Finally, by Eq. (14) A, B, C ˆ f(xmG , cG , k) and after
some algebra, explicit expressions for xmB and cB in
terms of the three GAB constants are obtained (Tim-
mermann, 2000):
 
xmB ˆ xmG = 1 ‡ 2…1 ÿ k†=cB…G† Rm …19a†
and
 
cB ˆ cB…G† 1 ‡ 2…1 ÿ k†=cB…G† Rc ; …19b†
where the functions Rm and Rc are given by
ÿ
ÿ
Rm  1 ‡ …1 ÿ k† cB…G† ‡ 1 ÿ k = cB…G†


‡ 2…1 ÿ k† ‰…d0 ‡ d1 †=d ÿ 2Š …20a†
and
 ÿ

Rc  Rm = 1 ‡ …1 ÿ k† cB…G† ‡ …1 ÿ k†‰d0 =d ÿ 1Š :
2
…20b†
These functions are always greater than unity (Tim-
…15† mermann, 2000). In consequence, Eqs. (19a) and (19b)
reproduce the inequalities (1) if k < 1.
Eqs. (19a) and (19b) explicit and quantify the di€er-
ences between the BET set (xmB ) cB ) and the GAB set
(xmG ) cB…G† ) of constants. These di€erences are directly
related to k < 1 through the factor (1 ) k) present in
these equations and hence, explain the inequalities set in
Eq. (1). They become more important with decreasing
values of k as well as with an increase of the regression
16a† interval. On the other hand, if k ˆ 1, all these expres-
sions coincide with the classical results shown before.
16b† Eqs. (16a), (16b), (19a) and (19b) have been used to
calculate the linear correlation of F(BET)GAB in terms of
the corresponding GAB constants and for the same
water activity interval used for the empirical BET
equation (numerical values are stated in Table 1); the
results are shown in Fig. 1(a±c). The reproduction of the
empirical BET constants and of the inequalities stated in
 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31 25

Eq. (1) are quite acceptable. For the case of ®sh ¯our
(Fig. 1(a)), a slight di€erence between the linear
F(BET)exp and the linear F(BET)GAB is observed, a dif-
ference which is determined by the empirical dispersion
of the experimental sorption data. In the case of corn
bran (Fig. 1(b)), this dispersion is less and the coinci-
dence of F(BET)exp and F(BET)GAB is better. Finally, in
the case of wheat starch (Fig. 1(c)), this dispersion is
minimal and F(BET)exp and F(BET)GAB become prac-
tically undistinguishable.
Thus, the approach given here solves the dilemma of
the inequalities stated by Eq. (1). It also explains the
restricted range of linearity of the BET regression, the
dependence of the values of the BET constants on
the activity range used for the regression, and the up-
swing of the BET plots at higher water activities.
3. Analysis of water sorption data for various foods and
food materials
Two groups of sorption systems were analysed, (1)
various foods and foodstu€s, and (2) proteins. The
second group corresponds exclusively to the compre-
hensive data set of water sorption by proteins due to
Bull (1944), where this author tested the applicability
of the BET isotherm to these sorption systems. The
results are presented in Tables 1 and 2, and in Fig. 2.

Table 2
Monolayer moisture contents for various proteinsa;b

Protein BET (range: 0:05 6 aw ÿ 6 0:3) GAB (range: 0:05 6 aw 6 0:8)

