Professional Documents
Culture Documents
Article history: Functional properties of conventional oat materials are relatively poor with respect to foam and emul-
Received 22 January 2013 sion formation and stabilization. This is largely due to the poor solubility of oat proteins and the presence
Received in revised form of lipids in aqueous extracts of oats. In the experimental part of this study, extracts were prepared from
1 November 2013 different type oat flours (oat endosperm flour, oat fine flour, CO2-defatted whole oat flour and CO2-
Accepted 17 January 2014
defatted oat flour) with a buffered aqueous extraction procedure at acidic (pH 4.5 and 6.5) and basic (pH
8.5 and 10.5) regions. The solubility of proteins was the highest at pH 10.5 and NaCl concentration of 2%.
Keywords: Among the extracts, CO2-oat flour showed improved foaming and emulsifying properties at basic pH
Oats
values. The presence of 0.1% NaCl resulted in the lowest foam volumes, but the emulsion activity and
Solubility
stability values being the highest. Sucrose addition resulted in increased foam and emulsion stability of
Foaming
Emulsification suspensions. Heat treatment at 80 ◦C impaired foam properties, whereas the stability of emulsions increased
with the increase in temperature from 20 ◦C to 80 ◦C. CO2-extracted oats can be useful raw
materials in beverages and other aqueous applications where protein functionality plays an important
role.
© 2014 Elsevier Ltd. All rights reserved.
http://dx.doi.org/10.1016/j.jcs.2014.01.013
0733-5210/© 2014 Elsevier Ltd. All rights reserved.
Please cite this article in press as: Konak, Ü.I_., et al., CO2-defatted oats: Solubility, emulsification and foaming properties, Journal of Cereal
Science (2014), http://dx.doi.org/10.1016/j.jcs.2014.01.013
2 Ü.I_ . Konak et al. / Journal of Cereal Science xxx (2014) 1e5
showed that oat protein concentrates and isolates had good 2.2.3. Foaming properties
emulsifying and fat binding properties. Moreover, oat albu- mins Foaming of 10 mL aliquots of different flour derived extracts
were shown to possess the best foaming ability among other oat were done using a household milk foamer (OBH Nordica6856)
storage proteins . modified with electric plug and whipping for 2 min. Further foaming
Oat protein concentrates and isolates contain lipids, mainly non- tests with CO2-oat flour derived extracts were prepared bywhipping
polar lipids, as oat grain contains high amounts of lipids of which 75 mL of the extract for 2 min with a household mixer (Philips
80% is soluble in non-polar solvents and thus co-extracted with Cucina HR1560, The Netherlands) at highest speed in a 500 mL
proteins. Often interaction of proteins with polar lipids enhances measuring cylinder. Foam volume was recorded immedi- ately after
the foaming attributes, whereas non-polar lipids are often whipping and after 5, 10 and 30 min standing.
detrimental to foam structures (Dubreil et al., 1997; Sroan and
MacRitchie, 2009). Lipid content of oat protein concentrates was 2.2.4. Emulsification properties
shown to decrease their foaming properties (Ma, 1983). The The extracts were analyzed by the turbidimetric technique for
removal of non-polar lipids by supercritical carbondioxide (SC-CO2) emulsion activity index (EAI) and emulsion stability index (ESI) as
extraction improved the foam formation of aqueous oat extracts, previously described (Pearce and Kinsella, 1978). The extract (30
which was linked to the presence of tryp- tophanin proteins in oat mL) and vegetable oil (10 mL) were mixed in an Erlenmeyer flask.
foams and further demonstrated to affect the performance in model The mixture was homogenized using an Ultra-Turrax model T25
baking (Kaukonen et al., 2011). No previous studies, however, exist homogenizer with S25N-25F dispersing element (IKA, Werke
on the solubility and emulsifica- tion properties of SC-CO2 treated GmbH & Co. KG, Germany) at a speed of 19,000 rpm for 1 min. An
oats. The objective of this study was to investigate the solubility, aliquot of the emulsion (50 mL) was taken from the bottom of the
foaming and emulsificationproperties of differently prepared oat flask at 0 and 10 min after homogenization. The aliquot was diluted
flours and the effect of pH, salt, sugar and temperature on the in 5 mL 0.1% sodium dodecyl sulfate (SDS) solution. The absorbance of
functional properties. The emphasis was to characterize these the diluted solution was measured at 500 nm. The EAI (m 2/g) and ESI
functionalities for non-polar lipid-free oat material. (min) were calculated as follow:
2 × 2:303 × A0
2. Material and methods EAI
¼
0:25 × proteinðgÞ
2.1. Material
Dt
ESI ¼ A0 ×
Oat endosperm flour was commercial organic oat flour from DA
Helsingin Mylly Oy (Järvenpää, Finland). The oat fine flour was
where A0 was the absorbance read at 0 min, Dt was 10 min and DA
commercial oat flour from Swedish Oat Fiber Ab (Bua, Sweden).
was the difference in absorbance value read at 0 and 10 min.
