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The effects of different levels of skim milk powder and whey powder on
apparent yield stress and density of different meat emulsions

Article  in  Food Hydrocolloids · January 2005


DOI: 10.1016/j.foodhyd.2004.05.001

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Food Hydrocolloids 19 (2005) 149–155
www.elsevier.com/locate/foodhyd

The effects of different levels of skim milk powder and whey powder
on apparent yield stress and density of different meat emulsions
Ömer Zorba*, Şükrü Kurt, Hüseyin Gençcelep
Department of Food Engineering, University of Yüzüncü Yıl, Van 65080, Turkey
Received 26 March 2003; revised 16 September 2003; accepted 4 May 2004

Abstract
The effects of different levels (0.00, 0.25, 0.50%) of skim milk powder (SMP) and whey powder (WP) on emulsion density (ED) and
apparent yield stress values of emulsion (raw emulsion) and emulsion gel (cooked emulsion) of beef, chicken and turkey meats were studied
by using a model system.
The effects of meat and WP were statistically significant ðp , 0:01Þ on ED. Chicken meat and 0.25% WP had the lowest ED values.
The effects of meat, WP and SMP were statistically significant ðp , 0:01Þ on apparent yield stress of emulsion and emulsion gels. Chicken
had lower apparent yield stress of emulsion than beef and turkey. In general, addition of WP and SMP decreased apparent yield stress of
emulsion, but increased that of emulsion gel. Chicken and turkey had higher apparent yield stress of emulsion gel than beef. Between the
levels of WP and SMP, 0.25% WP and 0.50% SMP increased apparent yield stress of emulsion gel. The results suggested that WP and SMP
were important to improve apparent yield stress of emulsion gel, and there was a significant ðp , 0:01Þ negative correlation between ED and
apparent yield stress of emulsion gel.
q 2004 Elsevier Ltd. All rights reserved.
Keywords: Emulsion gel; Milk protein; Skim milk powder; Whey; Chicken; Turkey; Beef

1. Introduction Hongsprabhas & Barbut, 1999). During the gel formation,


fat and water are retained inside the protein matrix in the
Functional properties of milk and meat proteins often products (Smith, 1988). The thermal transition from sol to
determine final quality of meat emulsions. Milk protein gel begins at different temperatures for different proteins.
ingredients widely used for emulsification are casein and Also, it is affected by other conditions like pH, ionic
whey proteins. They have different emulsification strength etc. (Dickinson, 1999). Ziegler and Acton (1984)
characteristics, depending on their physico-chemical prop- reported that such as myosin and actomiyosin denaturation,
erties which affect on the behavior of proteins in food rapid aggregation and subsequent gelation began at
systems during preparation, processing, storage and approximately 55 8C. Also, Zorba (1995) reported that
consumption, and contribute to the quality and organoleptic myofibrillar proteins started thermal aggregation at 50 8C
attributes of food systems (Dickinson & Lopez, 2001; and weak denaturation of meat proteins improved emulsion
Muguruma et al., 2003; Parks & Carpenter, 1987). characteristics. a-Actinin is the most heat-sensitive, and
Gel formation is one of the most important properties of tropomyosin and troponin are the most heat-resistant muscle
proteins. By gel formation, oil-in-water emulsion may be proteins (Foegeding & Lanier, 1996; Zorba, 1995).
converted from liquid-like to solid-like form (Dickinson & Texture is an important characteristic that is significantly
Casanova, 1999). It contributes to desirable texture and influenced by gel strength (Nowsad, Kanoh, & Niwa, 2000).
fat-water emulsion stabilisation in emulsified meat Milk proteins, such as casein and whey proteins can be
products (Clark, Kavanagh, & Ross-Murphy, 2001; Farouk, utilized to improve textural properties of meat emulsions
Wieliczko, Lim, Turnwald, & MacDonald, 2002; (Baardseth, Naes, Mielnik, Skrede, Holland, & Eide, 1992;
Beuschel, Culbertson, Partridge, & Smith, 1992; Ker &
* Corresponding author. Fax: þ 90-43222-51104. Toledo, 1992). These proteins also can be used to increase
E-mail address: omerzorba@yahoo.com (Ö. Zorba). fat binding capacity of meat proteins. Protein solubility and
0268-005X/$ - see front matter q 2004 Elsevier Ltd. All rights reserved.
doi:10.1016/j.foodhyd.2004.05.001
150 Ö. Zorba et al. / Food Hydrocolloids 19 (2005) 149–155

