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protein concentrates
Autors: Banach & Lamsal (2014) ABSTRACT
Extruded or toasted milk protein concentrate with approximately 80 grams protein per 100 grams were
incorporated into model high-protein nutrition bars formulated at 30 grams protein per 100 grams. The model
highprotein nutrition bars also contained other constituents, including glycerol, palm kernel stearin, sugar
alcohol syrup, and high-fructose corn syrup, to mimic commercial high-protein nutrition bars. The bars were
stored at room temperature (22 Celsius degrees approximately), 32 Celsius degrees, or 42 Celsius degrees for
up to 42 days. Texture, water activity, and color were measured periodically over the storage period. High-
protein nutrition bars formulated with unmodified milk protein concentrate served as the control and
maintained similar texture to those highprotein bars formulated with toasted milk protein concentrate. High-
protein nutrition bars prepared with milk protein concentrate extruded at 65 Celsius degrees were significantly
softer than the control. Significant differences in hardness and fracturability between high-protein nutrition
bars formulated with milk protein concentrate extruded at 120 Celsius degrees and the control were
intermittent over the storage period. Water activity of the high-protein nutrition bars increased slightly during
storage, but remained less than 0.65, which assured shelf stability. Surface color change was minimal at 22°C
storage, but increased at 32 and 42 Celsius degrees.
1. Introduction
Milk protein concentrates (M.P.Cs) are multifunctional ingredients used in processed cheese to improve
overall yield, specialty nutrition products to fortify with protein, and dairy foods such as yogurt to improve
texture (Mistry, 2002; Mistry & Hassan, 1992). M.P.Cs are produced from skim milk via membrane filtration.
diafiltration, evaporation, and spray drying to a food powder that maintains the proportion of casein (80 grams
per 100 grams protein) to whey (20 grams per 100 grams protein) (Singh, 2007). The total protein content in
M.P.C. is dependent on processing and ranges from 40 gram (this is, M.P.C.40) to 85 grams (this is, M.P.C.85)
protein per 100 grams of dry product. In food applications, M.P.Cs provide heat and emulsion stability,
opacity, and flavor (Baldwin & Pearce, 2005).
High-protein nutrition (H.P.N.) bars, intermediate-moisture foods containing 20 grams to 50 grams protein
per 100 grams, are one application where M.P.Cs are underutilized (Baldwin & Pearce, 2005; Imtiaz,
KuhnSherlock, & Campbell, 2012). Instead, blends of whey proteins, caseinates, and soy proteins are used in
HPN bars, but the nutritional value and flavor of M.P.Cs. make them suitable for these applications too (Imtiaz
et al., 2012). Prices of whey protein, a co-product of cheese production, have risen with the development of
their functionalized forms that improve performance in protein fortified foods (Smithers, 2008). Whey and
soy protein are nutritionally comparable with each other, but the casein protein in M.P.C. is digested slowly,
allowing for greater nitrogen retention and muscle growth post exercise (Tang, Moore, Kujbida, Tarnopolsky,
& Phillips, 2009).
Despite its advantages, M.P.Cs perform poorlyin H.P.N. bars. The minimum shelf-life for commercial H.P.N.
bars is 6 months, but product stability for greater than 12 months is often desired and not possible when M.P.Cs
are included (Imtiaz et al., 2012; McMahon, Adams, & McManus, 2009). Model protein bars prepared at 20
grams M.P.C.80 per 100 grams bar hardened substantially after 50 days storage at room temperature, well
short of the desired 6 months (Loveday, Hindmarsh, Creamer, & Singh, 2009). H.P.N. bars formulated with
milk protein isolate (M.P.I.) had crumbly texture and lacked cohesion, another important, but rarely reported
aspect of H.P.N. bar quality (Imtiaz et al., 2012; Li, Szlachetka, Chen, Lin, & Ruan, 2008).
