Journal of Food Engineering 168 (2016) 154159

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Journal of Food Engineering

journal homepage: www.elsevier.com/locate/jfoodeng

Fouling control in ultraltration of bovine serum albumin and milk by

the use of permanent magnetic eld
Guilherme Zin, Frederico Marques Penha, Katia Rezzadori, Fabiana Lusa Silva, Karina Guizoni,
Jos Carlos Cunha Petrus, Jos Vladimir Oliveira, Marco Di Luccio
Department of Chemical and Food Engineering, Federal University of Santa Catarina, Caixa Postal 476, 88040-900 Florianpolis, SC, Brazil

a r t i c l e i n f o a b s t r a c t

Article history: Membrane separation processes are widely employed for protein concentration in the food industry. The
Received 14 May 2015 major drawback is permeability reduction caused by concentration polarization and fouling. The present
Received in revised form 27 July 2015 work evaluated the inuence of a permanent magnetic eld applied to the ultraltration process (UF) of
Accepted 27 July 2015
protein solutions, as an alternative to improve the permeation performance and the permeability recov-
Available online 29 July 2015
ery. Permeation tests of bovine serum albumin (BSA) and milk as the feed protein solutions through a
50 kDa hydrophilic polyethersulfone (PES) membrane were carried out in a tangential ow module.
Keywords:
The feed pH was varied (4.0, 6.5 and 8.0) and ionic strength was modied by sodium chloride (NaCl).
Ultraltration
Concentration polarization
Permanent magnets were placed so as to obtain a maximum 0.7 T magnetic eld perpendicular to the
Fouling membrane surface. The magnetic induction effect (MI) on the feed solutions was also studied by
Magnetic eld submitting the feed to the magnetic eld for 2 h before permeation run. The presence of magnetic eld
Protein and the MI effect of the solution were effective in increasing both the permeate ux and the recovery of
hydraulic permeability. The magnetic eld application in the UF of protein solutions has proven to be an
attractive alternative for improving process performance.
2015 Elsevier Ltd. All rights reserved.

1. Introduction throughput of products and while maintaining product purity

The separation and purication of bioproducts such as proteins,
protein hydrolysates, polysaccharides, vitamins and amino acids
are important steps in the food industry due to the large number
of applications. Processes as precipitation, crystallization and
centrifugation may not result in a good selectivity, while more
selective methods like electrophoresis and chromatography
separation are often costly (Saxena et al., 2009).
Membrane separation processes (MSP) have found many appli-
cations in food industry, particularly in the concentration, recovery
and fractionation of proteins and protein hydrolysates (Sotoft et al.,
2015). MSP have numerous advantages over other methods such as
cost minimization, operational exibility and scaling up, high
Abbreviations: UF, ultraltration; BSA, bovine serum albumin; PES, polyether-
sulfone; MI, magnetic induction; MSP, membrane separation processes; WO/MF,
without the presence of the magnetic eld; W/MF, with the presence of the
magnetic eld; MMCO, molar mass cut off; WO/NaCl, without sodium chloride;
W/NaCl, with sodium chloride; IEP, isoelectric point; PC, physical cleaning; CC,
chemical cleaning.
Corresponding author.
E-mail address: di.luccio@ufsc.br (M. Di Luccio).
under ambient conditions, and a great cost benet regarding
energy consumption (Lujn-Facundo et al., 2015).
However, a major drawback of this technology is the ux reduc-
tion during permeation due to concentration polarization and
membrane fouling, which may occur by solute deposition on mem-
branes surface, forming a gel layer or by solute adsorption inside
the pore structure of the membrane, often irreversible (Saxena
et al., 2009).
Some chemical and physical strategies can be used to reduce
these undesirable effects. Despite being an effective cleaning
method, the use of chemicals in membrane processes may damage
both the membrane and the nal product (Zhang and Ma, 1999).
Other forms of chemical approach to minimize fouling involve
chemical modication of the membrane surface, e.g. nanoparticle
coating (Moghimifar et al., 2014; Razmjou et al., 2011), surface
modication by copolymerization (Li et al., 2014; Yu et al., 2011)
and plasma polymerization (Zou et al., 2011). The use of physical
processes toward fouling reduction are the most attractive because
they do not alter the molecular structures involved in the process,
and consist in clean, non-intrusive technology, since no chemical
agents are used. The physical strategies include the use of