fat binding capacity is an important properties for running, 46 ml corn oil was added at the rate of
determination of emulsion density (ED) (Özdemir, Zorba, 0.9– 1.0 ml/s. After the addition of oil ended the emulsion
& Gökalp, 1994). was mixed for an additional 5 s.
The density of dispersed phase was lower than
continuous phase in an oil-in-water emulsion. This means 2.3. Emulsion density
that the density of an emulsion usually decreases with
increasing oil content (Mcclements, 1999). Özdemir et al. ED measurement is one of the simplest methods of
(1994) found that there was significantly ðp , 0:01Þ determining emulsion properties and it can be required
negative correlation ðr ¼ 20:999Þ between ED and ES inexpensive equipment (Mcclements, 1999; Özdemir et al.,
(emulsion stability). Also, there was significantly 1994). It was determined according to Özdemir et al. (1994).
ðp , 0:05Þ positive correlation ðr ¼ 0:962Þ between ED Emulsion of 20 ml was pipetted with enlarged mouth side
and EV (emulsion viscosity). of the pipette and weighed. It was calculated according to
Zorba, Özdemir, and Gökalp (1998) reported that the equation:
emulsion properties were affected by the constructive
ED ¼ ml of emulsion=g of emulsion
interaction between whey and muscle proteins.
Functionality of these non-meat proteins in meat emulsions
has been estimated by model systems. Many researchers use 2.4. Apparent yield stress of emulsion
model systems to determine emulsification properties of
proteins (Hung & Zayas, 1991; Vuillemard, Gauthier, Apparent yield stress was determined by using the cone
Richard, & Paquin, 1990; Zorba, Gökalp, Yetim, & penetrometer (ELE, ELE Int. Ltd, UK). Special conical
Ockerman, 1993; Zorba et al., 1998). head (with 308 cone angle and 34.64 g weight) was placed
The objective of this study was to determine the effects of just above the surface of the emulsions and released.
SMP and WP on apparent yield stress of emulsion and Penetration depth was read after 5 s of penetration
emulsion gel and emulsion density of beef, chicken and (Rousseau & Marangoni, 1998). Three replicates were
turkey meat by using a model system. performed for each sample. Then, apparent yield stress
(AYS) was calculated as:
gw
2. Materials and methods AYS ðN=m2 Þ ¼
pd2 tan2 ð1Þ
Meat sources used in this study were beef where g is acceleration due to gravity, w is the weight of
(M. semimembranocus), chicken and turkey breast muscles. the cone assembly, 1 refers to the cone angle and d is
Also, SMP and WP obtained from local markets. The meats the penetration depth (Wright, Scanlon, Hartel, &
were ground separately using grinder (Kenwood KM300) Marangoni, 2001).
with a 5 mm diameter hole plate. Each ground meat was
divided to equal lots and packaged by three layers of 2.5. Preparation of emulsion gel and measurement
medium density polyethylene plus aluminum foil and stored of apparent yield stress
at 2 18 8C for 2 weeks. Refined corn oil was used in the
emulsion preparation. Emulsion was immediately transferred into the jars.
After heat treatment at 80 8C in a water bath for 30 min,
2.1. Homogenate preparation emulsion was transferred into a refrigerator immediately
and cooled to approximately 20 8C. Then, emulsion gel
NaCl solution of 0.4 M was prepared and adjusted to pH (cooked emulsion) was held for temperature standardisation
6.6. Solution of 100 ml (2 – 4 8C), 25 g ground meat, for 1 h at room condition and apparent yield stress was
SMP and WP were placed into a blender (Waring-80011S) determined as described in testing of emulsion.
jar and blended for 1 min at 18,000 rpm. Addition levels of
SMP and WP were calculated according to second 2.6. pH Determination
homogenate.
The pH of the prepared NaCl solution and materials was
2.2. Emulsion preparation measured by a pH meter equipped with temperature probe
(Hanna 8521) as outlined by Ockerman (1985).
Emulsion was prepared by using a model system, as
described by Ockerman (1985) and Zorba et al. (1993). 2.7. Statistical analyses
Solution of 37.5 ml and 12.5 g homogenate were placed into
the blender (Kenwood KM300) jar and homogenised at Data were analysed with ANOVA using a random
6500 rpm for 10 s. Corn oil of 50 ml was placed into the factorial design. Basic statistics and analysis of variance
second homogenate at first. While emulsification was were performed to test significance within replications
Ö. Zorba et al. / Food Hydrocolloids 19 (2005) 149–155 151

