Journal of Food Engineering 104 (2011) 323331

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Journal of Food Engineering

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Effect of whey protein concentration on the fouling and cleaning of a heat transfer surface
Adel Fickak, Ali Al-Raisi, Xiao Dong Chen
Biotechnology and Food Engineering Group, Department of Chemical Engineering, Monash University, Clayton Campus, Victoria 3800, Melbourne, Australia

a r t i c l e

i n f o

a b s t r a c t
In the studies of fouling and cleaning of heat exchange surfaces in dairy plants, whey protein deposits and heat induced whey protein gels (HIWPG) are considered as suitable model material to simulate the proteinaceous based type A milk fouling. Protein concentration of the fouling solution may signicantly inuence the formation of milk deposits on heat exchange surfaces, hence affecting the cleaning efciency. In this study, a laboratory produced heat induced whey protein gels (HIWPG) and a pilot plant heat exchanger fouling/cleaning were used to investigate the effect of protein concentration on formation and cleaning of dairy fouling. Here, HIWPGs made from different protein concentrations were formed in capsules and then dissolved in aqueous sodium hydroxide (0.5 wt%). The dissolution rate calculation based on the UV spectrophotometer analysis. In the pilot-scale plant study, whey protein fouling deposits were formed by recirculating whey protein solutions with different concentrations through the heat exchange section in different runs, respectively. The deposit layers were then removed by recirculating aqueous sodium hydroxide (0.5 wt%) and the cleaning efciency was monitored in the form of the recovery of heat transfer coefcient while both uid electric conductivity and turbidity were monitored as indications of cleaning completion. It was found that increasing the protein concentration of the HIWPG signicantly increased the gel hardness and the dissolution time. In addition, increasing the protein concentration signicantly increased both, the amount of the fouling on the pilot-scale plant and the time required to clean the fouling deposit. 2010 Elsevier Ltd. All rights reserved.

Article history: Received 11 March 2010 Received in revised form 4 November 2010 Accepted 10 November 2010 Available online 28 December 2010 Keywords: Cleaning-in-place (CIP) Fouling Heat induced gels Dissolution Dairy processing

1. Introduction During the thermal processing of dairy products, deposit layers are often formed on the process surface of the heat exchangers. The cleaning, or removal, of such deposits is crucial for quality and safety issues. Cleaning using chemicals is costly, both economically and environmentally (Toyoda et al., 1994). The fouling and cleaning of proteinaceous deposits have received considerable attention due to their importance in the dairy industries (Visser, 1997). In the last decades, the understanding of the fouling and cleaning processes in dairy plants has been considerably improved (Fryer et al., 1996a; Wilson et al., 1999, 2002; Chen et al., 2004). The major components in dairy fouling deposits are the heat-sensitive whey proteins (Visser, 1997). In fact aggregated whey protein molecules dominate the basic structure of the fouling deposits. Because of this and also the complex nature of milk deposits, many researchers (Belmar-Beiny et al., 1993; Schreier et al., 1994; Delplace and Leutiet, 1995; Fryer et al., 1996b; Davies et al., 1997;

Corresponding author. Tel.: +61 3 99059344; fax: +61 3 99055686.

E-mail address: dong.chen@eng.monash.edu.au (X.D. Chen). 0260-8774/$ - see front matter 2010 Elsevier Ltd. All rights reserved. doi:10.1016/j.jfoodeng.2010.11.004

Gillham et al., 1999; Chen et al., 2000, 2001; Xin et al., 2002a,b), found heat induced whey protein gels (HIWPG) to be a reliable model system for investigating milk fouling and cleaning. Heat induced whey protein gel (HIWPG) also contain a small quantity of minerals and have been found to have the same nature of type A milk deposits described by Lyster (1965) and Burton (1968), where proteins represent more than 60 wt% of the deposit mass. The formation of the HIWPG deposits results from the aggregation of whey proteins upon heating. At the time a HIWPG is formed, only a fraction of the whey proteins has aggregated (Verheul and Roef, 1998a,b). The magnitude of this fraction, as well as the gel point, depends on many factors such as the gelation pH, temperature and protein concentration (Mulvihill et al., 1990; Langton and Hermansson, 1992; Renard and Lefebvre, 1992; Verheul and Roef, 1998a). HIWPG with high protein concentration tend to form faster due to the increasing rate of aggregation and the decreasing coagulation time (Sharma and Hill, 1993). A Study by Mleko (1999) has found that increasing the protein concentration will increase the rmness and the aggregate size of WPC gels, accelerating the gelation process. Furthermore, a study by Puyol et al. (2001) found that WPI gels with high protein concentration tend to form at lower temperature.