http://dx.doi.org/10.1016/j.jfoodeng.2015.07.033
0260-8774/ 2015 Elsevier Ltd. All rights reserved.
 G. Zin et al. / Journal of Food Engineering 168 (2016) 154159
turbulence generating devices, sonication, centrifuge and use of
electric and magnetic elds (Vardanega et al., 2013).
The use of magnetic eld has been proposed for minimization of
scaling in heat exchangers caused by scaling (Lipus et al., 2011;
Shahryari and Pakshir, 2008). Then, some studies focused on its
use to control of scaling in nanoltration and reverse osmosis
membranes (Al-Qahtani, 1996; Li et al., 2007; Long et al., 2005;
Vedavyasan, 2001). Although not widespread yet, the use of
magnetic eld in some cases attracts attention due to some
advantages such as low cost and low power consumption, simple
operation and low environmental impact (Gabrielli et al., 2001;
Vedavyasan, 2001; Wang et al., 1997). Studies show that the mag-
netic eld inuences the layer of hydrated ions in the solution and
causes changes in the hydrating water structure around the ions,
changing the water conductivity (Holysz et al., 2007; Szczes
et al., 2011). The magnetic eld weakens the hydrogen bonds
due to the competition between the different hydrogen bond net-
works (intra- and intermolecular) forming smaller clusters with
greater bond strength (Toledo et al., 2008). It is also reported that
the magnetic eld causes the decrease of the surface tension and
viscosity of water, elevates the wettability of polymeric surfaces
(observed by contact angle); and increases the refractive index
and dielectric constant of water. The authors suggest that the
externally applied magnetic elds cause displacements and polar-
ization of molecules and atoms, and result in changes of dipole
moment in the transition and vibrational states of molecules
(Amiri and Dadkhah, 2006; Pang and Deng, 2008). In saline solu-
tions, the magnetic eld changes the way how the salt nucleation
and growth of salt crystals occurs. Several studies reported that the
effects of magnetic eld are mainly in the acceleration and in the
increase of precipitate amount (Alimi et al., 2009). For instance,
the magnetic eld application in calcium carbonate solutions
increases the salt formation in the aragonite form, less stable and
more soluble in water in comparison with calcite form, decreasing
the deposition (scaling) in tube and heat exchangers (Tai et al.,
2014; Chang and Tai, 2010). Some authors report that the
application of the magnetic eld promoted an increase in potas-
sium chloride ions transport through a cellulose membrane
(Ohata et al., 2004); increased ux and reduced the calcium car-
bonate deposition on nanoltration membranes (Li et al., 2007;
Long et al., 2005) and promoted a greater recovery of permeate ini-
tial ux after physical and chemical cleaning procedures in new
and used ultraltration membranes (Vardanega et al., 2013). A
patented device used for brackish water desalination is also
reported (Ballester and Garrido, 2012).
In this context, this work assessed the application of static per-
manent magnetic eld on the ultraltration of protein solutions in
a tangential module as a possible alternative to improve process
performance, by reducing membrane fouling and consequent
increase in permeate ux. So far, no further studies on the effect
of magnetic elds on protein UF can be found elsewhere, apart
from the preliminary study of the group (Vardanega et al., 2013).
2. Materials and methods
2.1. Experimental apparatus
The UF unit was operated in tangential ow and consists of a
feed tank, one positive displacement pump (Micropump, cat.
75211-15, Cole-Parmer, USA), a pressure gauge (Fiedler Ltda,
Brazil), a backpressure valve (SS4BK, Swagelok, USA) and a ow
meter (Blaster Controles Ltda, Brazil). The UF module had dimen-
sions of 100  65  10 mm, made of polyoxymethylene, with
effective ltration area of 0.0029 m2, onto where the magnets are
positioned. The solution leaving the module is divided in two
155
streams, the permeate and the retentate. Fig. 1 shows a schematic
diagram of experimental apparatus used in this study, and a side
view of tangential ultraltration module in the presence of
magnets.
2.1.1. Magnetic eld
The magnetic eld was generated by the presence of two neody
miumironboron (Nd2Fe14B) permanent magnets with dimen-
sions of 50  50  25 mm, positioned perpendicularly to the UF
module as shown in Fig. 1(b). The magnetic eld intensity was
measured with a magnetic eld transducer (model TMAG-1T,
Globalmag Ltda, Brazil). The ux density at the central point of
the module was 0.7 T.
2.2. Membranes
A poly(ethersulfone) membrane (Microdyn-Nadir GmbH,
Germany) with molar mass cut off (MMCO) of 50 kDa was used
in all experiments. The membranes were previously treated with
99% ethanol (Vetec Ltda, Brazil) for 30 min and then rinsed thor-
oughly with ultrapure water. A new sample of membrane was used
for each set of experimental runs.
2.3. Assay and reagent solutions
The feed solution consisted of bovine serum albumin (BSA,
SigmaAldrich #A2153, average molecular mass 66 kDa and iso-
electric point (IEP) 4.7) at a concentration of 2.5 g L1.
Homogenized standardized pasteurized milk was also tested for
validation purposes. The pH chosen to BSA solutions were 8.0
(higher than IEP) and 4.0 (lower than IEP) and pH 6.5 for milk
(pH commonly found in natura). Sodium chloride (NaCl) was added
to the feed solutions at a concentration of 0.5 M for testing the pro-
cess performance in the presence of an inorganic salt.
The cleaning protocol consisted of sequential rinses with solu-
tions of hydrochloric acid (HCl, at pH 4.0), sodium hydroxide
(NaOH, at pH 10) and phosphate buffer (pH 7.0). Ultrapure water
was used for preparing all solutions and reagents.
2.4. Experimental procedure
The experimental procedure was carried out in three different
ways. The standard procedure (control) was performed without
the presence of the magnet (WO/MF). The second set of assays
was carried out in the presence of magnet during ultraltration
of the protein solution (W/MF). Finally, magnetic induction effect
(MI) assays were performed. The latter consisted in the protein
solution circulation through the magnetic eld for 2 h before the
permeation process. All assays were carried out in duplicates at
ow rate 0.3 L min1 (0.055 m s1), while experimental errors
were lower than 5%. Control runs were carried out to account for
changes in the protein solution due to circulation of protein solu-
tion through the system. The membrane hydraulic permeability
was determined after compaction and after physical and chemical
cleaning procedures, at a ow rate of 0.3 L min1, varying the pres-
sure from 2.0 to 0.5 bar at 25 C.
UF of protein solutions were carried out for 120 min at constant
pressure of 2 bar, feed ow rate of 0.3 L min1 and 25 C, with pH
ranging according to the solution used. The assays were performed
in batch mode, with full recycle of retentate and permeate, thus
keeping the feed concentration constant. The return of the reten-
tate and permeate streams caused a constant mixing in the feed
tank. No precipitation of solids was observed in any of the experi-
mental assays. Permeate ux was determined at each 15 min for
BSA solutions and at each 20 min for milk solutions.
156 G. Zin et al. / Journal of Food Engineering 168 (2016) 154159

