Food Research International 44 (2011) 684692

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Food Research International

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Emulsifying and foaming capacity and emulsion and foam stability of sesame protein concentrates
Alicia Cano-Medina a, Hugo Jimnez-Islas b, Luc Dendooven c, Rosalba Patio Herrera a, Guillermo Gonzlez-Alatorre a, Eleazar M. Escamilla-Silva a,
a b c

Chemical Department, Instituto Tecnolgico de Celaya. Ave. Tecnolgico y A. Garca Cubas S/N. C.P. 38010. Celaya, Gto., Mexico Biochemical Engineering Department, Instituto Tecnolgico de Celaya. Ave. Tecnolgico y A. Garca Cubas S/N. C.P. 38010. Celaya, Gto., Mexico Laboratory of Soils Ecology, Department of Biotechnology and Bioengineering, CINVESTAV, Ave. Instituto Politcnico Nacional 2508, A.P. 14740, C.P. 07360 Mxico D.F., Mexico

a r t i c l e

i n f o

a b s t r a c t
This study examined the effects of oil concentration and pH on the emulsifying and foaming characteristics of sesame protein concentrate (SESPC). SESPC was obtained through a simplied process, and its properties were compared with those of a commercial soybean concentrate (SOYPC). The simplied process did not affect the functional characteristics of SESPC, which were often similar or superior to those of the SOYPC. The maximum emulsifying capacity of SESPC was 38% at an acidic and alkaline pH, while the maximum emulsifying capacity of SOYPC was 44% at the same pH. Emulsifying capacity increased signicantly as oil concentration increased; in SESPC, this capacity increased from 7.8 to 60.0%, while in SOYPC it increased from 7.6 to 68.2%. The emulsion stability of SESPC was greater at an acidic pH (51%) than at an alkaline pH (45%); it was also higher than the emulsion stability of SOYPC. The maximum emulsion stability of SESPC (96%) was obtained at a sample concentration greater than 55 g L 1 and oil concentration lees than 550 g L 1 oil. Minimum (118.3%) and maximum (240%) levels of SESPC foaming capacity were higher than those obtained for SOYPC (92% as maximum). These ndings show that SESPC may have potential use as raw matter in the food industry. At an extreme pH, SESPC continued to have important functional characteristics like emulsion stability, oil absorption and foaming capacity. 2010 Elsevier Ltd. All rights reserved.

Article history: Received 12 May 2010 Accepted 6 December 2010 Keywords: Functional properties Oil concentrations pH Production process Sesame protein concentrate Soybean protein concentrate

1. Introduction Sesame seed (Sesamun indicum) has an oil content of between 48% and 55%; as a result, it has become one of the main sources of edible oil. It is also a good source of protein, yielding between 20% and 25% protein depending on the variety (Paredes-Lpez, Guzmn-Maldonado, & Ordorica-Falomir, 1994). One of the principal characteristics of this protein is its high methionine and tryptophan content. In fact, it is this methionine content that distinguishes sesame from other oil seeds. Sesame is, however, decient in lysine and isoleucine (Paredes-Lpez et al., 1994). Sesame seed is important as a source of protein, but it has some undesirable nutritional characteristics (as phytic acid); these characteristics can be signicantly reduced when the hull is removed (Shamanthaka-Sastry, Subramanian, & Parpia, 1974). Dehulled seeds conserve signicant levels of ber (4.04.5%), phytic acid (more than 2.0%) and oxalic acid (more than 3.0%) (Paredes-Lpez et al., 1994; Toma, Tabekhia, & Willians, 1979). These compounds have welldocumented negative effects on the nutritional and functional properties of proteins and on the absorption of calcium, iron and zinc
Corresponding author. Instituto Tecnolgico de Celaya, Dep. de Ingeniera Qumica, Ave. Tecnolgico y Antonio Garca Cubas, CP.38010, Celaya Gto., Mexico. E-mail address: eleazar.escamilla@itcelaya.edu.mx (E.M. Escamilla-Silva). 0963-9969/$ see front matter 2010 Elsevier Ltd. All rights reserved. doi:10.1016/j.foodres.2010.12.015