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Nomenclature Q A T power requirement (W) heating surface area (m2) temperature (C) slope of the curve of the heat transfer coefcient versus time fouling resistance fouling layer thickness cleaning-in-place heat induced whey protein gel whey protein concentrate heating time temperature difference between the heater surface and the bulk solution (C) Subscripts S heater surface B bulk WPC HT DT

a
R d CIP HIWPG

All of these studies clearly show that high protein concentration can greatly inuence the formation mechanisms of whey protein gels; however, the effect of protein concentration on the fouling and cleaning of dairy heat exchange surface has not been demonstrated quantitatively. The dissolution of HIWPG has been studied extensively by Xin et al. (2002a) and Mercad-Prieto and Chen (2006) as mechanistic investigation of alkaline cleaning of proteinaceous deposits. They presented dissolution or cleaning mechanisms based on the breakdown of protein aggregates, diffusion of small oligomers throughout the swollen layer, and disentanglement of large aggregates next to the gelsolvent boundary layer. However, little is known about the effect of protein concentration within fouling and heat induced whey protein gel on their dissolution. Moreover, the cleaning of whey protein based deposits has also been studied using test rig experiments by a number of researchers (Bird and Fryer, 1991; Gillham et al., 1999, 2000). In these studies, the cleaning was achieved by circulating NaOH solution through the equipment. In most cleaning studies, a single fouling protocol is used while the cleaning conditions are modied. It is therefore important to understand the implication of the fouling solution conditions (e.g. protein concentration) on cleaning. In this study, the effect of whey protein concentration on the formation and dissolution behaviours of HIWPG has been investigated. Also, the effect of whey protein concentration on the fouling and cleaning behaviours of a pilot-scale heat exchanger has been studied using whey protein concentrate as the foulant solution.

eto and Chen (2006) were used in the current study. All gels were prepared in triplicate and the error bars are presented using excel. An experimental apparatus (Fig. 1) was employed to dissolve HIWPG in the laboratory. The apparatus consisted of an analytic balance, a digital magnetic stirrer plate with a stirring speed controller, a digital controller for the water bath, a dissolution cell (a 600 ml shock bottle and a capsule holder) and a peristaltic pump to recirculate the solutions through a UV spectroscopy that was linked to a computer. The HIWPGs were formed in capsules using the method developed by Mercad-Prieto et al. (2008). HIWPGs were formed inside test tubes (diameter 12 mm; length 75 mm) using well mixed whey protein solutions with different concentrations (14, 20, and 26 wt%, respectively). The capsules were lled with the whey solution, then sealed with plastic stoppers and covered with foil, and then held vertically in a water bath kept at 80 C for 1 h. The top 2 mm of the gel was removed with a spatula to ensure an even surface before each dissolution experiment (Mercad-Prieto et al., 2008). The gels were kept at 4 C overnight before use. The gel capsules were then dissolved in batch mode and the dissolution rate of each gel was calculated based on the measured increase of the dissolved protein concentration in the NaOH solution over time. The concentration of NaOH solution was veried by titration of an aliquot with HCl (0.01 N). As shown in Fig. 1, the gel capsules were held vertically with stainless steel wire that was xed to a hole at the top of the bottle lid and submerged inside a 600 ml test bot-

