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Article history:
Received 20 September 2013
Accepted 6 November 2013
The Maillard reaction has been used as a natural alternative to improve protein functionality by covalent
coupling with saccharides. However, if reaction conditions are not properly selected, glycation can lead to
a loss in functional properties. The objective of our research was to study the effect of temperature, time,
water activity and reactants molar ratio on the degree of glycation and color development in whey
protein isolate conjugated with maltodextrins. Three different levels of glycation (low, medium and high)
were selected to investigate functional properties. The extent of glycation was assessed by quantifying
the loss of amino groups using the o-phthaldialdehyde technique. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis was used to evaluate the molecular weight of the glycoproteins.
Color changes were determined using a Minolta colorimeter and calculating the browning index.
Functional properties evaluated were solubility, rheological behavior, foam overrun and foam stability.
Temperature and water activity were the most inuential factors determining the degree of glycation
and color change. The correlation coefcient between blocked amino groups and color was of 0.743.
Whey protein isolate exhibited lower solubility at pH 5 and conjugates at pH 4. Consistency index and
foaming properties improved according to the level of glycation achieved.
2013 Elsevier Ltd. All rights reserved.
Keywords:
Maillard reaction
Whey protein isolate
Maltodextrin
Functional properties
1. Introduction
Milk proteins consist mainly of caseins and whey proteins, 80%
and 20% respectively (Walstra, Wouters, & Geurts, 2006, chap. 21).
Whey proteins are widely used as raw materials in the food industry due to their nutritional value and functional properties.
Modern processing techniques have allowed the separation and
fractionation of whey proteins to create whey protein powders
with different protein contents (Tunick, 2008). Whey protein
isolate (WPI) contains at least 90% protein, with negligible amounts
of fat, sodium, and lactose and is an excellent source of essential
amino acids. Despite the good functional properties of proteins
from different sources, increasing consumer demand for functional
foods has prompted food scientists to improve protein
functionality.
The Maillard reaction (MR) is a complex series of chemical reactions that occur naturally between the amino group of an amino
X
Lmw *2
1
Pmw
(1)
111
BI
a 1:75L
5:645L a 3:012b
100x 0:31
0:172
(2)
(3)
112
fc
s so kg_ n
(5)
(4)
113
Table 1
Degree of glycation and browning index obtained at different reaction conditions.
Temperature ( C)
Relative
Humidity (%)
Time (h)
Molar Ratio
(Amino:Carbonyl)
Blocked Amino
Groups (% SD)a
60
60
60
60
50
60
60
50
60
60
50
50
50
50
50
50
80
80
80
80
80
50
50
80
50
50
80
80
50
50
50
50
48
48
24
24
48
48
48
48
24
24
24
24
48
48
24
24
1:2
1:1
1:2
1:1
1:2
1:2
1:1
1:1
1:2
1:1
1:2
1:1
1:2
1:1
1:2
1:1
7.42
8.33
8.79
9.13
9.16
9.45
9.88
10.00
10.28
10.83
11.10
11.49
11.75
12.34
12.73
13.03
51.75
45.82
42.87
40.61
40.47
38.54
35.75
35.00
33.15
29.55
27.84
25.28
23.57
19.74
17.20
15.28
1.75
2.49
1.66
1.79
0.96
1.69
2.10
1.29
1.43
1.03
1.61
2.14
1.05
1.30
1.47
2.00
a
b
c
c,d
c,d
d
e
e
e
f
f,g
g,f
g,f
i
i,j
j
Browning Index
30.87
26.57
17.59
16.20
12.43
9.37
11.84
14.58
6.30
7.48
9.85
7.97
5.65
6.20
4.65
5.18
2.3
0.9
0.2
0.8
1.6
0.6
0.3
0.1
0.3
0.3
0.7
0.3
0.1
0.1
0.3
0.2
a
b
c
d
f
g
f
e
i,j
h,i
g
h,i
j,k
i,j
k
j,k
a
Each value is an average of three samples standard deviation. The means followed by different online letters in the same column are signicantly different (p 0.05) by
Tukeys test.