Fig. 1. (a) Schematic diagram of experimental apparatus, (b) side view of tangential ultraltration module in the presence of magnets generating a magnetic eld.

As a nal step, the cleaning procedure was performed by circu-
lating a NaOH solution at pH 10.0, followed by a HCl solution at pH
4.0, with a subsequent recirculation of the sodium phosphate buf-
fer at pH 7.0 for 30 min. Before changing the cleaning solution, the
system was rinsed with 2 L of ultrapure water.
2.5. Permeate ux
The permeate ux (J) was calculated by the following equation:
Vp
J 1
t  Am
where Vp is the permeate volume obtained at the time interval t and
Am denotes the effective membrane area.
3. Results and discussion
3.1. Inuence of salt, pH and magnetic eld on the permeate ux of
bovine serum albumin solution and milk
The permeate ux of BSA solution (2.5 g L1) and milk were
evaluated based on the permeate ux of BSA and milk normalized
by the initial permeate ux of ultrapure water in all tested condi-
tions (WO/MF, W/MF and MI). Normalized permeate ux approach
was used to deduct the variation in the initial ux of ultrapure
water between different at sheet membrane samples.
Permeate uxes for all the runs are presented in Figs. 2 and 3.
Fig. 2 shows the results for BSA solutions at pH 4.0 and 8.0 (a) with-
out NaCl and (b) with 0.5 M NaCl, while Fig. 3 shows the milk per-
meate ux at pH 6.5 with and without addition of NaCl.

(a) 0.4
2.6. Hydraulic permeability recovery
0.35
Normalized Flux (J/Ji)

The recovery of the initial hydraulic permeability after physical 0.3

cleaning (Recp) was obtained by: 0.25
8.0; MI
8.0; W/MF
0.2
Permp 8.0; WO/MF
Recp % 2
Permi 0.15 4.0; MI
0.1 4.0; W/MF
where Permp is the permeability after physical cleaning procedure 4.0; WO/MF
0.05
and Permi is the ultrapure water permeability of the new
membrane. 0
0 20 40 60 80 100 120
The values of the hydraulic permeability recovery after chemi-
cal cleaning (Recc) were obtained by: Time (min)

(b) 0.4
Permc
Recc % 3 0.35
Permi
Normalized Flux (J/Ji)