CO2-whole oat flour and CO2-oat flour obtained from dehulled oats
were supplied by VTT Technical Research Centre of Finland (Espoo,
2.2.5. Salt/sugar addition and thermal treatment
Finland), and their manufacture process is previously described by
Effects of salt and sugar addition and heat treatment on foaming
Sibakov et al. (2011). In addition, the lipid profiles of various oat raw
materials were previously investigated as well as the lipids and emulsifying properties of extracts prepared at pH 10.5 were
removed during the SC-CO2 extraction (see Kaukonen et al., 2011). evaluated. Salt concentrations of 0.1, 0.5, 1 and 2% and sugar con-
Salt (NaCl) and sugar (saccharose) were purchased from Merck centrations of 1, 5, 10 and 25% were investigated. Besides at room
(Darmstadt, Germany) and SigmaeAldrich (St. Louis, MO, USA), temperature, the foaming and emulsification procedure were per-
respectively. formed at 50 ◦C and 80 ◦C.
Please cite this article in press as: Konak, Ü.I_., et al., CO2-defatted oats: Solubility, emulsification and foaming properties, Journal of Cereal
Science (2014), http://dx.doi.org/10.1016/j.jcs.2014.01.013
Ü.I_. Konak et al. / Journal of Cereal Science xxx (2014) 1e5 3
80 80 80 80
60 60 60 60
40 40 40 40
20 20 20 20
0 0 0 0
0% 0.5% 1% 2% 0% 0.5% 1% 2% 0% 0.5% 1% 2% 0% 0.1% 0.5% 1% 2%
pH 4.5 pH 6.5 pH 8.5 pH 10.5
Fig. 1. Amount of soluble protein (mg/g) in oat flour derived extracts. The solubility was determined at different NaCl-concentrations (%-value) under different pH-conditions.
classification fractionation method made it possible to prepare a 3.3. Foaming of CO2-oat extracts
protein-rich oat flour fraction (Sibakov et al., 2011).
Effects of pH and NaCl concentration on protein solubility are Protein contents of the CO2-oat extracts at different pH-levels
also shown in Fig. 1. Results revealed that solubility was pH- and foam volume produced from CO2-oat flour derived extracts are
dependent and was also significantly (p < 0.05) affected by NaCl presented in Table 1. The solubility of proteins increased with
addition. For all samples, the solubility was the lowest at pH increase in pH and the protein content reached the highest value in
4.5 and increased with increasing pH, and reached the highestvalue the extract produced at pH 10.5. Foamability of the CO2-oat flour
at pH 10.5. It was observed that the solubility of CO2-oat proteins derived extracts (100 mL) produced at different pH values was also
was remarkably higher at the alkaline pH than the acidic pH. This improved with extraction pH. The 0 min foam volumes increased
could be because of the increased net protein charge asa result of from 240 mL (pH 4.5) to 323 mL (pH 10.5) (Table 1). Moreover, the
elevating the pH (above the isoelectric point). This is similar to the relative stability of foams (volume at 30 min/volume at
reported solubility obtained by Ma and Harwalkar (1984); Wang et 0 min × 100) increased as well from 69 to 80% when the pH was
al. (1999); Khalid et al. (2003) and Ogunwoluet al. (2009) for oat, increased from 4.5 to 10.5, respectively (data not shown). This in-
rice bran, sesame seed and cashew nut proteins, respectively. crease in foam stability might be attributed to the improved solu-
bility of proteins at higher pH as the correlation between the
3.2. Foaming of different oat flours protein content of the extracts and volume of foam produced during
2 min whipping was strong (R2 0.96). Moreover,
¼ solely theabsence
The foaming ability of extracts produced from different flours of non-polar lipids can increase the affinity of surface active
was determined at different pH values. Foaming experiments were proteins at the airewater interface resulting in improved foaming
performed with 10 mL aliquots of extracts. The foam volume of (Paternotte et al., 1993). The results on the effect of pH on the
extracts produced from oat endosperm flour, oat fine flour, CO2- solubility of proteins reflect their behavior in foaming (Figs. 1 and
whole oat flour and CO2-oat flour are shown in Fig. 2. The extracts 2). The improved foamability in the alkaline pH region couldbe
from oat endosperm flour and oat fine flour showed poorer foam- explained by the higher solubility of the proteins in this region. The
ing capacity compared to the extracts from both CO2-whole oat flour results closely agree with those observed for pigeon pea (Akintayo
and CO2-oat flour. Oat endosperm flour did not produce any et al., 1999), for instance.