2. Experimental 2.1. Material Whey protein concentrate (WPC 85) powder was obtained from local suppliers. The approximate composition of the WPC is given in Table 1. The cleaning reagent, 60 wt% sodium hydroxide solution (NaOH), was purchased from LabServ, Melbourne, Australia. 2.2. Methods 2.2.1. Preparation of HIWPG in the lab and dissolution experiments The same sort of heat induced gels and the methodologies that were previously employed by Xin et al. (2002a) and Mercad-Pri-

Return line from UV-S To UV-S

75 m m 12mm

Table 1 Whey protein concentrate (WPC) powder composition. Component Proteins Fat Moisture Ash Content (wt%) 82.0 6.2 3.5 8.3

1. Dissolution solvent (0.5 wt %) NaOH 2. Capsule containing heat induced whey protein gel 3. Magnetic stirrer 4. Water bath 5. Pump 6. Heater
Fig. 1. Apparatus for the dissolution of heat induced whey protein gels.

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tle containing 500 ml of NaOH (0.5 wt%) solution, which was placed in a water bath at 60 1 C. The solution was stirred at 200 rpm using a magnetic stirrer to ensure the reading of a well mixed solution. A small fraction of the agitated solution was circulated through the cell of a UV spectrometer (HP Agilent 8453 Spectrophotometer, model number: G1103A, Agilent Technologies, Melbourne, Australia) using a peristaltic pump. Using the method of Mercad-Prieto and Chen (2006), the absorbance of the dissolved proteins was continuously recorded at 20 s intervals for at least 8000 s at wavelength 280 nm. The dissolution rate was calculated by measuring the increase of the concentration of protein in the alkali solution over time. 2.2.2. Gel strength measurement The mechanical properties, such as the hardness, of HIWPGs are affected by the protein concentrations in the gels. A simple effective technique to measure the change in gel strength and cohesiveness is the depth sensing indentation hardness test, which has been widely used for characterizing the consistency of fats and other materials (DeMan, 1983). The test involves the penetration of a sample surface by a metal probe indenter with a known geometry (DeMan, 1969). A parameter referred to as the yield value or hardness index of a sample can be calculated by monitoring the penetration force of the probe and the time taken to achieve that penetration depth (DeMan, 1983; Narine and Marangoni, 2001). The sample gels were made in a 50 ml beaker using 10 ml of well mixed whey protein solutions at concentrations of 14 and 26 wt% and held in a water bath at 80 C for 2 h. The gels were kept at

4 C overnight and brought to room temperature (23 2 C) before being tested. The texture analyses were performed at room temperature (23 2 C) using a EZ Graph texture analyser (EZ Graph 100 N, Shimadzu Scientic Instruments, Melbourne, Australia) equipped with a 100-N load cell, and a 12.8 mm diameter cylindrical probe. The test procedure was developed using Shimadzu Instruments texture tests guidelines. The test was performed by allowing the probe at speed of 50 mm min1 to penetrate 10 mm into the gel, and the force at 5 mm of penetration was taken as gel strength value. 2.2.3. Microstructure analysis Images of the microstructure of the gel samples were obtained using Scanning Electron Microscope (SEM) (JEOL JSM-840A SEM, 1986, Japan), located at Monash University, Clayton Campus, Melbourne, Australia. Prior to image scanning, 2 mm2 gel samples were sliced and placed in a dry oven at 30 C for 10 min. The gel samples were then sputter coated (approximately 1 mm) with gold palladium for charge dissipations. The samples were then viewed with the SEM operating at 15 KV using back scattering electrons. 2.2.4. Pilot-scale fouling and cleaning-in-place (CIP) experiments A pilot-scale plant test rig was designed to generate and remove whey protein fouling layers (Fig. 2). A 60 L reservoir was equipped with heating coils to preheat the sample solutions. The solution in the holding tank was stirred continuously by re-circulating

1 Tank including coiled heater 2 Centrifugal pump 3 Flow meter 4 Fouling section (include a heater rod) 5 Conductivity meter 6 Turbidity meter 7 Computer for temperature, turbidity and conductivity recording

TI-1: Tank temperature sensor TI-2: Fouling section inlet temperature sensor TI-3: Heater rod bottom surface temperature sensor TI-4: Heater rod middle surface temperature sensor TI-5: Heater rod top surface temperature sensor TI-6: Bulk solution temperature sensor TI-7: Fouling section outlet temperature sensor ( (TI-3) + (TI-4) + (TI-5)) / 3: Surface temperature

Fig. 2. Fouling and cleaning test system.