NB xmB (exp) cB (exp) xmB (calc) cB (calc) nG xmG cG k cG k

Collagen 4 9.64 ‹ 0.15 21.0 ‹ 1.3 10.2 ‹ 0.19 17.2 ‹ 1.1 9 11.5 ‹ 0.5 17.3 ‹ 4.4 0.80 ‹ 0.09 13.8 ‹ 5.1
NEF ˆ 0.94 NEF ˆ 0.92 NEF ˆ 3.01
Gelatin 4 8.47 ‹ 0.48 23.9 ‹ 6.1 9.11 ‹ 0.18 18.6 ‹ 1.4 9 10.3 ‹ 0.8 18.7 ‹ 7.8 0.78 ‹ 0.14 14.6 ‹ 8.7
NEF ˆ 3.22 NEF ˆ 1.01 NEF ˆ 4.31
Seroalb. 4 6.52 ‹ 0.26 14.3 ‹ 1.7 6.71 ‹ 0.12 13.3 ‹ 0.7 8 7.55 ‹ 0.42 13.6 ‹ 3.7 0.81 ‹ 0.10 11.0 ‹ 4.4
NEF ˆ 1.75 NEF ˆ 0.75 NEF ˆ 2.57
Elastinc 5 6.54 ‹ 0.98 15.0 ‹ 8.0 6.39 ‹ 0.2 17.3 ‹ 2.1 9 7.61 ‹ 1.3 15.5 ‹ 13.8 0.77 ‹ 0.32 11.9 ‹ 15.5
NEF ˆ 11.1 NEF ˆ 2.2 NEF ˆ 9.2
Wool 4 6.73 ‹ 0.31 12.6 ‹ 1.6 7.00 ‹ 0.18 11.5 ‹ 0.7 9 8.47 ‹ 0.52 12.2 ‹ 3.6 0.71 ‹ 0.11 8.7 ‹ 3.9
NEF ˆ 1.87 NEF ˆ 0.99 NEF ˆ 2.42
a=b-pseudo 4 6.72 ‹ 0.26 16.3 ‹ 2.1 7.11 ‹ 0.13 13.7 ‹ 0.7 9 7.99 ‹ 0.45 13.9 ‹ 3.9 0.81 ‹ 0.11 11.3 ‹ 4.5
Globulin NEF ˆ 1.90 NEF ˆ 0.75 NEF ˆ 3.28
c-pseudo 4 6.74 ‹ 0.32 15.7 ‹ 2.4 7.09 ‹ 0.13 13.5 ‹ 0.7 9 7.98 ‹ 0.41 13.8 ‹ 3.5 0.81 ‹ 0.10 11.2 ‹ 4.2
Globulin NEF ˆ 2.32 NEF ˆ 0.76 NEF ˆ 2.84
Lactoglob. 4 6.62 ‹ 0.40 9.7 ‹ 1.3 6.77 ‹ 0.12 9.3 ‹ 0.3 9 7.72 ‹ 0.45 9.5 ‹ 2.4 0.81 ‹ 0.10 7.7 ‹ 2.9
Crist. NEF ˆ 1.90 NEF ˆ 0.59 NEF ˆ 1.93
Lactoglob. 4 5.91‹0.08 10.8‹0.4 6.39‹0.12 9.0‹0.3 9 7.35‹0.52 9.3‹2.8 0.80‹0.13 7.4‹3.5
f.dried NEF ˆ 0.49 NEF ˆ 0.60 NEF ˆ 3.39
Eggalbum. 4 5.19 ‹ 0.12 13.2 ‹ 0.9 5.46 ‹ 0.11 11.5 ‹ 0.6 10 6.30 ‹ 0.26 11.8 ‹ 2.3 0.78 ‹ 0.07 9.3 ‹ 2.6
Coag.d NEF ˆ 0.99 NEF ˆ 0.76 NEF ˆ 2.70
Egg album 4 5.64 ‹ 0.27 13.3 ‹ 1.8 6.02 ‹ 0.11 11.3 ‹ 0.5 9 6.88 ‹ 0.47 11.6 ‹ 3.7 0.80 ‹ 0.12 9.2 ‹ 4.3
f.dried NEF ˆ 1.99 NEF ˆ 0.72 NEF ˆ 3.06
Egg album 4 6.28 ‹ 0.16 12.1 ‹ 0.8 6.45 ‹ 0.13 11.4 ‹ 0.6 9 7.43 ‹ 0.30 11.7 ‹ 2.2 0.78 ‹ 0.07 9.2 ‹ 2.5
Not f.dried NEF ˆ 1.05 NEF ˆ 0.76 NEF ˆ 1.68
c-zein 4 3.83 ‹ 0.07 13.7 ‹ 0.7 3.93 ‹ 0.06 12.6 ‹ 0.5 9 4.37 ‹ 0.21 12.8 ‹ 3.0 0.83 ‹ 0.09 10.5 ‹ 3.6
NEF ˆ 0.83 NEF ˆ 0.64 NEF ˆ 4.42
b-zein 4 4.10 ‹ 0.15 12.5 ‹ 1.2 4.11 ‹ 0.08 12.5 ‹ 0.7 8 4.75 ‹ 0.21 12.9 ‹ 2.8 0.77 ‹ 0.08 9.9 ‹ 3.2
NEF ˆ 1.43 NEF ˆ 0.64 NEF ˆ 1.88
Silk 4 4.15 ‹ 0.24 14.3 ‹ 0.2 4.33 ‹ 0.09 12.8 ‹ 0.7 9 5.00 ‹ 0.30 13.2 ‹ 3.9 0.77 ‹ 0.11 10.2 ‹ 4.4
NEF ˆ 2.40 NEF ˆ 0.86 NEF ˆ 2.62
Salmine 4 5.94 ‹ 0.29 40.0 ‹ 13.6 11.6 ‹ 0.12 2.2 ‹ 0.02 6 13.6 ‹ 19.4 2.15 ‹ 6.6 0.89 ‹ 1.4 1.9
NEF ˆ 3.27 NEF ˆ 0.10 NEF ˆ 1.54
a
nB , nG , number of experimental points; xm : in g H2 O/100 g dry matter; (exp): obtained using the direct regression by F(BET); (calc): calculated in
terms of the GAB constants using F (BET); NEF: normalized error function (Eq. (21)).
b
Experimental data: Bull (1944).
c
BET range: 0.05±0.4.
d
GAB range: 0.05±0.9.
e
The isotherm presents two branches which are incompatible with each other; at aw ˆ 0:05±0:3 BET applies, but at aw ˆ 0:3±0:8, the application of
GAB is quite questionable (see error ®gures) and the BET and GAB monolayer and energy values cannot be related.
26 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31
Fig. 2. Experimental and calculated water sorption isotherms for
(a) foods/foodstu€s and (b) proteins (Bull). Note that the isotherms
have been displaced upwards a certain amount of units for a better view.
The left-side sections of Tables 1 and 2 present the sets
of BET constants obtained by (a) the direct regression
by F(BET) (Eqs. (6) and (7)) and (b) in terms of the
GAB constants using F (BET) [Eqs. (14), (16a)±(18b)];
and the right-side section contains the set of GAB
constants obtained using a parabolic regression (Eq.