2000). Reaction rates observed during the rst and second 24h periods (Fig. 1) were signicantly different among them,
showing a strong effect of reaction temperature and relative humidity during the rst 24 h and a highly reduced reaction rate
during the second 24-h period, when the effect of temperature and
relative humidity was no longer relevant, having an average reaction rate value of only 0.046 blocked residues per mole per hour.
It is interesting to note that the lowest levels of blocked amino
groups obtained in this study (15e19% blocked amino groups in
samples subjected to 50 C and 50% RH) roughly coincide with the
number of accessible amino groups in a-lactalbumin alone. According to Jimnez-Castao, Villamiel, and Lpez-Fandio (2007),
80e90% of lysine residues in the three dimensional structure of alactalbumin are readily accessible for interaction with other molecules. This number of free residues would correspond to 18.4%e
20.7% of the total number of amino residues in WPI, considering the
occurrence of b-lactoglobulin and a-lactoglobulin in a mole ratio of
approximately 2.7 to 1, having 16 and 13 free amino groups,
respectively (Wooster & Augustin, 2007a). This observation suggests that glycation during the rst 24 h may have proceeded
mainly with a-lactalbumin amino residues, requiring of more time
and more stringent conditions in order to be able to proceed with
b-lactoglobulin amino residues. This hypothesis is further supported by the results reported by Nacka, Chobert, Burova, Leonil,
and Haertl (1998) who found that glycation of a-lactalbumin
was faster and more pronounced compared to that of b-lactoglobulin in the presence of mono- and disaccharides.
3.1.1.4. Effect of reactants molar ratio. Generally, an excess of
carbonyl groups in the molar ratio of reactants promotes the
development of the MR. In this study, an increase of 1:1 to 1:2
(amino/carbonyl ratio) increased glycation by w3.5%. An increase in
the molar ratio of 1:3 to 1:15 in conjugates formed between bovine
serum albumin and galactomannan resulted in the binding of 2.5e
6.7 molecules of polysaccharide to protein. Wooster and Augustin
(2007b) evaluated the degree of glycation of conjugates created
between b-lactoglobulin and MD according to the following molar
ratios: 1:0.09, 1:0.17, 1:0.25, 1:0.33, 1:0.66, and 1:1.7 obtaining 10.4,
12.9, 16, 25.5, 35 and 47% of blocked amino groups, respectively.
3.1.2. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis
(SDS-PAGE)
SDS-PAGE under denaturing conditions was employed to evaluate the molecular weight of the produced GPs. In Fig. 2, GPs are
114
0.3
First 24 h
0.25
Second 24 h
0.2
0.15
0.1
0.05
0
60C/80%
60C/50%
50C/80%
50C/50%
arranged according to the OPA results, from the one with the
highest percentage of blocked amino groups to the one with the
lowest level, and also according to the employed treatment temperature. The lanes from 2 to 9 correspond to GPs obtained at 60 C,
and lanes from 10 to 17 to those obtained at 50 C. Controls (mixtures not treated and WPI subjected to treatments in absence of
MD) are not included in the shown gel because no signicant
reduction of free amino groups was observed during OPA analyses
and because their SDS-PAGE results did not signicantly differ from
those corresponding to untreated WPI. Two intense bands are
shown in lane 1, which are characteristic of WPI and belong to alactalbumin (lower band) and b-lactoglobulin. The WPI protein
bands tend to disappear, and new compounds with higher molecular weight start to form as the degree of glycation increase, which
seems to indicate that all the WPI proteins were glycosylated.
However, when comparison was made between the OPA results
(available amino groups) and the assumption of the formation of
highly glycosylated molecules from all the a-lactalbumin and blactoglobulin proteins, it would be expected a lower protein glycation. This demonstrates that OPA method shows an average of
available amino groups per molecule and does not distinguish between glycosylated and non-glycosylated molecules (Wooster &
Augustin, 2007a).