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Table 2 Pilot plant operation conditions during fouling and CIP processes. Operation variable Feed tank liquid volume Feed tank temp Velocitya Heat ux
a

Fouling 50 L 70 0.5 C 0.1 cm s1 6.56 kW m2

CIP 50 L 60 0.5 C 10.4 cm s1 1.098 kW m2

At the start of the experiment, the heater rod surface temperature (the average of the temperature around the outside diameter of the heater rod upper, middle and bottom surface) was obtained at approximately 81 1 C by applying the heat ux described in Table 2 using a 5A variac autotransformer. The fouling layer formed in each run was found to be reasonably evenly distributed along the heater rod surface. 2.2.6. Monitoring of fouling The fouling process was monitored through the change in the heat transfer coefcient. A drop in the heat transfer coefcient indicates the formation of a fouling layer on the heater surface. The heat transfer coefcient was calculated using the following equation:

Based on the cross-sectional area of the heater section (the annuli).

through the bypass valves. A centrifugal pump was used to ensure an easy circulation of sample solutions. The owrate in the heating section was kept constant (Table 2) during the fouling and cleaning processes and monitored through a owrate meter (Model 257133 from RS Components, Melbourne, Australia) installed at the inlet of the fouling section. The velocity was calculated using the owrate and the heating section area. The fouling section consisted of a heater rod (diameter = 17 mm, length = 160 mm) xed inside a sealed glass tube reactor (ID = 80 mm with length = 300 mm) with the bottom inlet of ID = 20 mm. Three outlets (ID = 20 mm) were uniformly distributed (120 apart) at the top. Other devices such as a turbidity meter (Model TB750G) and conductivity meter (Model DC402G) from YOKOGAWA Electric Corporation, Melbourne, Australia) were installed downstream of the fouling section to monitor the cleaning process. In the current study, the rig operating conditions were kept constant for each run (see Table. 2). Fig. 3 shows a typical plot of the ow rate record. The velocity values indicate to the ow of the medium inside through the heating section. The very low velocity used for fouling was to exaggerate the fouling process as the removal due to the shear is minimized. Also, the freshness of the concentrate in the tank can last longer as the fouling is understood to be primarily due to the action of whey protein (in fact the native whey proteins). In the cleaning process, high velocity was used to improve the shear removal in any case. 2.2.5. Generation of the fouling layer Whey proteins concentrate powder (WPC, 80 wt%) was reconstituted to protein concentrations of 2, 4 and 6 wt% solids, respectively in 50 L of RO water. The solution was then transferred to the holding tank and preheated to approximately 70 0.5 C and then held for 5 min before being pumped through the fouling section and back to the tank. The recirculation of the solution in the holding tank through the bypass valve results in a continuous stirring of the solution, this help to sustain the required tank temperature.

U

Q AT S T B

where U = overall heat transfer coefcient (W m2 K1); Q = power input to the heater rod (W); A = heater rod surface area (m2); TS = heater rod surface temperature (C) (the average of the temperature around the outside diameter of the heater rod upper, middle and bottom surface); TB = bulk uid temperature (C) measured in the fouling section. 2.2.7. Monitoring the temperature As mentioned above the average temperature measurement of the heater rod surface was obtained by attaching three thermocouples around the outside diameter of the upper, middle and bottom surface of the heater rod. The bulk uid temperature was measured through another thermocouple that was placed inside the bulk solution in the heating reactor. The inlet and outlet temperatures of the fouling section were monitored using thermocouples inserted at the inlet and outlet of the fouling section. The tank temperature was monitored using a thermocouple located at the centre of the tank. All measured temperatures (surface, bulk, inlet, outlet and tank) were logged to a computer. 2.2.8. Cleaning of the fouled surface The fouled surface was cleaned using a three-stage cleaning method. In the rst stage, after the fouling layer was formed, the whey protein solution was drained and the system was rinsed with water at a velocity of 10.423 cm s1 (for approximately 10 min), until there were no protein traces left in the rinsing water. The rinsing efciency was indicated using the turbidity meter (see Fig. 4 for one example). The rinsing process was stopped once
30