Table 1 Nakai, & Wood, 1985). Protein solubility increase with


Properties of meat sources, WP and SMP increasing or decreasing pH from isoelectric points and this
pH Protein Fat Moisture Ash affects on water and fat binding properties of meat emulsions.
(%) (%) (%) (%) Turkey and chicken meat had significantly ðp , 0:01Þ
higher apparent yield stress values of emulsion gel than beef
Beef 5.51 20.49 2.7 76.14 1.07 (Table 3), because of higher pH of turkey and chicken
Chicken breast meat 6.14 21.73 3.0 74.86 1.24 meats. pH and heat treatment are important factors on the
Turkey breast meat 5.87 22.82 3.2 73.94 1.19
properties of the gel network. Also myosin and actomyosin
Whey powder (WP) 5.96 8.12 4.0 4.08 7.82
Skim milk powder (SMP) 6.52 34.20 0.8 4.72 7.91 gel strengths increase with pH (optimum 5.5 –6.0) during
heat treatment (Ziegler & Acton, 1984). The gelation is an
important property of myofibrillar proteins requiring heat
and between treatments (Mstat-C, 1986). Significant means treatment. This property is largely affected by physical and
of treatments and interactions were further analysed with chemical stabilisation fat and water in meat products (Schut,
Tukey multiple range test. 1976; Ziegler & Acton, 1984). Also, Li-Chan et al. (1985)
reported that heat treatment may improve emulsifying and
fat binding properties.
3. Results and discussion The addition of WP and SMP decreased apparent yield
stress of emulsion significantly ðp , 0:01Þ (Table 3).
Some properties of meats, WP and SMP are summarised Milk contains more globular proteins which decrease
in Table 1. viscosity of emulsions (Işık & Gökalp, 1996). Although
WP and SMP decreased apparent yield stress of emulsion,
3.1. Apparent yield stress of emulsion and emulsion gel they increased significantly ðp , 0:01Þ apparent yield stress
of emulsion gel (Table 3). This result might be due to the
The results of analysis of variance indicating apparent partially dissociation of globular proteins during heat
yield stress values of emulsion and emulsion gel were treatments (Clark et al., 2001). The functionality of such
summarised in Table 2. The effects of meats, WP, SMP and milk proteins is not only related with emulsion formation
their interactions were significant ðp , 0:01Þ on apparent but also related with improving textural properties of
yield stress of emulsion and emulsion gel. food products (Hughes, Mullen, & Troy, 1998; Ker &
Beef and turkey meat had significantly ðp , 0:01Þ higher Toledo, 1992; Lyons, Kerry, Morrissey, & Buckley, 1999;
apparent yield stress values of emulsion than chicken meat Muguruma et al., 2003). WP and SMP contains lactose
(Table 3). This result might be due to lower pH of beef and which can interact with proteins during heat treatment,
turkey meat (Table 1). Chicken meat had higher pH and it therefore improve gel strength (Işık & Gökalp, 1996).
was probably caused higher solubility of proteins.
Thus, chicken meat emulsion required higher amount of fat 3.2. The effects of two and three way interactions
for binding. The pH values of beef and turkey meat among variables on apparent yield stress
approached to the isoelectric point of the salt-soluble of emulsion and emulsion gel
myofibrillar proteins. As the net electrical charge density
approaches to zero, the reducing electrostatic repulsion cause The addition of WP decreased apparent yield stress
insoluble aggregate formation (Dickinson, 1998; Li-Chan, values of emulsion of beef significantly ðp , 0:01Þ

Table 2
Analysis of variance of the effects of different meats, WP and SMP on apparent yield stress values of emulsion and emulsion gel