0.3

where Permc is the permeability after chemical cleaning procedure. 0.25

8.0; MI
8.0; W/MF
0.2
8.0; WO/MF
2.7. Zeta potential 0.15 4.0; MI
0.1 4.0; W/MF
The zeta potential analysis reects the electric potential of par-
4.0; WO/MF
ticles surface, solids and liquids. The zeta potential of BSA protein 0.05
was determined by laser doppler anemometry associated with the 0
microelectrophoresis using the Zeta sizer Nano ZS3600 (Malvern 0 20 40 60 80 100 120
Instruments Ltd., UK). The Zeta sizer was also used for monitoring Time (min)
the size of protein agglomerates during system operation. The zeta Fig. 2. Normalized permeate ux in UF of BSA solutions at pH 4.0 and 8.0, without
potential of the membrane was determined by electrokinetic ana- (WO/MF) and with (W/MF) magnetic eld and after the magnetic induction (MI) (a)
lyzer SurPass (Anton Paar GmbH, Austria). without and (b) with 0.5 M NaCl.
 G. Zin et al. / Journal of Food Engineering 168 (2016) 154159
0.016
0.014
0.012
Normalized Flux (J/Ji)
0.01
0.008
0.006
0.004
0.002
0 membrane
0 20 40 60 80 100
Time (min)
Fig. 3. Normalized permeate ux during UF of milk ultraltration at pH 6.5,
without (WO/MF) and with (W/MF) magnetic eld and after magnetic induction
(MI), with (W/NaCl) and without (WO/NaCl) 0.5 M NaCl.
Initially, the ux decreases rapidly due to the effects of
concentration polarization, progressing to a slower decrease as a
consequence of fouling. This is the usual behavior in UF processes.
Literature reports that for UF experiments with random-coil food
proteins solutions and calcium deposition in nanoltration mem-
branes, the same ux behavior is observed (Li et al., 2007; Lim
and Mohammad, 2010).
Fig. 2(b) shows a lower permeate ux compared to the Fig. 2(a),
due to the presence of NaCl in the BSA solution, which caused a more
severe membrane fouling. The salt leads to an increase in the ionic
strength of the solution, which decreases the electrostatic repulsion
between protein chains. This results in an accelerated accumulation
of proteins on the membrane surface, thus contributing to the for-
mation of a thicker polarization layer (Lim and Mohammad, 2010).
The different pH values inuenced the permeate ux of solutions
with and without NaCl. The farther from the BSA IEP, the higher are
the permeate uxes obtained. Similar behavior has been found in
tests with BSA solutions, where lower permeate uxes were found
in pHs near the IEP of the protein (Vardanega et al., 2013).
At IEP, protein molecules have no positive or negative net
charge, thereby assuming its most compact form. Consequently,
near to IEP, the electrostatic repulsion between the protein and
the membrane surface is reduced, conrmed by zeta potential
results shown in Table 2, and hence the protein can easily accumu-
late on the membrane surface, forming a dense and compact layer,
which increases the resistance to permeate ux (Lim and
Mohammad, 2010; Wang and Tang, 2011). Although the proximity
to IEP can culminate with protein precipitation, no precipitate was
detected in the feed tank after each experimental run. Dynamic
Light Scattering measurements (Zetasizer) showed that the size
of protein aggregates did not signicantly change (p < 0.05) during
the runs, and was considered evidence that the particles were not
disintegrated during the process.
Fig. 3 shows that in the permeate ux of milk UF is lower than
BSAs and there was little variation over process time. This fact can
be related to milks higher solid content (proteins, fats, vitamins
and salts), therefore inducing greater polarization and fouling
effects (Vincent Vela et al., 2007).
It can be seen from Figs. 2 and 3 that the magnetic eld pres-
ence during the UF and the magnetic induction of the solution
resulted in an increase of the permeate ux of BSA solutions and
milk, especially when the eld was applied to the feed solution