22) (see also Fig. 3). The general regression ranges are
given in the headings, with exceptions indicated in
each case. The error of each numerical value has been
calculated using the regression covariance of each
parameter. Finally, the normalised error function
(NEF), de®ned as
" !, #1=2,
X
iˆn
ÿ
2
NEF ˆ 100 x exp ÿ xcalc n xm …
iˆ1
i parameters by Eqs. (19a) and (19b) using the GAB
is also given. This function is related to, but simpler than
the relative percentage root, mean square value often
used in the literature.
It can be seen (see also the top graphs of Fig. 4) that
GAB monolayer values are about 10±40% higher than
the BET value, while the energy constant cB…G† is much
lower (35±50% and even more) than the BET value. In
the same way, the errors of the energy constant values
are much stronger (15±25% up to 60±70% and more)
than that of the monolayer (4±8%). It is also to be noted
that the error of the third GAB constant, k, is in the
order 10±15% and therefore, the value of this constant
should be given with only two signi®cant ®gures. For
the constant k, the values already stated elsewhere
(Chirife et al., 1992) for proteins and protein foods
(k  0.8, range 0.78±0.85) and for starchy foods (k  0.7,
range 0.65±0.75) are con®rmed. A lower value of k in-
dicates a much less structured state of the sorbate in the
layer following the monolayer, the so-called GAB lay-
ers, as in the sorbate's pure liquid state (Timmermann,
2000).
In food science studies, preferred or almost exclusive
attention is paid to the monolayer value (Karel, 1973;
Iglesias & Chirife, 1976b). However, the values of the
energy constants should not be overlooked nor ignored
because they are simultaneous outputs of the regression
processes and they in¯uence the sigmoidal shape of the
isotherms, i.e., the form of the normalised Ôx/xm vs aw Õ
plot, since cB and cG determine the more or less pro-
nounced form of the `knee' at the lower water activity
range. On the other hand, the third GAB constant k
determines the pro®le of the isotherm at the higher
water activity range, regulating the upswing after the
ÔplateauÕ at medium water activity range. Higher values
of k determine a more pronounced upswing. This can be
readily observed in Fig. 2; proteins and protein-foods
(k  0.8) present a much more noticeable upswing than
starchy foods (k  0.7).
Finally, the function NEF is a measure of the ex-
perimental dispersion of the sorption data; good (mean)
values of NEF are in the order 2±5%. If this dispersion is
homogeneous over the whole GAB range, NEF has
coincident values for the BET as well as for the GAB
regressions indicating the much better ability of the
GAB equation to represent the data as it embraces a
much broader range of water activity. But if this dis-
persion is heterogeous (in the BET region di€erent than
in the GAB region), then NEF oscillates about the same
values being in some cases the BET values lower than
the GAB values and in others the opposite is observed,
but always within the range 2±5%. A case markedly
beyond this range is the protein elastin, the sorption
data of which present NEF values of 9% (GAB) to 11%
(BET). Morover, the NEF values of the calculated BET
21†
constants are due to the intrinsic hyperbolic curvature of
F (BET) (Eqs. (12) and (13)) over the BET range of
activities. The experimental NEF values of the BET
regression include this e€ect and therefore, by the
 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31 27