measurable foam. The lower foaming capacity of the non-CO2- The effects of NaCl, sucrose concentrations and foaming tem-
treated samples was likely due to the presence of non-polar lipids perature on foam volumes of CO2-oat flour derived extracts pro-
in the water extracts as reported previously (Kaukonen et al., 2011). duced at pH 10.5 were determined (Fig. 3). The results showed that
Based on the foaming results, CO2-oat flour was selected for further the foamability was similar in all NaCl concentrations with the
analyses. exception of 0.1% which resulted in the lowest foam volumes (Fig.
3A). Thus, increasing NaCl concentration did not systemati- cally
affect the foaming ability as it reached the lowest values at 0.1%
NaCl.
Table 1
Protein content of extracts prepared from CO 2-oats and volume of foam produced from
the extracts. Results are presented as the mean standard deviation. Protein content is
expressed on a dry weight basis.
Please cite this article in press as: Konak, Ü.I_., et al., CO2-defatted oats: Solubility, emulsification and foaming properties, Journal of Cereal
Science (2014), http://dx.doi.org/10.1016/j.jcs.2014.01.013
4 Ü.I_ . Konak et al. / Journal of Cereal Science xxx (2014) 1e5
Fig. 3. Foam volumes of CO2-oat extracts (at pH 10.5) with different concentration of NaCl (A), sucrose (B) and at different temperatures (C).
Similarly to salt concentrations, varying sucrose levels from 0% oat globulin polypeptides are between pH 4e5 and pH 7e8,
to 25% (w/v) had practically no influence on foamability of CO2-oat respectively (Walburg and Larkins, 1983) Oat globulins (dimeric
flour derived extracts (Fig. 3B). However, the presence of sucrose form of acidic and basic polypeptide) were the major proteins in
delayed the drainage from foam (data not shown). Lau and water extracts used for emulsion preparations (data not shown).
Dickinson (2005) stated that the addition of sugar results in The effects of NaCl, sucrose and emulsification temperature on
increased viscosity of the continuous phase, which in turn was EAI and ESI of CO2-oat extracts produced at pH 10.5 are shown in
disadvantageous for the air incorporation and the rapid diffusion of Fig. 5. EAI and ESI values were clearly optimal at 0.1% NaCl con-
the protein to the interface. Sugars can contribute, thus, to foam centration as the values were lower in the absence of NaCl and
stability by increasing the viscosity of the liquid phase in the lamella decreased with higher NaCl concentrations (Fig. 5A). According to
and thereby retarding drainage (Walstra, 2002). Kim et al. (2002), protein unfolding occurred at the droplet inter-
The foam volumes of CO2-oats derived extracts (pH 10.5) were face in the presence of 0.1e0.9%, salt which enhanced the hydro-
also determined after foams were prepared at different tem- phobic attraction and disulfide bond formation between the
peratures (Fig. 3C). Increasing temperature from 20 ◦C to 50 ◦C droplets.
and further to 80 ◦C systematically decreased the foam volumes. In the present study, EAI was not influenced by sugar addition.
The foam was stable at 50 ◦C as 71% of the original foam volume No significant difference among the sucrose concentrations of 1e
was retained after 30 min. Instead, at 80 ◦C, the relative foam 10% was observed in ESI values either. However, a significant (p
volume was only 9% at 30 min, which means that the foam had < 0.05) increase in ESI at the highest sucrose concentration of 25%
collapsed. compared to 0% was observed (Fig. 5B). An increase in the
emulsification temperature caused a slight decrease in the emul-
3.4. Emulsifying properties of CO2-oat extracts sion activity (EAI) whereas emulsion stability (ESI) increased with
increasing temperature from 20 to 80 ◦C (Fig. 5C). The effect of heat
Both EAI and ESI of the emulsions prepared from CO2-oat ex- treatment on the rheological properties of emulsions prepared with
tracts at different pH values are shown in Fig. 4. The lowest EAI (1.7 soybean protein dispersions of different concentrations were
m2/g) and ESI (21.1 min) values were found at pH 4.5, whereas,the studied by Puppo et al. (2003) who showed that heating high
highest values, 15.4 m2/g and 411.3 min, were observed at pH protein concentration emulsions formed a viscoelastic network that
10.5. While emulsion activity was enhanced gradually with stabilized the emulsion potentially due to crosslinking of proteins
increasing pH, the emulsion stability was similar between pH 4.5 at higher temperature.