Sources of variation Degrees of freedom Emulsion Emulsion gel

Mean square F value Mean square F value

Meat 2 632.002 54.1871** 60822.96 142.2705**


WP 2 237.409 20.3552** 13145.32 30.7481**
SMP 2 917.452 78.6613** 16059.16 37.5639**
Meat £ WP 4 435.515 37.3405** 10618.69 24.8381**
Meat £ SMP 4 517.133 44.3384** 1917.902 4.4861**
WP £ SMP 4 192.450 16.5004** 4087.454 9.5609**
Meat £ WP £ SMP 8 186.853 16.0206** 1771.844 4.1445**
Error 54 11.663 427.516
Total 80

**p , 0:01 significance level.


152 Ö. Zorba et al. / Food Hydrocolloids 19 (2005) 149–155

Table 3 Table 5
Mean apparent yield stress values showing the effect of different meats and The effects of Meat £ SMP interactions on apparent yield stress values of
levels of WP and SMP emulsion and emulsion gel

Variables Apparent yield stress (N/m2) SMP (%)

Emulsion Emulsion gel Emulsion Emulsion gel

Meat ðn ¼ 27Þ Beef 180.8a 437.2b Meat 0.00 0.25 0.50 0.00 0.25 0.50
Chicken 173.5b 525.1a Beef 192.1a 174.8bc 175.4bc 411.0d 429.6d 471.0c
Turkey 182.7a 512.2a Chicken 170.5c 171.1c 179.0b 499.0bc 511.8b 564.4a
Turkey 194.1a 177.4b 176.6bc 507.0bc 508.2bc 521.4b
WP (%) ðn ¼ 27Þ 0.00 182.4a 467.5b SE 1.138 6.892
0.25 177.3b 511.0a
0.50 177.2b 495.9a a–c
The mean values with the same letters within a group for a variable
SMP (%) ðn ¼ 27Þ 0.00 185.6a
472.3 b are not significantly different ðp , 0:01Þ from each other.
0.25 174.4b 483.2b
0.50 177.0b 518.9a It is widely suggested that myofibrillar proteins,
SE 0.657 3.979
particularly myosin, are responsible for the bind strength
a–c
The mean values with the same letters within a group for a variable of cooked meat batters. Myosin contains two globular head
are not significantly different ðp , 0:01Þ from each other. attached to the end of a rod-like tail (Smith, 1988; Ziegler &
Acton, 1984). For the heat-induced gelation of myosin, two
and increased chicken significantly ðp , 0:05Þ (Table 4). reactions take places, which are aggregation of the globular
Also, the effects of WP addition were not significant for head segments and network formation, which resulted from
turkey. The addition of 0.25% WP increased apparent yield the unfolding helical segment. Gel can be stabilised from
stress values of emulsion gel of beef significantly ðp , 0:01Þ the interactions between segments, which had non-covalent
and increasing WP addition increased apparent yield stress in nature (Ziegler & Acton, 1984). During heat treatment,
values of emulsion gel of chicken and turkey meat light chains of myosin are dissociated and solubilised,
significantly (Table 4). The addition of SMP decreased therefore heavy chains are necessary to obtain maximum gel
apparent yield stress values of emulsion of beef and turkey strength (Smith, 1988; Ziegler & Acton, 1984). In the
meat significantly ðp , 0:01Þ and increased significantly myosin rod, the major changes involve protein complex
ðp , 0:01Þ chicken (Table 5). The addition of SMP dissociation and molecule unfolding at 55 8C or higher
generally increased apparent yield stress values of emulsion temperatures (Li-Chan et al., 1985; Ziegler & Acton, 1984).
gel of beef, turkey and chicken meats (Table 5). It can Milk proteins used in comminuted meat products differ
conclude that addition of SMP increased apparent yield significantly in functionality, but generally bind water,
stress values of emulsion gel of all treatments. improve overall yields, stabilise fat and impart texture
The effects of WP addition with SMP generally decreased upon gelation (Ensor, Mandigo, Calkins, & Quint, 1987;
emulsion and increased apparent yield stress of emulsion gel Parks & Carpenter, 1987). Non-meat proteins do not produce
(Table 6). WP and SMP addition into the meats (beef and gel strength similar to muscle proteins. The gel properties are
turkey) generally decreased apparent yield stress values of affected not only by the relative contribution of various
emulsion (Fig. 1) and generally increased apparent yield protein fractions but also by their interactions (Hongsprabhas
stress values of emulsion gel (Fig. 2). However, 0.50% & Barbut, 1999; Nowsad et al., 2000). Functional and
WP £ 0.50% SMP £ Chicken meat and 0.25% WP £ 0.50% textural effects of non-meat proteins in meat emulsion
SMP £ Beef interactions had higher apparent yield stress systems, generally indicating high performance with meat
values of emulsion gel (Fig. 2). proteins (Parks & Carpenter, 1987). Zorba et al. (1998)