Fig. 3. (a) Inverse and (b) parabolic plots for various foods, foodstu€s and proteins. Symbols: experimental data. The arrows in the graphs indicate
the upper limit of each equation.

experimental dispersion of the data, the NEF values where

¯uctuate (upwards or downwards) about the `theoreti- a  1=xmG cG k; …23a†
cal' values indicated by the former.
Fig. 2 shows calculated food isotherms obtained by b  …cG ÿ 2†=xmG cG ; …23b†
the BET and GAB regressions as well as by the BET
constants calculated in terms of the GAB parameters, c  ÿ…cG ÿ 1†k=xmG cG : …23c†
using the constants given in Tables 1 and 2. The limited
The three constants a, b and c are readily determined by
range of applicability of the BET equation and the
a least-square regression of this second degree polyno-
ability of the GAB equation to represent the experi- mial and from these, the three GAB constants are cal-
mental data up to aw  0.85 is observed in all cases; as culated by
well as the good agreement between calculated BET
isotherm by the GAB constants with the BET curve k ˆ …f 1=2 ÿ b†=2a; …24a†
obtained directly by the regression of the experimental
data. xmG ˆ f ÿ1=2 ˆ 1=…b ‡ 2ka† ˆ k=…k 2 a ÿ c†; …24b†
To determine the GAB constants, a simple method
was used which is straightforward; it uses the so-called cG ˆ 1 ÿ c=k 2 a ˆ 2 ‡ b=ka ˆ f ÿ1=2 =ka; …24c†
transformed form of the GAB equation (Schaer & Ru- where
egg, 1988), i.e., the following parabolic expression,
which is easily derived from Eq. (8): f  b2 ÿ 4ac: …24d†
The constants stated in Tables 1 and 2 were obtained
aw =x ˆ a ‡ baw ‡ ca2w ; …22† by this method. The upper limit of the regression or
28 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31

Fig. 4. Comparison of (a) experimental BET and GAB constants and (b) experimental and calculated BET constants: (from data shown in Tables 1
and 2). Error bars are indicated in each case.