present in the human diet; they must therefore be reduced or eliminated (Cheryan, 1980; Frossard, Bucher, Machler, Mozafar, & Hurrell, 2000). Sesame proteins, while contributing to the nutritional value of foods, can also be used as additives; their interesting functional properties reect their physico-chemical characteristics, composition and structure (Wagner & Gueguen, 1999; Autran, Halford, & Shewry, 2001; Bradley, 2002; Escamilla-Silva, Guzmn-Maldonado, CanoMedina, & Gonzlez-Alatorre, 2003). The sub-product of the oil extraction process is sesame cake, whose protein content can reach 50% depending on the extraction method (Paredes-Lpez et al., 1994). However, oil extraction processes also increase the content of antinutritional components such as phytic acid, which increases from 2% to 5%, and crude ber, which increases to 5.3%. Despite these disadvantages, sesame cake has traditionally been used as animal feed due to its high content of quality protein (Little, van der Grinten, Dwinger, Agyemang, & Kora, 1991). Attempts have been made to use it as a source of protein for human consumption. We hypothesized that the modication of some characteristics of sesame proteins could improve its physicalchemical properties. Emulsifying capacity (EC) and emulsion stability (ES) are two important functional characteristics of proteins that affect the behavior of various industrial products, including adhesives, cosmetics and

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packing material (Hettiarachy & Kalapathy, 1998; Wagner & Gueguen, 1999). Sesame proteins are a by-product of these industrial processes. Because the extraction process is inexpensive, the protein concentrate has an attractive and economic cost. EC and ES are critical parameters that affect the choice of a protein for use in an industrial process. Proteins can reduce tension at the wateroil interface and help prevent coalescence (McWatters & Cherry, 1981). A protein's stabilizing effect in an emulsion comes from the membrane matrix that surrounds the oil drop and prevents its coalescence (Jones, 1984). Another practical application of proteins in industrial production comes from their ability to generate foam. Foaming capacity (FC) and foam stability (FS) are important parameters in the characterization of the functional properties of proteins. Proteins must be highly soluble in water, exible and form part of a cohesive lm at the waterair interface to ensure good foam formation (Wagner & Gueguen, 1999). The lm should possess sufcient viscosity to maintain stability and prevent rupture and subsequent coalescence. Lipids are the main cause of destabilization of the foam from protein concentrates and isolates. Studies have shown that the removal of neutral lipids with hexane and of polar lipids with aqueous alcohol leads to a marked increase in the foaming properties of soybean proteins. In addition, the foaming properties of these proteins increase when the product is heated to 7580 C. Although soybean proteins have a good foaming capacity after both heating and the extraction of lipids, the practical applications of these proteins are still limited by their structural instability (i.e., the rupture of hydrogen and disulphide bonds) (Hutton & Campbell, 1977; Inyang & Nwadimkpa, 1992). Sesame proteins can add avor to foams, emulsions and gels used in a many food products. There is therefore continued interest in improving the functional properties of sesame proteins to ensure attractive products (Escamilla-Silva et al., 2003). One way to increase the functional properties of a protein is to determine its origin and concentration as well as the mechanical forces used for its extraction (Hutton & Campbell, 1977). Additionally, the effect of drying conditions on the functional properties of protein concentrates and isolates must be investigated (Gueguen & Cerletti, 1994). Drum drying, as opposed to spray and freeze drying, increases the emulsifying capacity of pea, fava bean and soybean proteins (Gueguen & Cerletti, 1994). An increase in drying temperature from 50 C to 98 C, however, gradually reduces the solubility and emulsifying properties of proteins. Most of the variation in functional properties is related to modications of protein structure that result from processing conditions. The objective of the present work was to study the EC, ES, FC and FS of sesame protein concentrate (SESPC). The SESPC was obtained with a simplied method in which the product of an alkaline extraction did not undergo isoelectric precipitation or protein neutralization (Escamilla-Silva et al., 2003).This study examined the effects of SESPC concentration, oil concentration and pH on EC and ES; while SESPC concentration and pH on FC and FS. These properties were compared with those of a commercial soybean protein concentrate (SOYPC). 2. Materials and methods 2.1. Proteins Sesame meal (b 1% oil), made from defatted and mechanically dehulled seed, was obtained from DIPASA, Mexico, a local company specializing in oil production. The proteins were obtained from defatted sesame meal through alkaline extraction at pH 9 at a 1:10 (w/v) meal: water ratio at room temperature. The extraction mixture was ltered and a protein-rich aqueous solution was recovered. The SESPC was obtained by a simplied process, i.e., direct spray-drying of the proteinrich aqueous solution without isoelectric precipitation and neutraliza-