and 8.5. However, a significant (p < 0.05) increase in ESI was Largely due to the higher protein content, the extracts prepared
observed at pH 10.5. Proteins tend to aggregate at pH values close to from CO2-oats showed good foaming and emulsification properties
their pI which may result in poor emulsifying properties (Scopes, compared to other oat materials. Moreover, the previously
1994). Emulsifying activity and emulsion stability were lower at demonstrated absence of nonpolar lipids and the presence of
acidic and neutral pH conditions, which are closer to the isoelectric tryptophanin proteins in the water extracts of CO2-oats (Kaukonen
range of oat proteins. The isoelectric ranges of the acidic and basic et al., 2011) likely played roles in the interfacial behavior of oat
proteins.
4. Conclusion
The present study showed that partially defatted oat flour pre-
pared with SC-CO2 extraction, had good functional properties
compared to the conventional oat flours. This can be linked to the
amount of soluble protein, but also to the known presence of
tryptophanin proteins and the absence of nonpolar lipids in
aqueous extracts prepared from CO2-oats. It was also demonstrated
that the functional properties of CO2-oats are to some extent
dependent on and, thereby, can be adjusted by chemical conditions
as the effects of NaCl, sucrose and pH as well as heating influenced
Fig. 4. EAI (m2/g) and ESI (min) values of CO2-oat extracts produced at different pH- foam and emulsion properties. On the other hand some of the
conditions. functionalities tolerated the conditions relatively well, which can
Please cite this article in press as: Konak, Ü.I_., et al., CO2-defatted oats: Solubility, emulsification and foaming properties, Journal of Cereal
Science (2014), http://dx.doi.org/10.1016/j.jcs.2014.01.013
Ü.I_. Konak et al. / Journal of Cereal Science xxx (2014) 1e5 5
Fig. 5. EAI (m2/g, black bar) and ESI (min, gray bar) values of CO2-oat extracts produced at different NaCl (A) and sucrose concentrations (B), and at different temperatures (C).
also be considered as a positive feature. The CO2-extracted oatflours Ma, C.Y., Harwalkar, V.R., 1987. Thermal coagulation of oat globulin. Cereal Chem.
64, 212e218.
might serve as a promising cereal raw material in beverages and
Marcone, M.F., Kakuda, Y., Yada, R.Y., 1998. Salt-soluble seed globulins of dicotyle-
other aqueous food applications utilizing oats. donous and monocotyledonous plants II. Structural characterization. Food
Chem. 63, 265e274.
Acknowledgments Meng, G., Ma, C.Y., 2002. Characterization of globulin from Phaseolus angularis (red
bean). Int. J. Food Sci. Technol. 37, 687e695.
Naik, A.D., Bhagwat, S.S., 2005. Optimization of an artificial neural network for
JL and TSS acknowledge University of Helsinki Funds, and DEC modeling protein solubility. J. Chem. Eng. Data 50, 460e467.
acknowledges the funding from the Academy of Finland. Ogunwolu, S.O., Henshaw, F.O., Mock, H.P., Santros, A., Awonorin, S.O., 2009.
Functional properties of protein concentrates and isolates produced from cashew
(Anacardium occidentale L.) nut. Food Chem. 115, 852e858.
References Paternotte, T.A., Orsel, R., Hamer, R.J., 1993. Interactions between flour proteins and
flour lipids at the liquid/air interface. In: Gluten Proteins. Association of Cereal
Akintayo, E.T., Oshodi, A.A., Esuoso, K.O., 1999. Effects of NaCl, ionic strength and pH Research, Detmold, Germany, pp. 207e217.
on the foaming and gelation of pigeon pea (Cajanus cajan) protein concentrates. Pearce, K.N., Kinsella, J.E., 1978. Emulsifying properties of proteins: evaluation of a
Food Chem. 66, 51e56. turbidimetric technique. J. Agric. Food Chem. 26, 716e723.
Colyer, T.E., Luthe, D.S., 1984. Quantitation of oat globulin by radioimmunoassay. Puppo, M.C., Sorgentini, D.A., Añón, M.C., 2003. Rheological properties of emulsions
Plant Physiol. 74, 455e456. containing modified soy protein isolates. J. Am. Oil. Chem. Soc. 80, 605e611.
Dubreil, L., Compoint, J.P., Marion, D., 1997. Interaction of puroindolines with wheat Ruckenstein, E., Shulgin, I.L., 2006. Effect of salts and organic additives on the solubility
flour polar lipids determines their foaming properties. J. Agric. Food Chem. 45, of proteins in aqueous solutions. Adv. Colloid Interface Sci. 123e126, 97e103.