0.5

25

Flowrate (L/min)

0.4

Turbididty (NTU)

20

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0.2

10

0.1

0 0

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1000 1500 2000

2500 3000 3500 4000

4500

0 0

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800 1000 1200 1400 1600 1800 2000

Time (s)
Fig. 3. Velocity during the fouling process.

Time (s)
Fig. 4. Turbidity measurements of the rinsing water during the CIP process.

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the standard turbidity of drinking water (0.51 NTU) was reached (USEPA, 2001). In the second stage, a cleaning solution (50 L of NaOH at 0.5 wt%) was used. During cleaning, the cleaning solution temperature was kept constant at 60 0.5 C. In the cleaning-in-place (CIP) process, rst the cleaning solution was recirculated through the system. The heater rod surface temperature (approximately 66 0.5 C) was obtained by applying the heat ux described in Table 2 using an enclosed 5A variac autotransformer. The CIP process was monitored visually by observing the change in the heat transfer coefcient and by observing the complete removal of the fouling layer through the glass wall of the fouling section (see Fig. 9b). An increase of the heat transfer coefcient corresponds to the removal of the fouling layer on the heater surface. The CIP solution was drained when the fouling layer was seen to be completely removed.

In the third stage, the system was continuously rinsed with water for approximately 10 min until there were no NaOH traces left in the rinsing water. The rinsing efciency at this stage was monitored using the conductivity meter (see Fig. 5 for one example). The rinsing was stopped when the typical conductivity of drinking water (<500 lS/cm) (DeZuane, 1990) was reached. The turbidity and conductivity measurements were both used to indicate the efciency of the cleaning process.

3. Results and discussion 3.1. Inuence of protein concentration on HIWPG formation From the SEM images of the microstructure of HIWPG (see Fig. 6), it is clear that HIWPG with high protein concentration 26 wt% (Fig. 6a) contain larger aggregate sizes than HIWPG with lower protein concentration 17 wt% (see Fig. 6b). These observations are consistent with the observations of Mleko (1999) who reported that increasing the protein concentration results in increasing the aggregate size of the whey protein gel. These results can be explained as follows. Whey protein solution contains a number of cysteine residues and upon heating the free SH groups of cysteine residues get oxidized and form disulphide bonds. These bonds are involved in cross-linking proteins to form large aggregates. However, increasing the protein concentration in the solution will ultimately increase the number of cysteine residues in the solution. According to Skudder et al. (1981), increasing the level of free SH group, accelerates the rate of the gel formation by increasing the number of disulphide cross links between the protein molecules. This in turn leads to an increased aggregation rate (Sharma and Hill, 1993) aggregate size (see Fig. 6a) and number of aggregates (Mleko, 1999), resulting in the formation of a hard and rigid gel. In the current study, such hard and rigid gel was obtained. The texture analysis results (Fig. 7) show that a higher force was required (approximately 48 N) to penetrate the HIWPG with high protein concentration compared to the HIWPG with lower protein concentration. This suggests that HIWPG with high protein con-

1200

1000

Conductivity (S)

800

600

400

200

0 0 200 400 600 800 1000 1200

Time (s)
Fig. 5. Conductivity measurements of the rinsing water during the CIP process.

Fig. 6. SEM images of the microstructure of (a) 26 wt% HIWPG and (b) 17 wt% HIWPG.