tion (Escamilla-Silva et al., 2003; Hutton & Campbell, 1977). A soybean protein concentrate was obtained from a local business (FABSA, Mexico) so the functional characteristics of the sesame protein concentrate could be compared with those of a commercial product. 2.2. Emulsifying capacity and emulsion stability The EC of SESPC and SOYPC were measured according to the method described by Wang and Kinsella (1976). Aqueous dispersions of 25, 50 and 75 g L 1 of both products were prepared and adjusted to pH 4.5, 7.0, and 9.5 with 0.01 M HCl or NaOH. The dispersions were blended at high speed (10,000 rpm) while corn oil was poured into the blender at a ow rate of 1 mL s 1.The nal concentration of oil in each sample was 50, 200, 400, and 550 g kg 1. After agitation, the samples were centrifuged at 5000 rpm for 5 min in a Gallenkamp centrifuge. The EC was expressed as: EC % = Height of the emulsified layer cm 100: Total height cm

A similar procedure was followed to determine the ES, but the samples were incubated at 80 C for 30 min before centrifugation. The ES was calculated with the same formula. 2.3. Foaming capacity and foam stability The method described by Tsutsui (1988) was used to determine the FC and FS of SESPC and SOYPC. Solutions of SESPC and SOYPC were prepared at 5, 20, 30, and 45 g L 1, and pH was adjusted to 2.0, 5.0, 7.0, 8.5 and 10 with 0.01 M HCl or NaOH. The solutions were agitated in graduated plastic tubes at high speed in an Oster blender for 1 min. Foam capacity was reported as: FC % = Volume after agitation volume prior to agitation 100: Volume prior to agitation

A similar procedure was used to determine the FS, but the samples were allowed to stand for 30 min at room temperature and the residual foam volume was measured. The following formula was used to calculate FS: FS% = Residual foam volume 100: Total foam volume

2.4. Statistical analyses Response surface methodology was used to analyze the range and intervals of the experimental parameters. Data analysis and graphic plotting were done with STATISTICA software (tatsoft, 1995). Quadratic models were used to create 3-dimensional response surfaces. In response surfaces, independent variables are located along the X and Y axes, while the response variable is located along the Z axis perpendicular to the XY axes. Analysis of variance and least signicant differences were used to analyze for signicant differences at the 5% level between treatments. The Steel and Torrie (1982) method of regression analysis was used for simple regression models. 3. Results and discussion 3.1. Emulsifying capacity Fig. 1 shows the response surface interaction between pH and SESPC and SOYPC reected the interdependent effects of these two factors on emulsifying capacity (EC) at oil concentration of 550 g L 1. The maximum EC for SESPC (38.0%) was found in the range of 40 to

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Fig. 1. The emulsifying capacity (%) as affected by sample concentration and pH for a) sesame protein concentrate (SESPC) and b) commercial soybean concentrate (SOYPC) at oil concentration of 550 g L 1.

65 g L 1 protein concentrate and a pH of more than 9.0 or less than 5.0 (Fig. 1a). The lowest EC (19.2%) was found at lower SESPC concentrations and in a pH range between 4.6 and 6.8 ( b 0.05). This decrease was the result of the low solubility of the protein when its isoelectric point of 5.0 is reached (Escamilla-Silva et al., 2003). Protein solubility is known to directly affect the EC of a protein (Paredes-Lpez et al., 1994). The isoelectric point changes with the ambient ionic strength of the solution so that the potential Z tends to zero (i.e., Coulombic forces cause the molecules to be more stable and the Brownian movement facilitates the formation suspensions rather than emulsions). As shown in Fig. 1a, the SESPC concentration increased for the same pH range. The EC level also increased, supporting the previously-described theory. The response area of the interaction between the SOYPC concentration and pH shows that EC increased signicantly from 8.5% to 40.1% when pH increased ( b 0.05) (Fig. 1b). Wang and Zayas (1992) observed a similar behavior with soybean protein. However, they reported larger EC percentages (70105%) than those observed