The exact mechanism of instability in M.P.C.-formulated H.P.N. bars has not been elucidated. However, it is
most likely due to moisture migration, limited free water, macronutrient phase separation, and internal
disulfide bond formation with subsequent protein aggregation that lead to quality deterioration in other H.P.N.
bars (Loveday et al., 2009; McMahon et al., 2009; Zhou, Liu, & Labuza, 2008a). Macronutrient phase
separation can occur with preferential exclusion of the solvent (for example, water) and co-solvent (for
example, sugar alcohol, sugar syrup) from the local protein domain (McMahon et al., 2009). Without
solvent/co-solvent protein interactions, water can migrate away from the protein to lower molecular weight
constituents allowing for local protein interactions via disulfide bond formations, subsequent aggregations,
and more complete network formations, which have all been previously linked to H.P.N. bar hardening
(Loveday et al., 2009; Loveday, Hindmarsh, Creamer, & Singh, 2010; Zhou, Liu, & Labuza, 2008b). However,
excessive interaction between the protein and some co-solvents such as propylene glycol can lead to rapid
aggregations and subsequent hardening (Liu, Zhou, Tran, & Labuza, 2009).
Two of Fonterra's (Auckland, New Zealand) protein bar specific M.P.Cs (this is, PowerProtein 4857 and
PowerProtein M 4861) and one W.P.C. (this is, PowerProtein 515) were evaluated instrumentally and
texturally by a trained sensory panel in model H.P.N. bars formulated at 30 grams protein per 100 grams
(Imtiaz et al., 2012). The bar specific W.P.C. imparted softening and improved cohesion without being
enzymatically hydrolyzed (Imtiaz et al., 2012). H.P.N. bars formulated entirely with PowerProtein M 4861
maintained firmness, but had increased crumbliness during storage (Imtiaz et al., 2012). H.P.N. bars
formulated with Power Protein 4857 hardened during storage, but had less influence on cohesiveness (Imtiaz
et al., 2012). No protein modification details were provided in the study, but it was shown that M.P.C.
functionalization prior to use in H.P.N. bars can improve its feasibility in these applications.
Earlier, we reported on physical modification of M.P.C.80 using extrusion and toasting and characteristics of
resulting ingredients (Banach, Clark, & Lamsal, 2013). The altered functionality of the modified M.P.C.80s,
notably reduced protein solubility, altered water-holding capacity, and incidence of preformed disulfide bonds,
was favorable for inclusion in H.P.N. bars. In this study, we report texture and related changes in model H.P.N.
bars formulated with M.P.C.80 processed at the same conditions.
Note:
Table 1 says: “Model high-protein nutrition (h.p.n.) bar formulations”.
End of note.
The modified or unmodified M.P.C.80 ingredient, glycerol, maltitol syrup, and water were combined with a
wire whip attachment on 'stir' for 60 seconds followed by 2 minutes mixing on speed 4 using a stand mixer
(model K.5.S.S., Kitchen Aid, St. Joseph, M.I.). Palm kernel stearin and H.F.C.S. were heated together until
fat liquefaction and were cooled to 55 Celsius degrees before being mixed into the protein/polyol mixture on
speed 4 for 2 min. All mixing times were discontinuous as the mixers were paused every 30 seconds to scrape
the side of the mixing bowl. Each model H.P.N. bar listed in Table 1 are identified by their protein source
(this is, M.P.C., E.65, E.120, T.75, and T.110) and were prepared twice; once from each M.P.C.80 ingredient
preparation.
H.P.N. bar dough was uniformly packed into cylindrical molds with 21 millimeters internal diameter and
lengths of 13 millimeters or 107 millimeters. H.P.N. bar dough in each mold was leveled with a spatula and
the mold was sealed at both ends with parafilm. Water activity sample cups were filled halfway with H.P.N.
bar dough, covered with a lid, and were sealed with parafilm. Samples were sealed into separate zipper-seal
plastic bags and were left at room temperature for 1 hour prior to being randomly assigned to 42 Celsius
degrees, 32 Celsius degrees, or room temperature (22 Celsius degrees) storage.