Table 4 Table 6
The effects of Meat £ WP interactions on apparent yield stress values of The effects of WP £ SMP interactions on apparent yield stress values of
emulsion and emulsion gel emulsion and emulsion gel

WP (%) SMP (%)

Emulsion Emulsion gel Emulsion Emulsion gel

Meat 0.00 0.25 0.50 0.00 0.25 0.50 WP (%) 0.00 0.25 0.50 0.00 0.25 0.50
Beef 192.8a 177.3bc 172.3c 418.0e 493.2cd 400.4e 0.00 194.6a 176.5bcd 176.2cd 451.7d 471.6cd 565.7a
Chicken 171.9c 171.7c 177.0bc 505.6bcd 522.9abc 546.8a 0.25 182.5b 171.9d 177.6bcd 484.8bcd 482.5bcd 479.2bcd
Turkey 182.7b 183.0b 182.4b 479.0d 516.9abc 540.6ab 0.50 179.6bc 174.8cd 177.3bcd 480.4bcd 495.5bc 511.9b
SE 1.138 6.892 SE 1.138 6.892
a–c a–c
The mean values with the same letters within a group for a variable The mean values with the same letters within a group for a variable
are not significantly different ðp , 0:01Þ from each other. are not significantly different ðp , 0:01Þ from each other.
Ö. Zorba et al. / Food Hydrocolloids 19 (2005) 149–155 153

Fig. 1. The effects of Meat £ WP £ SMP interactions on apparent yield stress value of emulsion.

Fig. 2. The effects of Meat £ WP £ SMP interactions on apparent yield stress of emulsion gel.

reported that the constructive interactions between whey and solubility. Beef had higher ED that can be concluded from
meat proteins might arise. Milk proteins which adding to lower pH, which was near the isoelectric points of the meat
emulsified meat products, can interact directly with meat proteins, particularly myosin. Thus, the insoluble aggregate
proteins, can improve gel properties of the system (Mugur- formation increased (Li-Chan et al., 1985).
uma et al., 2003). Important functional properties of milk
proteins come from their molecular structures. Caseinates Table 7
contain higher amount of proline, lower S –S bonds and whey Analysis of variance of the effects of different meats, WP and SMP on ED
proteins contain lower amount of proline, many S –S bonds values
(Özdemir et al., 1994; Smith, 1988; Zorba et al., 1998). Sources of variation Degrees of freedom Mean square F value

3.3. Emulsion density Meat 2 5.83 £ 1023 249,832**


WP 2 4.72 £ 1024 20,231**
SMP 2 7.64 £ 1026 0.327
The results of analysis of variance which were Meat £ WP 4 4,79 £ 1024 20,525**
summarised in Table 7, indicated that the effects of meats, Meat £ SMP 4 1.07 £ 1024 4.593**
WP, SMP and their interactions, except SMP and SMP £ WP £ SMP 4 2.60 £ 1025 1.113
Meat £ WP £ SMP 8 1.31 £ 1024 5.596**
WP interaction, were significant ðp , 0:01Þ on ED. Error 54 2.34 £ 1025
Chicken meat had significantly ðp , 0:01Þ lower ED than
Total 80
beef and turkey meat (Table 8). This result may have
occurred due to higher pH, which caused increasing protein **p , 0:01 significance level.
154 Ö. Zorba et al. / Food Hydrocolloids 19 (2005) 149–155