in this research. These differences could be due to the difference in products and/or the process by which the SOYPC was obtained. Moure, Sineiro, Dominguez, and Parajo (2006) report a protein solubility of 97 mg mL 1 and 36100 mg mL 1 for sesame and soybean, respectively. These values explains the similar magnitude of EC both SESPC and SOYPC, The protein solubility exhibits a minimum value at isoelectric point, originating that surface tensions of wheat proteins were lowest. (Kinsella, 1981; Escamilla-Silva et al., 2003; Alfaro, Alvarez, Khor, & Padilla, 2004). The concentration of SOYPC affected EC less than pH. Below pH 6, the EC of the protein concentrate increased when the SOYPC concentration increased. Above pH 6, however, this effect was not as strong. This study also examined the effect of oil concentration for SESPC and SOYPC. EC increased signicantly when oil concentration increased ( b 0.05) as shown in Fig. 2 at pH 7. EC reached a maximum of 60% when SESPC concentration was more than 45 g L 1 and oil concentration was more than 500 g L 1 (Fig. 2a). SESPC concentration

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Fig. 2. The emulsifying capacity (%) as affected by sample concentration and the amount of oil (g L 1) for a) sesame protein concentrate (SESPC) and b) commercial soybean concentrate (SOYPC) at pH 7.

did not affect EC as much as the presence of oil. EC reached a maximum of 68.2% when SOYPC concentration was more than 70 g L 1 and oil concentration was more than 500 g L 1. EC decreased as oil concentration decreased (Fig. 2b). The maximum EC percentages found in this study were similar to those reported by Marcone and Kakuda (1999). They found that the EC of soybean globulins did not exceed 58%. EC values were very similar for SESPC and SOYPC at the oil concentrations and pH levels studied. Therefore, SESPC can be substituted SOYPC at an acidic pH. Table 1 shows quadratic models that present the best conditions for SESPC EC and SOYPC EC as a function of pH of the medium (P), concentration of SESPC or SOYPC (Q), and concentration of oil (S). 3.2. Emulsion stability Fig. 3 depicts the effect of pH and sample concentration on emulsion stability at oil concentration of 550 g L 1. The response

surface interaction between SESPC concentration and pH showed that ES was greater at acidic (50.6%) pH levels than at basic (44.8%) pH levels for larger SESPC concentrations (Fig. 3a). As pH approached a
Table 1 Response surface of the form Z1 = a + a1P + a2Q + a3P2 + a4PQ + a5Q2 for emulsifying capacity of SESPC and SOYPC. I Z1 Z2 I Z3 Z4 a 26.687 19.733 a 16.747 49.720 a1P 0.679 3.246 a1S 0.545 0.318 a2Q 23.397 2.999 a2Q 8.349 17.309 a3P2 0.356 0.468 a3S2 0.003 0.006 a4PQ 0.814 0.831 a4SQ 0.053 0.151 a5Q2 1.65 0.401 a5Q2 0.804 1.472 R2 0.975 0.978 R2 0.984 0.975

Z1 and Z3 the EC of SESPC and Z2 and Z4 the EC of SOYPC; P = pH of the medium; Q = the concentration of SESPC or SOYPC (%); and S = concentration of oil (%). The models were resolved using a 95% condence interval.