Note:
See equation 1 and 2
End of note.
First, stress-time data were normalized using the left-hand side of Equation (1). Normalized stress was plotted
against time and a linear regression line was fitted. Average slope from the linearized plot was “lowercase “k”
subscript 2” and the “y”-intercept of the regression line was “lowercase “k” subscript 1”, the inverse of which
corresponds to the initial decay rate of the stress ratio. The equilibrium stress (“sigma subscript “e””) or
internal stress in the sample at infinite time was calculated from Equations (2). The mean stress ratio (sigma
subscript 300 “s” divided by sigma subscript “e”) was determined by dividing the stress observed in the sample
at 300 seconds of compression by the calculated sigma subscript “e”.
The longer H.P.N. bar samples were used for a shear test adapted from McMahon et al. (2009). The cylindrical
H.P.N. bar was sheared along the circular cross-section at three different points with a 45 degrees chisel blade
(T.A.-42. Texture Technologies, Scarsdale, NY) at 1 millimeters per second to 85 percent of the original
sample height. The average maximum force during shear was reported as shear strength.
2.5. Color and water activity measurement of model high-protein nutrition bars
Color and water activity measurements were made on days 0, 1, 4, 13, 22, and 42, after equilibrating H.P.N.
bar samples at room temperature for at least 1 hour. Color values for the H.P.N. bar in each water activity
sample cup were acquired with a LabScan X.E. benchtop colorimeter (Hunter Laboratory Associates, I.n.c.,
Reston, V.A.) operating with D.65 northern daylight light and a 10 degree standard angle observer. Color
values were determined on three H.P.N. bar samples from each batch, storage temperature, and storage time
combination. Total color change (Delta Uppercase “E”) was calculated with Equation (3) for each H.P.N. bar
preparation with the reference color values (this is, lowercase “a”, “b” and uppercase “L” superscript asterisk
and lowercase zero) set to the values of that H.P.N. bar on day 0.
Note:
See equation 3.
End of note.
Water activity was measured after color measurement with a water activity analyzer (model Aqua Lab 4.T.E.
Duo, Decagon Devices Inc., Pullman, W.A.). Prior to measurement, the analyzer was standardized using 6
mol per kilogram sodium chloride and 13.41 mol per kilogram lithium chloride. Three separate water activity
measurements were made for each batch, storage temperature, and storage time combination. The “delta
uppercase “E”” and water activity values are reported as the average of duplicate HPN bar preparations.
Note:
Figure 1 says: “Water activity of model high-protein nutrition (H.P.N.) bars stored at (“A”) room temperature
(22 Celsius degrees approximately), (“B”) 32 Celsius degrees, and (“C”) 42 Celsius degrees. M.P.C. identifies
a model H.P.N. bar made with unmodified M.P.C.80, E.65 and E.120 identify model H.P.N. bars prepared
with M.P.C.80 extruded at die temperatures of 65 Celsius degrees and 120 Celsius degrees respectively: T75
and T110 identify model H.P.N. bars prepared with M.P.C.80 toasted 4 hours at 75 Celsius degrees and 110
Celsius degrees, respectively.
End of note.
All model H.P.N. bars had significantly increased water activity after 42 days storage at room temperature
except for those prepared with E.65, which only increased by 0.03 (lowercase “p” inferior to 0.05). At room
temperature, the water activity of H.P.N. bars formulated with unmodified M.P.C.80 increased by 0.07.
However, the water activity at 32 Celsius degrees was more stable for H.P.N. bars formulated with unmodified
M.P.C.80 than those formulated with E.65. Increased water activity may indicate movement of water
molecules from the intermediate phase, where they act as a plasticizer, to the bulk phase (Li et al., 2008).