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(a)

40 Force (N)

be broken clusters can disengage from the surface and interior of the gel assembly. The disengaged species can leave the interior of the gel body and then leave the gelsolvent interface as proposed in previous works (Mercad-Prieto and Chen, 2006; Mercad-Prieto et al., 2006a,b; Mercad-Prieto et al., 2008). 3.3. Inuence of protein concentration on whey protein solution fouling The results in Fig. 9 show: (a) the heat transfer coefcient prole during the fouling process; and (b) the temperature difference (DT) between the heat exchange surface (average) and the bulk solution during the fouling process of the 4 wt% whey protein concentrate solution (as an example). The decreasing heat transfer coefcient is an indication of the fouling layer formation on the heat transfer surface. As the fouling process proceeds the amount of deposit formed on the heat exchange surface also increases, leading the heat transfer coefcient to drop. Fig. 10 shows an example of fouled and cleaned heater rod, and it can be seen that higher protein concentration resulted in signicantly more fouling. The heat transfer coefcient plots however, seem not very different especially towards the end of each experiment (Fig. 9a). The fouling behaviour of deposits formed from 4 to 6 wt% solutions seems even more similar to each other. As it can be observed from the description of the results above, more highly concentrated (46 wt%) whey protein solutions fouled more quickly than the less concentrated (2 wt%) whey protein solution. The possible explanation for this is that increasing the whey protein concentration of the solution results in an increase of the number of b-lactoglobulin molecules in the solution and increasing the driving force of mass transfer of the fouling species towards the wall. Jun and Puri (2005) provided a more detailed summary of the factors inuence fouling. It is well known that heating above 65 C, these b-lactoglobulin molecules undergo denaturation. The denaturation of b-lactoglobulin is considered by Grijspeerdt et al. (2004) to be signicant in most dairy fouling. The denaturation reaction of b-lactoglobulin consists of a number of steps in which the monomer to dimer dissociation is the rst essential process. This dissociation occurs at temperatures much lower than those at which modications to the tertiary structure are observed (Cairoli et al., 1994; Iametti et al., 1996). This is followed by the rearrangement of the native b-lactoglobulin conformation to a state in which the free thiol is exposed and initiates sulfhydryl/disulphide (SH/SS) interchange reactions, leading to irreversible aggregation/polymerization (De Wit, 1990). The irreversible aggregation/polymerisation may happen at the metal surface to form fouling that is not soluble in worm water. The rate for the aggregation is expected to be strongly inuenced by the protein concentration. At high b-lactoglobulin concentrations, the rate for the aggregation is observed to increase due to the more frequent interactions between protein intermediate species (Roefs and de Kruif, 1994; Hoffmann and van Mil, 1997). Indeed, the kinetics of whey protein, and especially b-lactoglobulin, thermal denaturation has been extensively studied (Lyster, 1970; Sawyer et al., 1971; Hillier and Lyster, 1979; Harwalkar, 1986; Manji and Kakuda, 1987; Dannenberg and Kessler, 1988; Roefs and de Kruif, 1994; Anema and McKenna, 1996; Galani and Apenten, 1997; Chen et al., 1998; Verheul et al., 1998). According to Arnebrant et al. (1987) partly denatured proteins are more surface active than native proteins, so it would be expected that a fouling layer forms very rapidly with increased native protein concentration. Although there is an established link between protein denaturation and fouling, the relative impact of the denatured and aggregated proteins on fouling is not clear (Bansal and Chen, 2006).

30

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(b)

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15 Time (s)

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Fig. 7. Texture analysis of (a) 26 wt% HIWPG and (b) 17 wt% HIWPG.

centration is harder and more rigid than HIWPG with low protein concentration. 3.2. Inuence of protein concentration on HIWPG dissolution The dissolution experiments (Fig. 8) showed that HIWPG with high protein content HIWPG had the lowest dissolution rate (0.12 g m2 s1). HIWPG with high protein concentration have shown to contain large aggregates size (Fig. 6a), these aggregates are cross-linked via disulphide bonds and as a result, hard (Fig. 7) and large clusters are formed (Fig. 6a). In the dissolution process of HIWPG, these clusters are expected to be released and disengaged very slowly from the HIWPG matrix hence lowering the dissolution rate. In the dissolution studies of polymers (Devotta et al., 1995; Narasimhan and Peppas, 1996), it was predicted that the large clusters or the large chains of molecules are expected to disengage very slowly from the polymer matrix into the solvent. In the same study, it was proposed that the rate at which these large chains of molecules disengage themselves from the gelliquid interface controls the dissolution rate in large polymeric systems. However, for whey protein gels, it is likely that due to the cluster chain size varies in a wider range as a result of the mixture, smaller and easier to