Fig. 2. SDS-PAGE of WPI and GP. Lane 1) WPI, 2) GP (60-80-48-1:2), 3) GP (60-80-48-1:1), 4) GP (60-80-24-1:2), 5) GP (60-80-24-1:1), 6) GP (60-50-48-1:2), 7) GP (60-50-48-1:1),
8) GP (60-50-24-1:2), 9) GP (60-50-24-1:1), 10) GP (50-80-48-1:2), 11) GP (50-80-48-1:1), 12) GP (50-80-24-1:2), 13) GP (50-80-24-1:1), 14) GP (50-50-48-1:2), 15) GP (50-50-481:1), 16) GP (50-50-24-1:2), 17) GP (50-50-24-1:1). WPI means whey protein isolate and GP means glycoprotein. Numbers in parentheses correspond to the reaction conditions:
temperature ( C), relative humidity (%), time (h), and molar ratio, respectively.
115
Fig. 3. Color development in samples treated under different experimental conditions. WPI means whey protein isolate and GP means glycoprotein. Numbers in parentheses
correspond to the reaction conditions: temperature ( C), relative humidity (%), time (h), and molar ratio, respectively. (For interpretation of the references to color in this gure
legend, the reader is referred to the web version of this article.)
3.1.3.1. Effect of reaction conditions on color development. The factors that showed a statistically signicant effect (p < 0.0001) on
color development were relative humidity, temperature and time,
from the most to the least inuential, representing 46, 26, and 13%,
respectively. Molar ratio did not showed a signicant effect
(p 0.8325). Medrano, Abirached, Panizzolo, Moyna, and An
(2009) reported that molar ratio had a signicant effect on the
color development of GP obtained from b-lactoglobulin and
glucose, but no effect was observed on GP made from b-lactoglobulin and lactose, which indicated that the carbohydrate reactivity is a determinant factor. In a monosaccharide e single amino
14
Available amino Groups
y = -0.1839x + 12.572
R = 0.7432
13
12
11
10
9
8
7
6
0.0
10.0
20.0
Browning Index
30.0
40.0
Fig. 4. Lineal correlation between available amino groups (Residues per WPI mole)
and Browning index (obtained from equation (3)) of glycoprotein samples.
116
acid system, the molar ratio showed a signicant effect on the color
development at pH values higher than 8 (Renn & Sathe, 1997). At
RH of 50%, the browning index average was 7.08, whereas at 80% an
average of 17.01 was reached. These results concur with those obtained by Pan and Melton (2007), where the maximum color
attained in GP made from sodium caseinate and lactose occurred at
80% of RH. Results shown in Table 1 suggest that as the temperature
increased, the development of color also increased, producing an
average difference of w7.5 units between 50 and 60 C treatments.
Likewise, an average difference of w5.2 units was found between
24 h and 48 h treatments.
The browning index increased as the temperature and time rose,
getting the highest browning index value at 60 C for 48 h. Color
was approximately 3 times higher at 60 C and 80% RH, than at
60 C and 50% RH. Similarly, a considerable increase was observed
as time and RH increased. Similar results were reported for GP
prepared from whey proteins and polysaccharides, and also for
protein/monosaccharide and amino acid/monosaccharide systems
(Bosch, Alegra, Farre, & Clemente, 2007; Einhorn-Stoll et al., 2005;
Rozycki, Buera, Piagentini, Costa, & Pauletti, 2010).
3.2. Functional properties
3.2.1. Solubility
Solubility of WPI, controls, and GPs was assessed as a function of
pH (Fig. 5). Untreated WPI was almost completely soluble at all pH
conditions evaluated in this study, showing a minimum solubility
value of 85% at its isoelectric point. Solubility of control treated at
60 C, 80% RH for 48 h (WPI treated under glycosylation conditions
without MD) decreased considerably to a minimum solubility value
of 27% at pH 5. A decrease in solubility of b-lactoglobulin from 30 to
40% was reported by Jimnez-Castao et al. (2005) when protein
was heated at 60 C, 44% HR for 4 days in a concentration of 1 mg/
mL. The low solubility of WPI controls is probably due to a higher
exposition of hydrophobic amino acid residuals to water owing the
spatial conformation of proteins. The GP sample with the lowest
glycosylation level (GP, 50-50-24-1:1) resulted in a solubility
comparable to that of the WPI sample, with an increase of 3% at its
isoelectric point, possibly due to the addition of hydroxyl groups
provided by MD. GP samples with high and moderate glycosylation
levels showed a change in the minimum solubility value from pH 5
100
1200
70
60
GP 50-50-24-1:1
GP 50-80-48-1:1
GP 60-80-48-1:2
WPI
WPI 50-50-24
WPI 50-80-48
WPI 60-80-48
4
5
pH
Fig. 5. Solubility of WPI controls and GPs in water at different pH values. Samples
nomenclature corresponds to temperature ( C) e relative humidity (%) e time (h) e
molar ratio, respectively. Results are expressed as the percentage of the initial WPI
solubility.