Small magnitude increases in water activity in model H.P.N. bars in this study are consistent with other studies
that use accelerated storage conditions. Increased water activity has been reported to correspond with H.P.N.
bars that harden more quickly compared with those H.P.N. bars with stable water activity (Li et al., 2008;
McMahon et al., 2009). Lack of water molecules associated with the local protein domain allows neighboring
amino acids to form disulfide bonds that cause subsequent protein aggregation, one of the suggested
mechanisms of H.P.N. bar hardening when formulated with whey protein (Zhou et al., 2008, 2008b). Although
some increases in water activity within each batch at constant temperature over time were significant
(lowercase “p” inferior to 0.05), the relative increase was small and may have no influence on H.P.N. bar
hardening. Significant water activity differences between each H.P.N. bar batch at fixed storage temperature
and fixed storage time combination was limited.
Note:
Figure 2 says: “Model high-protein nutrition (H.P.N.) bar color after 1 day and 42 day storage at room
temperature (22 Celsius degrees approximately), 32 Celsius degrees, and 42 Celsius degrees. “Delta uppercase
“E”” values displayed on the figure are calculated with respect to color on the day of H.P.N. bar manufacture
(day 0). M.P.C. identifies a model H.P.N. bar made with unmodified M.P.C.80; E.65 and E.120 identify model
H.P.N. bars prepared with M.P.C.80 extruded at die temperatures of 65 Celsius degrees and 120 Celsius
degrees, respectively: T.75 and T.110 identify model H.P.N. bars prepared with M.P.C.80 toasted 4 hours at
75 Celsius degrees and 110 Celsius degrees respectively.
End of note.
Color progressively developed to a different extent for H.P.N. bars made with modified and control M.P.C.80.
Total color change (delta uppercase “E”) values of each H.P.N. bar relative to itself on day 0 are presented in
Table 2.
Note:
Table 2 says: “Model high-protein nutrition (H.P.N.) bar total color change (Delta uppercase “E”).
End of note.
H.P.N. bars prepared with unmodified M.P.C.80 underwent extensive color change during storage. M.P.C.80
toasted at 110 Celsius degrees (T.110) prior to H.P.N. bar incorporation, developed a brown color, and thus
total color change during storage of H.P.N. bars prepared with this ingredient was more reserved. The H.P.N.
bars formulated with extruded M.P.C.80 had reduced color development. We hypothesized that the color
development was due, in part, to amines taking part in Maillard reactions. This was tested by measuring free
amine in H.P.N bar samples.
Note:
Figure 3 says: “Relative free amine (percent) of model high-protein nutrition (H.P.N.) bars stored at 32 Celsius
degrees for 0, 6, 13, 22, and 42 days. M.P.C. identifies a model H.P.N. bar made with unmodified M.P.C.80;
E.65 and E.120 identify model H.P.N. bars prepared with M.P.C.80 extruded at die temperatures of 65 Celsius
degrees and 120 Celsius degrees, respectively: T75 and T110 identify model H.P.N. bars prepared with
M.P.C.80 toasted 4 hours at 75 Celsius degrees and 110 Celsius degrees, respectively”.
End of note.
Within each HPN bar batch, all samples had reduced free amine content over the storage period (lowercase
“p” inferior to 0.05). H.P.N. bars formulated with unmodified M.P.C.80, T.75, and T.110 underwent rapid and
significant free amine decline after 6 days storage at 32 Celsius degrees (lowercase “p” inferior to 0.05).
Rapid decline in relative free amine content observed is consistent with the protein bars formulated with
unmodified M.P.C.80, W.P.I., or calcium caseinate after 12 days storage at 20 Celsius degrees (Loveday et
al., 2009, 2010). H.P.N. bars formulated with extruded M.P.C.80 had no significant free amine reduction until
13 days storage. The relative free amine content in the H.P.N. bars prepared with unmodified M.P.C.80, T.75,
and T.110 were statistically equivalent to each other on each day of storage and relative free amine reduction
was greater than H.P.N. bars prepared with extruded M.P.C.80. Relative reduction in free amine progressed
with storage time in all model H.P.N. bars. This differed from a reported amine content plateau after 12 days
storage at 20 Celsius degrees for protein bars formulated with unmodified M.P.C.80 (Loveday et al., 2009),
rather is similar to those protein bars formulated with calcium caseinate (Loveday et al., 2010).