before permeation run (magnetic induction). The magnetic induc-
tion was more effective than using the eld during permeation
possibly due to the inuence of the eld on protein interactions.
When the eld is applied in permeation run, the protein solution
157
Table 1
Percentage increase of permeate ux after magnetic induction compared to exper-
iments without magnetic eld in BSA solution at pH 4.0 and 8.0 and milk at pH 6.5,
with and without NaCl addition.
MI; W/NaCl
Permeate ux increase (%)
W/MF; W/NaCl pH 4.0 pH 8.0 Milk pH 4.0/NaCl pH 8.0/NaCl Milk/NaCl
WO/MF; W/NaCl 88 90 45 31 75 47
MI; WO/NaCl
W/MF; WO/NaCl
WO/MF; WO/NaCl Table 2
Zeta potentials of membrane and BSA solutions at different pH.
pH New BSA solution WO BSA solution after
exposure to MF exposure to MF
120
4.0 9.22 0.46 8.54 0.17 11.32 0.31
8.0 13.76 0.41 40.85 0.83 43.45 0.86
is only gradually exposed to the action of the eld. On the other
hand, when the solution is treated before permeation, the process
already starts with a more stable protein solution, increasing pro-
cess performance. The noticeable changes in zeta potential of the
protein solution after exposure to magnetic eld also contribute
to support the hypothesis that BSA is affected by the magnetic
eld. The circulation of the protein solution through the magnetic
eld may also have helped to intensify this effect, as suggested by
Kobe et al. (2002), who investigated the crystallization of CaCO3 in
applied magnetic elds.
Table 1 shows the percentage increase of the permeate ux in
magnetic induction experiments in comparison to permeate ux
without magnetic eld, for the BSA solutions and milk, after
120 min of permeation.
The experiments showed an increase of ux for all runs in
which the magnetic induction was applied to the solution. The ux
was increased, in the experiments without NaCl, by 88% and 90%
for pH 4.0 and 8.0, respectively, in comparison to permeate ux
without magnetic eld, as shown in Table 1.
A previous study on membrane fouling caused by protein sug-
gests that the protein intermolecular interactions are modied by
the action of magnetic eld, decreasing protein aggregation on
the membrane surface (Vardanega et al., 2013). To check such
hypothesis, the zeta potential of BSA solutions and of the new
and used membranes were measured and are presented in Table 2.
At pH 4.0, the protein net charge is near zero, since it is near its
isoelectric point (4.7) and solution is less stable. The zeta potential
of membrane surface was also carried out at pH 4.0. The zeta
potential of the reference BSA solution at pH 4.0 without salt
was 8.54 mV. Membrane zeta potential at pH 4.0 was 9.22 mV.
The opposite charges explain the higher fouling that was observed
at this pH, as it can be seen in Fig. 2.
After 2 h of magnetic induction of the BSA solution, the zeta
potential increased to 11.32 mV. This behavior showed that the
magnetic eld can change the double layer conformation, possibly
due to changes in protein net charge, increasing colloidal stability
of the solution, due to molecular repulsion, and thus improving the
ux during the permeation. Zeta potential of membrane fouled by
BSA solution increased to 1.65 mV after the permeation run. This
fact can contribute to reduce further fouling of the membrane by
the BSA molecules. Wang and Tang (2011) also demonstrated the
important role of electrostatic interaction during BSA fouling, with
the square of zeta potential (f2) of the foulant being potentially a
good indicator for predicting the long term fouling behavior.
They showed that the higher the zeta potential, the lower
membrane fouling.
Preliminary studies involving UF of protein solutions also
provided good results. For instance, Vardanega et al. (2013) with
158 G. Zin et al. / Journal of Food Engineering 168 (2016) 154159