Table 8 capacity of unit protein (Zorba et al., 1993) so that negative


Mean ED values showing the effect of different meats and levels of WP and correlation might be possible between EC and ED. Kurt and
SMP
Zorba (2003) found that it was significant negative
Variables ED correlation between ED and EC also ES (emulsion stability)
from second part of this research.
Meat ðn ¼ 27Þ Beef 0.903a
Chicken 0.874c
Turkey 0.891b
WP (%) ðn ¼ 27Þ 0.00 0.892a
3.4. The effects of two and three way interactions
0.25 0.884b among variables on ED
0.50 0.892a
SMP (%) ðn ¼ 27Þ 0.00 0.889a
0.25 0.890a As shown in Table 9, addition of 0.25% WP decreased
0.50 0.890a ED values of beef significantly ðp , 0:01Þ: Vuillemard et al.
SE 0.001 (1990) noted that, increasing fat binding capacity is not
a–c
The mean values with the same letters within a group for a variable linear with increasing concentration of protein, and might be
are not significantly different ðp , 0:01Þ from each other. decreased after critical concentration. The effect of WP
addition was not found significant on ED of chicken and
turkey meat (Table 9).
Table 9 The effect of SMP addition was found significant ðp ,
The effects of Meat £ WP and Meat £ SMP interactions on ED 0:05Þ on ED of beef and turkey meat (Table 9). In
WP (%) SMP (%)
meat £ WP £ SMP interaction, SMP addition generally
increased ED of beef and decreased ED of turkey meat.
Meat 0.00 0.25 0.50 0.00 0.25 0.50 Also, 0.25% WP addition decreased ED of beef significantly
Beef 0.910a 0.888b 0.911a 0.900ab 0.904ab 0.905a
(Fig. 3).
Chicken 0.874c 0.874c 0.873c 0.871d 0.875d 0.876d
Turkey 0.891b 0.891b 0.891b 0.895bc 0.891c 0.888c
SE 0.0016 0.0016
a–c
3.5. Results of correlation analysis
The mean values with the same letters within a group for a variable
are not significantly different ðp , 0:01Þ from each other.
According to the results of research, there was
significant ðp , 0:01Þ negative correlation ðr ¼ 20:652Þ
The effect of 0.25% WP was statistically significant on between ED and apparent yield stress of emulsion gel.
ED (Table 8). Zorba, Yetim, Özdemir, and Gökalp (1995) This correlation was an indication of the relationship
reported that protein solubility increased with addition of between ED and apparent yield stress of emulsion gel,
whey to the total meat proteins. Özdemir et al. (1994) noted which might be a valuable quality criteria of meat
that, ED was important parameter for high amount of fat emulsions. Also, there was significant ðp , 0:05Þ positive
containing emulsions, as much as emulsion stability (ES) correlation ðr ¼ 0:286Þ between ED and apparent yield
and emulsion capacity (EC). EC is the maximum fat binding stress of emulsion.

Fig. 3. The effects of Meat £ WP £ SMP interactions on ED.


Ö. Zorba et al. / Food Hydrocolloids 19 (2005) 149–155 155

4. Conclusion Işık, F., & Gökalp, H. Y. (1996). Peyniralti suyu ve peyniralti suyu tozunun
emülsiyon özellikleri ve gida sanayiinde bu amaçla kullanimlari II
(in Turkish). Standard, (Kasım), 61–68.
Chicken meat had lower ED and higher apparent yield Ker, Y. C., & Toledo, R. T. (1992). Influence of shear treatments on
stress of emulsion gel than beef and turkey meat. consistency and gelling properties of whey protein isolate suspensions.
These results might arise from pH and myofibrillar proteins. Journal of Food Science, 57(1), 82– 86.
WP and SMP increased cooked meat emulsion apparent Kurt, Ş., and Zorba, Ö., (2004). The effects of different levels of skim milk
yield stress. They contain many globular proteins which powder and whey powder on emulsion capacity and stability of different
meats (submitted for publication).
have often been unfolding during heat treatment, so that Li-Chan, E., Nakai, S., & Wood, D. F. (1985). Relationship between
they effect directly the mechanisms of gel formation. functional (fat binding, emulsifying) and physicochemical properties of
According to the correlation analysis results, a significant muscle proteins, effects of heating, freezing, pH and species. Journal of
negative correlation was found between emulsion density Food Science, 50, 1034–1040.
and apparent yield stress of emulsion gel. Lyons, P. H., Kerry, J. F., Morrissey, P. A., & Buckley, D. J. (1999).
The influence of added whey protein/carrageenan gels and tapioca
starch on the textural properties of low fat pork sausages. Meat Science,
51, 43–52.
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