Soluble protein in the model H.P.N. bar extracts ranged from 0.75 to 3.34 milligrams protein per milliliters
and decreased with increased storage time. Protein content of all H.P.N. bar extractions was standardized to
the soluble protein content of the H.P.N. bar prepared with T.110 stored for 42 days for each measurement to
help alleviate the effect of reduced protein solubility on free amine results. The calculated protein solubility
for the H.P.N. bar prepared with T.110 after 42 days storage ranged from 0.54 to 1.11 miligrams protein per
milliliters in three separate extractions and was always the H.P.N. bar sample with the lowest protein
solubility.
Magnitude of relative free amine reduction in the model H.P.N. bars prepared with extruded M.P.C.80 might
be less than the other H.P.N. bar samples since lysine, a free-amine containing amino acid, in M.P.I. co-
extruded with reducing sugars had low retention (Singh, Wakeling, & Gamlath, 2007). Lysine destruction
upon extrusion of M.P.C.80 may limit Maillard browning in those H.P.N. bars formulated with extruded
M.P.C.80, which translates into less color change. T.110 browned during toasting due to Maillard browning
and likely contained less lysine available to participate in Maillard browning during H.P.N. bar storage.
Advanced Maillard browning products (this is, glyoxal, methylglyoxal) and the environmental conditions that
favor the progression of the reaction, contribute to the development of protein crosslinks, including disulfide
bonds, that can create a hydrophobic network that expels water from the local protein domain and thus may
facilitate H.P.N. bar hardening (Anema, Pinder, Hunter, & Hemar, 2006; Gerrard, 2002; Lederer & Klaiber,
1999; Le et al., 2011; Zhou, Liu, & Labuza, 2008a). However, in one study Maillard browning was inhibited
in H.P.N. bars by sulfite addition and the bars still continued to harden, which has prompted some researchers
to refute this suggested mechanism (Baier et al., 2007).
Note:
Figure 4 says: “Representative stress-relaxation plots for a model high-protein nutrition (H.P.N.) bar sample
prepared with unmodified M.P.C.80 stored for 42 days at 32 Celsius degrees. Plot “A”: stress versus time
data, and Plot “B”: linearized data following Equation (1). Linear regression was used to determine lowercase
“k” subscript 2 (this is, slope) and lowercase “k” subscript 1, this is, “y”-intercept), the viscoelastic properties
of the H.P.N. bar samples.
End of note.
Mean initial stress (sigma subscript “zero”) values obtained at the beginning of compression for each H.P.N.
bar sample are presented in Table 3.
Note:
Table 3 says: “Model high-protein nutrition (h.p.n.) bar stress-relaxation analysis: initial stress (sigma
subscript “zero” in kiloPascals).
End of note.
The stress-relaxation parameters calculated from normalized stress plots and Eq. (2), including the average
slope of linearized plots (lowercase “k” subscript 2), the initial decay rate of the stress ratio (“1” divided by
lowercase “k” subscript “1”), and the predicted sample stress at equilibrium (sigma subscript “e”), are
presented in Tables 4 to 6, respectively.
Initial sample stress (sigma subscript “zero”) increased significantly in all model HPN bars during 42 days
storage at 22, 32, or 42 Celsius degrees (Table 3). The H.P.N. bars formulated with E.65 and E.120 tended to
have lower o values and corresponded with decreased H.P.N. bar hardness (Table 7).
Note:
Table 7 says: “Model high-protein nutrition (H.P.N.) bar hardness, in Newtons”.
End of note.
Average slopes from the linearized plots (Table 4) remained greater than 1 (lowercase “k” subscript 2 superior
to 1), which suggested that the model H.P.N. bars exhibited more solid-like, as opposed to liquid-like,
viscoelastic properties.