108e116. Schmidt, I., Novales, B., Boué, F., Axelos, M.A.V., 2010. Foaming properties of protein/
Flander, L., Salmenkallio-Marttila, M., Suortti, T., Autio, K., 2007. Optimization of pectin electrostatic complexes and foam structure at nanoscale. J. Colloid Interface
ingredients and baking process for improved wholemeal oat bread quality. Sci. 345, 316e324.
LWT-Food Sci. Technol. 40, 860e870. Scopes, R.K., 1994. Protein Purification Principles and Practice, third ed. Springer-
Foegeding, E.A., Luck, P.J., Davis, J.P., 2006. Factors determining the physical prop- Verlag, Inc., New York, USA.
erties of protein foams. Food Hydrocoll. 20, 284e292. Sibakov, J., Myllymäki, O., Holopainen, U., Kaukovirta-Norja, A., Hietaniemi, V., Pihlava,
Kaukonen, O., Sontag-Strohm, T., Salovaara, H., Lampi, A.-M., Sibakov, J., Loponen, J., J.-M., Poutanen, K., Lehtinen, P., 2011. Lipid removal enhances separa- tion of oat
2011. Foaming of differently processed oats: role of nonpolar lipids and tryp- grain cell wall material from starch and protein. J. Cereal Sci. 54, 104e109.
tophanin proteins. Cereal Chem. 88, 239e244. Smith, D.M., 2003. Measurement of functional properties: overview of protein
Khalid, E.K., Babiker, E.E., El Tinay, A.H., 2003. Solubility and functional properties of functionality testing. In: Wrolstad, R.E., Acree, T.E., Decker, E.A., Penner, M.H., Reid,
sesame seed proteins as influenced by pH and/or salt concentration. Food Chem. D.S., Schwartz, S.J., Shoemaker, C.F., Smith, D.M., Sporns, P. (Eds.), Current
82, 361e366. Protocols in Food Analytical Chemistry. John Wiley & Sons Inc, pp. 266e269.
Kim, H.J., Decker, E.A., McClements, D.J., 2002. Impact of protein surface denatur- ation Sroan, B.S., MacRitchie, F., 2009. Mechanism of gas cell stabilization in breadmak- ing.
on droplet flocculation in hexadecane oil-in-water emulsions stabilized by b- II. Secondary liquid lamellae. J. Cereal Sci. 49, 41e46.
lactoglobulin. J. Agric. Food Chem. 50, 7131e7137. Walburg, G., Larkins, B.A., 1983. Oat seed globulin: subunit characterization and
Lapveteläinen, A., Aro, T., 1994. Protein composition and functionality of high- demonstration of its synthesis as a precursor. Plant Physiol. 72, 161e165.
protein oat flour derived from integrated starch-ethanol process. Cereal Chem. Walstra, P., 2002. Formation of emulsions and foams (Chapter 11). In: Physical
71, 133e139. Chemistry of Foods. CRC Press, ISBN 978-0-203-91043-6 eBook.
Lau, C.K., Dickinson, E., 2005. Instability and structural change in an aerated system Wang, M., Hettiarachchy, N.S., Qi, M., Burks, W., Siebenmorgen, T., 1999. Preparation
containing egg albumen and invert sugar. Food Hydrocoll. 19, 111e121. and functional properties of Rice bran protein isolate. J. Agric. Food Chem. 47,
Loponen, J., Laine, P., Sontag-Strohm, T., Salovaara, H., 2007. Behavior of oat globulins 411e416.
in lactic acid fermentation of oat bran. Eur. Food Res. Technol. 225, 105e110. Wilde, P.J., 2000. Interfaces: their role in foam and emulsion behaviour. Curr. Opin.
Ma, C.Y., 1983. Chemical characterization and functionality assessment of protein Colloid Interface Sci. 5, 176e181.
concentrates from oats. Cereal Chem. 60, 36e42. Youngs, V.L., 1986. Oat lipids and lipid-related enzymes. In: Webster, F.H. (Ed.), Oats:
Ma, C.Y., Harwalkar, V.R., 1984. Chemical characterization and functionality Chemistry and Technology. AACC International, St. Paul, MN, pp. 205e226.
assessment of oat protein fractions. J. Agric. Food Chem. 32, 144e149.
Please cite this article in press as: Konak, Ü.I_., et al., CO2-defatted oats: Solubility, emulsification and foaming properties, Journal of Cereal
Science (2014), http://dx.doi.org/10.1016/j.jcs.2014.01.013