0.4 0.35

Dissolution Rate (g m s )

-1 -2

0.3 0.25 0.2 0.15 0.1 0.05

14

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18

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Whey Protein Concentration (wt %)

Fig. 8. Dissolution rates of heat induced whey protein gels with different protein concentration in (0.5 wt%) NaOH at 60 C.

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700

Heat Transfer Coefficient(W.m .K )

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600 500 400 300 200 100 60 6 wt % WPC 4 wt % WPC 2 wt % WPC

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T (Heater surface and bulk solution) for the 4 wt % run

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Time (sec)
Fig. 9. (a) Fouling behaviour of whey protein concentrates (WPC) solution with various protein concentrations and (b) heater surface and bulk solution temperature difference (DT) during the fouling of 4 wt% WPC.

Fig. 10. (a) Fouled rod heater with deposit layer from (6 wt%) WPC solution before and (b) after cleaning.

3.4. The inuence of protein concentration during fouling on the subsequent cleaning The results in Fig. 11 show: (a) the heat transfer coefcient prole during the cleaning process; and (b) the temperature difference (DT) between the heat exchange surface (average) and the bulk solution during the cleaning process of the fouling layer from 4 wt% whey protein concentrate solution (as an example). The heat transfer coefcient recovery time indicates to the cleaning time of the fouling layer from the heat transfer surface.

The slope of the cleaning curve in Fig. 11a shows the speed of the recovery of the heat transfer coefcient, which is an increasing parameter. The initial slopes were not so different, which indicate a similar nature of the deposits that were formed at the nal stages of fouling where the temperature at the fouling layer surface would be partly close to the bulk solution temperature. The nal slopes (a1 > a2 > a3) in Fig. 11a were distinctly different, which indicate that the higher the protein concentration of the fouled solution the harder is to remove the fouling formed at the beginning of the fouling process. These slopes would be a good indicator

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(a)
Heat Transfer Coefficient(W.m .K )
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T ( C)

T (Heater surface and bulk solution) for cleaning 4 wt % WPC fouling 5

(b)
0 0 500 1000 1500 Time (sec) 2000 2500 3000

Fig. 11. (a) Cleaning behaviour of fouling deposits from whey protein concentrates (WPC) solution with various protein concentrations. a1, a2 & a3 show the signicant slopes towards the nish of the cleaning runs. (b) Heater surface and bulk solution temperature difference (DT) during the cleaning of 4 wt% WPC fouling.

of the effect of the deposit aging process for any single run, where physical and chemical changes might have occurred at the metal surface temperature. Though the nal heat transfer coefcient in the fouling stage seems not so dissimilar, the time taken to clean was drastically different, with high protein concentration fouling taking much longer to clean. This implies that the nature of the fouling that was formed under higher whey protein concentration is quite different. Considering the fouling resistances among the three concentration levels similar, it means that the additional resistance d/Rfouling (where, Rfouling = the thermal conductivity of the fouling layer and; d = the thickness of the fouling layer) would be similar. Considering that the fouling is mainly consisted of proteins and water, then Rprotein  0.2 W m2 K1 and Rwater  0.6 W m2 K1 (Rahman, 1995), more protein in the layer leads to smaller thermal conductivity of the layer. Visualization of the fouled layers showed that the fouling layers formed at higher protein concentration appear denser which may suggest the fouling layer has more proteins. The much longer cleaning time indicates the fouling is stronger (most likely because of the higher protein concentration in the fouling layer hence lower thermal conductivity hence greater thermal resistance) which seems to be mirrored by the gel strength tests and the gel dissolution experiments.

Acknowledgement The authors are grateful to the nancial support provided by Dairy Australia, Melbourne, Australia. References
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