Note:
Table 4 says: “Model high-protein nutrition (h.p.n.) bar stress-relaxation analysis: average slope from
linearized relationship (Equation (1)) (lowercase “k” subscript 2).
End of note.
The initial decay rate of the stress ratio (“1” divided by lowercase “k” subscript “1”) remained relatively the
same among samples for each fixed storage temperature and fixed storage time combination, meaning stress
decayed across each batch of H.P.N. bars at about the same internal rate (Table 5).
Note:
Table 5 says: “Model high-protein nutrition (h.p.n.) bar stress-relaxation analysis: initial decay rate of the
stress ratio (Equation (1)) (“1” divided by “k” lowercase 1, per second).
End of note.
The observed equilibrium stress after 300 seconds of compression (300 subscript 300 “s”) and the calculated
equilibrium stress (sigma subscript “e”)both of which are representative of residual internal sample stress,
were typically larger in the H.P.N. bars formulated with T.110 when compared with H.P.N. bars formulated
with extruded M.P.C.80. However, significant difference in de between batches at each fixed storage
temperature and fixed storage time combination was intermittent (Table 6).
Note:
Table 6 Model high-protein nutrition (h.p.n.) bar stress-relaxation analysis: calculated equilibrium stress
(Equation (2) (Uppercase “epsilon” subscript “e” in kiloPascals).
End of note.
The stress ratio (sigma subscript “300s” divided by sigma subscript “e”) ranged from 1.01 to 1.15 for all
prepared model H.P.N. bars, which indicated that 300 seconds worth of stress versus time data was sufficient
to accurately predict the relaxation characteristics and validate the model. No stress-relaxation analysis has
been reported in literature before for H.P.N. bars made with modified MPC80s.
Note:
Table 8 says: “Model high-protein nutrition (H.P.N.) bar fracturability, in Newtons”.
Table 9 says: “Model high-protein nutrition (H.P.N.) bar shear strength, in Newtons”.
End of note.
Statistical comparisons in these tables are made between all batches at constant storage temperature and
storage time as well as within each batch over time at constant temperature. Hardness, as instrumentally
evaluated, can be related to the force needed to compress a H.P.N. bar sample between a consumer's thumb
and index finger (Imtiaz et al., 2012). Shear force is more closely related to the force required to shear through
a sample with a consumer's front incisors (Imtiaz et al., 2012). Fracturability relates to how easily an H.P.N.
bar breaks apart during compression (Imtiaz et al., 2012). On the day of manufacture, there was no statistical
difference in H.P.N. bar hardness, fracturability, and shear strength.
H.P.N. bars prepared with extruded M.P.Cs had significantly lower hardness, fracturability, and shear strength
when compared with H.P.N. bars formulated with T.75, T.110, or unmodified M.P.C.80 with increased storage
time. The hardness and fracturability behavior of H.P.N. bars formulated with E.65 were similar to H.P.N.
bars prepared with E120 when stored at 42°C, but at lower storage temperatures significant differences
between these response variables were not consistent. Texture change at 42 Celsius degrees storage may not
follow the same mechanism as room temperature or 32 Celsius degrees storage due to moisture loss and
increased fluidity of H.P.N. bar matrix at higher temperatures. The shear strength of H.P.N. bars formulated
with E.120 did not differ significantly with H.P.N. bars formulated with unmodified M.P.C.80, except on day
42 with storage at room temperature (lowercase “p” is inferior to 0.05). HPN bars prepared with E.65 and
E.120 maintained lower hardness and fracturability toward the end of storage as well as at most instances in
the beginning.
H.P.N. bars produced with T75 were not significantly different in terms of hardness, fracturability, or shear
strength when compared to those prepared with unmodified M.P.C.80 at each fixed storage temperature and
fixed storage time combination. Hardness, fracturability, and shear strength values for the H.P.N. bars
produced with T.110 were similar to those prepared with unmodified M.P.C.80 at each fixed storage
temperature and fixed storage time combination. Toasting M.P.C.80 at the temperatures studied prior to
incorporation into model H.P.N. bars did not slow texture change when compared to H.P.N. bars prepared
with an unmodified control M.P.C.80.