applicability range of the GAB isotherm (the lower limit
is, as in the BET case, aw ˆ 0.05) is determined with the
so-called inverse plot (Timmermann, 1989). At high aw ,
for strongly sorbing substances (cG  1), both isotherms
become very simple for the inverse of x(aw ):
BET : 1=x ˆ …1=xmB †…1 ÿ aw †; …
GAB : 1=x ˆ …1=xmG †…1 ÿ kaw †: …
These relations indicate that 1/x is linear at high
enough aw for both isotherms and that the limits for
1/x ˆ 0 (x ! 1) are at the points (aw ˆ 1, 1/x ˆ 0; BET)
and (aw ˆ 1/k (>1), 1/x ˆ 0; GAB), respectively. Thus, if
the linear part at higher aw of the inverse plot 1/x vs aw
do not extrapole to aw ˆ 1 for 1/x ˆ 0 (BET condition),
it is readily concluded that k < 1 (see Eq. (25b)) and
that the GAB equation applies. The extrapolation to
1/x ˆ 0 gives 1/k directly as the intercept with the
25a†
aw -axis (Timmermann, 1989). Hence, these plots
readily illustrate which isotherm applies. Furthermore,
25b†
if after the linear part the graph becomes curved
downwards (usually at aw  0.85±0.9), then this is a
direct evidence of the presence of the third sorption
stage (Timmermann, 1989; Timmermann & Chirife,
 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31
1991), these points should not be used for the GAB
regression. These procedures (inverse and parabolic
plots) are shown in Fig. 3 for various food materials.
The calculated BET and GAB isotherms are also
drawn and the upper limits of both equations are
shown by arrows.
An alternative method to obtain the GAB constants
consists in a non-linear least-squares regression of the
GAB equation. It has been claimed (Schaerr & Ruegg,
1988) that this method and that of the parabolic trans-
form give di€erent results, but it can be shown (Tim-
mermann et al., 1991) that if the points of the third
sorption stage are not included, both regressions give
identical results. Accordingly, it has already been stated
that, if points belonging to the third sorption stage are
included in the GAB regression, NEF increases very
sharply this being another criterion to ®x the upper limit
of the GAB regression.
The results contained in Tables 1 and 2 are illustrated
in Fig. 4; the BET monolayer value (xmB ) and energy
constant (cB ) are plotted against the GAB monolayer
value (xmG ) and the value by GAB (cB…G† ˆ cG k), re-
spectively (Figs. 4(a)). These plots illustrate the in-
equalities stated by Eq. (1); i.e., that the BET evaluation
always underestimates the monolayer, while it overesti-
mates the energy constant. Figs. 4(b) shows the plot of
the two BET constants against the respective values
calculated in terms of the GAB constants. Within the
corresponding error intervals, the `experimental' BET
values are well reproduced by the calculated ones, and
the scatter is much lower for the monolayer capacity
than for the energy constant.
It is therefore straightforward to conclude that the
GAB constants are to be taken as the representative
parameters of the multilayer sorption. A much more
precise description of multilayer sorption of water by
food materials can be achieved if the analysis is made
with a set of experimental data, which span over the
`quasi'-complete water activity range.
4. The stoichiometry of water sorption by proteins:
Paulings (1945) hypothesis
In 1945, short after Bull's (1944) paper about the
water sorption by proteins, Pauling (1945) published a
now classical paper about the hydration of proteins. He
advanced that the water sorption monolayer of proteins
can be thought in terms of the attachment of one water
molecule to each polar group of the side chains of the
aminocids in the protein. In his analysis, Pauling utilised
BET monolayer values reported by Bull (1944). The
agreement of these BET monolayer values with the
number of polar groups of the proteins was roughly
satisfactory in as much both values were of the same
order of magnitude. However, it is worth noticing that
29
the monolayer values were in most cases lower than the
number of polar groups.
In view of the results stated in the previous sections, it is
straightforward to compare Pauling's data with the
monolayer capacity obtained here by the GAB evalua-
tion, as this equation is directly related and is an im-
provement of the original BET formulation. Pauling
(1945) expressed his numerical data in terms of the
number of polar groups or moles of water per 105 g of
protein. We retain here these units, the monolayer values
given as grams of water per 100 g of proteins in Table 2 are
to be multiplied simply by 55.5 ( ˆ 1000/18) mol H2 O/g.
Table 3 shows the results of this new analysis of
Pauling's hypothesis. The BET monolayer values stated
in Table 2 are slightly di€erent from those reported by
Bull (1944) in his original paper, data which are given
within parenthesis in the same table. This is likely due to
some di€erences in the water activity interval used for
the BET regression (interval which is not stated exactly
in Bull's paper) and to the fact that Bull's values are the
mean between the values at 25°C and at 40°C. As in
Pauling's (1945) original paper, the second value of the
second column (Table 3) corresponds to the value ob-
tained by taking also into account the aminoacids pro-
line and hydroxiproline. Data within [ ] are the number
of polar groups reported by other authors found in a
rapid and not-exhaustive search of the literature, as a
more profound revision of Pauling's values in terms of
modern literature of protein aminoacid composition, is
beyond the scope of this paper.
The inspection of Table 3 shows that the rough
agreement noted by Pauling is certainly improved when
the GAB monolayer values are used for comparison.
This conclusion becomes even more evident when the
BET and GAB monolayers are graphically plotted
against the number of polar groups (Fig. 5). The
agreement is quite better for collagen, gelatin, serumal-
bumin, lactoglobulin, c- and b-zein. For silk, the BET
value seems to be better and, on the other side, for
salmin, the GAB value correlates surprisingly well, al-
though its isotherm presents two branches (see Fig. 2
and note 4 of Table 2), a fact observed already by
Pauling (1945) and by Bull (1944) themselves. Further-
more, in the case of egg albumin and wool, the agree-
ment is improved when the number of polar groups
reported in more modern publications are considered
instead. In the case of collagen and gelatin, Pauling
(1945) noted that the BET value failed to reach the value
of the number of polar groups including the proline and
hydroxiproline, and advanced some possible explana-
tion for this discrepancy. However, when the GAB
monolayer value is used, a close agreement is observed.
Casein, a protein not considered by Pauling in his paper
and not stated in Table 2, has been included in the
present analysis. The sorption data due to Schaerr and
Ruegg (1988) were evaluated elsewhere (Timmermann
30 E.O. Timmermann et al. / Journal of Food Engineering 48 (2001) 19±31