(a) 100
(b) 100
81

Permeability rec. (%)

Permeability rec. (%)

80 80

60 60
47 47
39 42 42
40 40 33
28 29
18 16
20 20 12

0 0
WO/MF W/MF MI WO/MF W/MF MI
PC CC PC CC

(c) 100 (d) 100

Permeability rec. (%)

Permeability rec. (%)

80 75 80
66 69
63 64
58 57
60 53 60

38
40
30 40 32 35

20 20

0 0
WO/MF W/MF MI WO/MF W/MF MI
PC CC PC CC

Fig. 4. Percentage recovery of hydraulic permeability of the UF membrane after the BSA solutions permeation at pH 4.0 (a) without and (b) with NaCl addition and pH 8.0, (c)
without and (d) with NaCl addition after physical (PC) and chemical (CC) cleaning, to all performed assays (WO/MF, W/MF and MI).

(a) 100
(b) 100
82
Permeability rec. (%)

Permeability rec. (%)

80 80

58 57
60 60
45 44 47
40 40

18 20
20 14 12 20 12 13

0 0
WO/MF W/MF MI WO/MF W/MF MI
PC CC PC CC

Fig. 5. Percentage recovery of hydraulic permeability of the UF membrane after milk permeation at pH 6.5, (a) without and (b) with NaCl addition, after physical (PC) and
chemical (CC) cleaning, to all performed assays (WO/MF, W/MF and MI).