Hardness and fracturability data should be compared side-by-side because in some instances the force needed
to cause initial fracture was greater than the hardness value obtained at 60% compression. This occurred
predominantly for the H.P.N. bars formulated with T110 after 2 days storage at both 22 Celsius degrees and
32 Celsius degrees, and in less than 24 hours at 42 Celsius degrees. The H.P.N. bars prepared with extruded
M.P.C.80 also exhibited this trend with storage at 42 Celsius degrees. At 22 Celsius degrees storage, only the
HPN bars formulated with T.110 had higher fracturability force than hardness at 60% compression. A
fracturability force greater than sample hardness is common among H.P.N. bar samples that lack cohesion and
crumble upon initial fracture. Decreased H.P.N. bar cohesiveness or increased crumbliness is another problem
that occurs in H.P.N. bars formulated with M.P.C. or M.P.I. (Imtiaz et al., 2012; Li et al., 2008). H.P.N. bars
formulated with unmodified M.P.C.80 also lacked cohesion, but the difference between fracturability and
hardness here was overshadowed by the large differences between these values in the H.P.N. bars formulated
with T.110.
Performance of protein ingredients, this is, M.P.C., E.65, E.120, T.75, and T.110, in the model H.P.N. bars
was shown to be related to its own functional properties discussed in Banach et al. (2013). 175 exhibited
similar reduced and non-reduced S.D.S.-P.A.G.E. profiles, protein solubility, surface hydrophobicity, and gel
strength as unmodified M.P.C.80 and thus similar performance in the model H.P.N. bar was not surprising.
T.110 may have reduced ability to interact with water molecules, as suggested by reduced water-holding
capacity (Banach et al., 2013), and thus became firmer with inability to maintain a well plasticized state.
H.P.N. bars prepared with extruded M.P.Cs may have remained softer due to the formation of disulfide bonds
in these protein ingredients prior to incorporation into the H.P.N. bar matrix. Beta-Lg in extruded M.P.C.80
was soluble only under reduced conditions and was insoluble under non-reduced conditions due to intact
disulfide bonds (Banach et al., 2013; Onwulata, Phillips, Tunick, Qi, & Cooke, 2010). Beta-Lg solubility in
T.110 was not completely regained under reduced conditions, which suggested another possible mechanism
of insolubility other than disulfide bond formation. This helps explain why H.P.N. bars formulated with
toasted M.P.C., which involved heat without shearing force during production performed differently than E.65
and E.120, the extruded M.P.Cs used in this study (Banach et al., 2013).
4. Conclusion
Unmodified, extruded, and toasted M.P.C.80s were used to formulate model H.P.N. bars and measure change
in water activity, color, relative free amine content, and texture. M.P.C.80 toasted at 75 Celsius degrees or 110
Celsius degrees for 4 hours prior to incorporation produced model H.P.N. bars that hardened similarly to
model H.P.N. bars formulated with unmodified M.P.C.80. Toasting M.P.C.80 at these conditions did not
improve performance and it is unlikely toasting modification will enhance M.P.C. feasibility in H.P.N. bars.
However, M.P.C.80 extruded at die temperatures of 65 Celsius degrees and 120 Celsius degrees lessened
textural changes when compared with H.P.N. bars formulated with unmodified M.P.C.80. The M.P.C.80
extruded at 65 Celsius degrees fared significantly better than the M.P.C.80 extruded at 120 Celsius degrees in
the model HPN bars. Extruding M.P.C.80 prior to use in H.P.N. bars may serve as a way to lessen hardening
and extend the textural shelf-life. Increased M.P.C.80 use in H.P.N. bar applications stands to benefit the dairy
industry through increased demand for a complete dairy protein derived directly from skim milk as opposed
to use of a dairy protein fractions or another protein source.