Table 3
Comparison between number of polar groups and BET or GAB monolayer valuesa

Protein Number of polar groups Monolayer capacity

(mol/105 g) (mol/105 g)

Paulingb BET GAB k (GAB)

Collagen 328±609 535 638 0.80

Gelatin Idem 470 572 0.78
Seroalbumin 424 362 419 0.81
Wool 303, 341, 420c 373 470 0.71
Lactoglob.crist. 472, 508 367 428 0.81
Idem, f.dried. Idem 328 408 0.80
Eggalbum, coag 277, 313, 380d 288 350 0.78
Idem, f.dried Idem 313 382 0.80
Idem, not f.dried Idem 348 413 0.78
c-zein 305, 390 212 242 0.83
b-zein Idem 227 263 0.77
Silk 219±228 230 278 0.77
Salmin 611±707 330 755 0.89
Casein 416e , 456, 521f 306g 343g 0.89
a
In Fig. 5, the underlined values of the polar group number are represented in the abscissa axis.
b
Reported by Pauling (1945).
c
Value reported by Windle (1956).
d
Value reported by Fogiel and Heller (1966).
e
Value reported by Ruegg and Hani (1975).
f
Values reported by McLaren and Rowen (1951).
g
Calculated by Timmermann et al. (1991).

et al., 1991) using the BET and GAB equations and the
corresponding monolayer capacities are stated directly
in Table 3. It is observed that casein also ®ts well into
the picture given by Fig. 5.
Finally, it is interesting to consider also the case of
another biopolymer, namely starch. The BET and GAB
monolayer values for potato and wheat starch (Table 1)
were 0.45 and 0.55 mol H2 O/100 g, respectively. Since
the polar group number (one water molecule per anhy-
droglucose monomer) is 0.62, as reported by McLaren
and Rowen (1951), it follows that again the GAB
monolayer correlates much better than the BET value.
Thus, it is to be concluded that the present ®ndings
that GAB parameters are more representative than the
corresponding BETs ones, obtains additional support
when Pauling's hypothesis of initial hydration of pro-
teins, is considered.

Acknowledgements

The ®nancial support from University of Buenos

Aires and CONICET (Argentina) are greatfully ac-
knowledged.

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Fig. 5. Comparison of BET and GAB monolayer values with number
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