WPI 60-80-48
10
200
WPI50-80-48
20
400
WPI 50-50-24
30
600
Mixture 1:2
40
800
Mixture 1:1
50
1000
WPI
Solubility (%)
80
GP 50-50-241:1
GP 50-80-481:1
GP 60-80-481:2
90
Fig. 6. Foaming capability of whey protein isolate (WPI), untreated mixtures of WPI
and maltodextrins, treated WPI controls, and selected glycoproteins (GP) produced
under different conditions (temperature ( C) e relative humidity (%) e time (h) e
molar ratio). Results are expressed as a percentage of the sample solution volume
before stirring.
80
60
40
20
WPI 60-80-48
WPI50-80-48
WPI 50-50-24
Mixture 1:2
Mixture 1:1
WPI
GP 50-50-241:1
GP 50-80-481:1
GP 60-80-481:2
100
Fig. 7. Foam stability of whey protein isolate (WPI), untreated mixtures of WPI and
maltodextrins, treated WPI controls, and glycoproteins (GP) produced under different
conditions (temperature ( C) e relative humidity (%) e time (h) e molar ratio). Results
are expressed as the time to attain half of the initial foam weight obtained after
stirring.
value (n) of 1, the presence of yield stress (so) in all of them turned
the classication of their behavior into non-Newtonian (Bingham
plastic). Table 2 shows the consistency coefcient (k) and yield
stress (so) observed in the different studied solutions. Consistency
coefcients in general increased as the glycosylation level of the
samples increased, indicating that glycosylation tends to cause a
thickening effect on solutions, probably due to an increased molecular size (hydrodynamic volume). Similar results were published
by Corzo-Martnez et al. (2009). It is noted that only the consistency
coefcient of GP samples with medium and highest glycosylation
levels (GP, 50-80-48-1:1, and GP, 60-80-48-1:2, respectively) were
statistically signicantly different than their own controls. On the
contrary, yield stress tended to decrease with the increase in the
degree of glycosylation, implying that less stress is necessary to
start ow, probably suggesting a lower level of interaction between
proteins as the glycosylation level increases. The yield stress of WPI
controls was not statistically different among them.
4. Conclusions
Glycoproteins with w2.5ew8 maltodextrins attached per WPI
molecule were successfully produced in this study. GPs obtained at
Table 2
Consistency coefcient and yield stress of studied solutions (5% w/v).
Treatment
b
WPI
MD
Mixture 1:1
Mixture 1:2
WPI 50-50-24
WPI 50-80-48
WPI 60-80-48
GP 50-50-24-1:1
GP 50-80-48-1:1
GP 60-80-48-1:2
so (Pa s)a
k (Pa s)a
0.00115
0.00108
0.00134
0.00141
0.00121
0.00113
0.00136
0.00141
0.00154
0.00300
0.00009
0.00006
0.00008
0.00020
0.00001
0.00001
0.00001
0.00003
0.00003
0.00004
c
c
b,c
b,c
b,c
c
b,c
b,c
b
a
0.11913
0.04609
0.13311
0.14733
0.05888
0.05688
0.06228
0.23288
0.12696
0.12608
0.01495
0.00038
0.00288
0.01294
0.00001
0.00001
0.00001
0.00003
0.00003
0.00004
b
c
b
b
c
c
c
a
b
b
a
k and so are the HerscheleBulkley model parameters: consistent coefcient and
yield stress, respectively.
b
Each value is an average of three samples standard deviation. The means
followed by different online letters in the same column are signicantly different
(p 0.05) by Tukeys test. WPI means whey protein isolate, MD means maltodextrin,
and GP means glycoprotein. Numbers of GP correspond to the reaction conditions:
temperature ( C), relative humidity (%), time (h), and molar ratio, respectively.
117
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