a weaker magnetic eld (0.4 T) and different BSA solution concen-
trations, obtained a small percentage increase of 27% and 12% on
permeate ux of solutions with pH 3.0 and 5.0, respectively. Li
et al. (2007) employed the ultrasonic time-domain reectometry
technique to detect the precipitation and growth of CaCO3 scale
deposition on the surface of NF membranes, in the presence and
absence of 0.02 T magnetic eld intensity. The scaling experiments
were carried out with 1.8 and 3 mmol L1 CaCO3 solution
non-magnetically and magnetically pretreated by 2 h. The results
showed a percentage increase of 9% and 20% in the normalized ux
after 420 min when compared with the solutions non-magnetically
and magnetically treated, for 1.8 and 3 mmol L1 CaCO3 solutions,
respectively.
In the present study, we could reach up to 90% and 47% of
permeate ux improvement after magnetic induction of BSA
solution and milk, respectively, showing that the application of
magnetic elds clearly improves the performance of ultraltration.
3.2. Inuence of salt, pH and magnetic eld application on the recovery
of membrane hydraulic permeability after bovine serum albumin and
milk ultraltration
The recoveries of membrane hydraulic permeability were
assessed after the ltration of BSA solutions (2.5 g L1) and milk.
The permeability recovery quantication was determined by com-
parison of the initial membrane hydraulic permeability with the
permeability after physical and chemical cleaning. The operating
parameters used were the same previously mentioned. Figs. 4
and 5 show the recovery of the hydraulic permeability of mem-
branes in the three different sets of assays.
For all the analysis carried out with BSA, it is evident the
increase in hydraulic permeability recovery caused by the mag-
netic eld on the process after physical and chemical cleaning pro-
cedures, especially when the solution was subjected to the
magnetic induction before permeation. These results can be con-
sidered very promising, since the gains in ux recovery would
allow the use of smaller amounts of cleaning solution and a reduc-
tion in manufacturing time.
As in the item 3.1, the application of magnetic eld to the feed
solution prior to permeation (MI) was more effective when com-
pared to the application of the eld during UF run. In most runs
with the BSA solutions, a higher percentage of hydraulic perme-
ability recovery occurred in physical cleaning, when compared
with chemical cleaning. It can be inferred that the ux decrease
in this process is caused mainly by the concentration polarization.
The difference between the solution pH and the protein IEP
causes a series of changes in the process behavior. A greater
hydraulic permeability recovery can be noticed at pH 8.0 in both
 G. Zin et al. / Journal of Food Engineering 168 (2016) 154159
experiments (with and without NaCl), when compared with the
recovery obtained at pH 4.0, due to higher electrostatic repulsion
between the protein and membrane surface. At pH 8.0 a lower inci-
dence of irreversible fouling in comparison with the results
obtained at pH 4.0 is also observed. This can be veried by the
small difference in the permeability recovery between physical
and chemical cleaning.
The effect of magnetic eld on permeability recovery after milk
UF (Fig. 5) was in general less effective than the performance of
magnetic eld in BSA ultraltration, except in the cases of mag-
netic induction of milk added with salt, which showed an increase
in the recovery of 74% in comparison with the solution that was
not treated.
Unlike the assays with BSA, it can be noted that irreversible
fouling is the main cause of permeability reduction in milk UF,
since the chemical cleaning procedure is the major responsible
for hydraulic permeability recovery. This difference between the
behavior of ux recovery after BSA and milk permeation runs
demonstrate how complex are the phenomena involved in fouling
control, probably due to the diversity of proteins found in milk and
other components such as fat.
Finally, the use of a permanent magnetic eld in protein UF
proved to be a very promising technique for fouling control.
Advantages rely on its clean technology character, producing no
waste, besides the relatively low cost for installation in processes
already established (Vedavyasan, 2001). Furthermore, it can poten-
tially minimize process outages for membrane cleaning, besides
using smaller amounts of chemicals for the same purpose, thus
increasing membranes lifespan.
4. Conclusions
This work evaluated the effect of magnetic eld application for
fouling control in BSA and milk ultraltration. Results showed that
the presence of the magnetic eld and the magnetic induction
alters the zeta potential of the BSA solutions and have proven to
be effective in increasing the permeate ux and the hydraulic per-
meability recovery of BSA solutions with and without the presence
of NaCl at pH 4.0 and 8.0, especially in the cases when the eld was
applied to the solution prior to permeation (magnetic induction
effect). In the assays of milk concentration, a high decline of the
permeate ux was observed. The addition of NaCl to the milk
improved the effect of the magnetic eld in the permeate ux
and in permeability recovery. It is noteworthy that these effects
were greater for the assays with magnetic induction. Hence, the
application of magnetic eld in membrane processes is an attrac-
tive alternative to other methods of fouling reduction and ux
enhancement, leading to more economical and efcient processes.
Acknowledgements
The authors thank CNPq Brazil (552185/2011-6;
477497/2013-6; 304137/2012-0) and CAPES Brazil for the nan-
cial support and scholarships. Control Process Laboratory
(LCP/UFSC) and Multi-user Analytical Laboratory (CA-EQA/UFSC)
are acknowledged for zeta potential analyses.
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