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Fig. 3. The emulsion stability (%) as affected by sample concentration and pH for a) sesame protein concentrate (SESPC) and b) commercial soybean concentrate (SOYPC) at oil concentration of 550 g L 1.

neutral value, the ES gradually decreased, and the lowest value of 35.6% was found at lower SESPC concentrations. The concentration of SESPC had a smaller effect on ES than pH. The response surface interaction between SOYPC concentration and pH showed that the maximum ES value (39.0%) was found at pH levels over 5 and with SOYPC concentrations of 2560 g L 1 (Fig. 3b). The ES value of SOYPC was signicantly lower than that of SESPC ( b 0.05). As pH approached a neutral value, the ES dropped for the entire concentration range of SOYPC studied. At SOYPC concentrations less than 30 g L 1 and more than 65 g L 1, the ES values were under 15.5% for the 5.5 to 9.0 pH range (Fig. 3b). In general, the ES of SESPC was greater than that of SOYPC for the entire pH and concentration range studied. Fig. 4 depicts the effect of sample concentration and oil concentration on emulsion stability at pH 7. The effect of the interaction between SESPC concentration and oil concentration showed that ES was not affected signicantly by the SESPC concentration (Fig. 4a). The minimum ES value was found with an oil concentration ranging from 150 to 350 g L 1; ES increased when the oil concentration increased or

decreased. The largest ES value (96%) was obtained at SESPC concentrations of more than 55 g L 1 and less than 530 g L 1 oil. The ES of SOYPC was less stable than that of SESPC. The maximum ES value (56%) occurred at an oil concentration of approximately 550 g L 1 and at a SOYPC concentration of less than 55 g L 1 (Fig. 4b). The maximum ES value of SOYPC (56%) was signicantly lower than that of SESPC (96%) ( b 0.05). The SOYPC also reached much lower ES values (8.4%) than the SESPC for oil concentrations between 150 and 400 g L 1 and at SOYPC concentrations b 27 g L 1 or N 60 g L 1. In all interactions, SOYPC had lower ES values than SESPC; these results are similar to those reported by Konishi and Yoshimoto (1987). These authors found that the ES of amaranth proteins were almost double that of soybean proteins, especially at basic and acidic pH levels. Marcone and Kakuda (1999) found that even in the region of the isoelectric point, amaranth globulins showed greater EC and ES than soybean globulins. SESPC behavior at acidic and basic pH levels could reect the presence of hydrophobic residues and the denaturalization or partial unfolding of the globular protein caused by the change in pH(Sze-Tao

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Fig. 4. The emulsion stability (%) as affected by sample concentration and the amount of oil (g L 1) for a) sesame protein concentrate (SESPC) and b) commercial soybean concentrate (SOYPC) at pH 7.

& Sathe, 2000). This process exposes a greater hydrophobic surface that gives greater mobility at the interface and improves the penetration of the aqueous phase to the native structure (Konishi & Yoshimoto, 1987; Pandya et al., 2000; Schwenke, 2001; Deng et al., 2011). Table 2 shows quadratic models expressing the best conditions for the ES of SESPC and SOYPC as a function of P, Q and S. 3.3. Foaming capacity The response surface showed that both the SESPC concentration and the pH signicantly affected FC (Fig. 5a). As the SESPC concentration increased and the pH decreased, the FC increased. The maximum FC value observed for SESPC was 240% at a pH less than 5 and SESPC concentrations more than 40 g L 1. This FC level was 2.5times greater ( b 0.05) than the maximum value found for SOYPC (Fig. 5b). The maximum FC level of the SOYPC was around 92% at a pH near to 10 and a protein concentrate levels above 40 g L 1 (Fig. 5b). The FC levels of SOYPC were lower than those of SESPC over the pH

range and concentration tested for. As the pH decreased towards the isoelectric point for SOYPC, the FC also decreased more accentuated when the SOYPC concentration increased. The same tendency was observed at low SOYPC concentrations and basic pH. The SESPC
Table 2 Response surface of the form Z1 = a + a1P + a2Q + a3P2 + a4PQ + a5Q2 for emulsion stability of SESPC and SOYPC in function of P, Q and Z. I Z7 Z8 I Z9 Z10 a 124.736 125.990 a 90.634 12.401 a1P 25.713 38.683 a1S 4.333 1.592 a2Q 2.072 16.203 a2Q 7.571 20.1148 a3P2 1.724 2.467 a3S2 0.076 0.043 a4PQ 0.046 0.543 a4SQ 0.069 0.0941 a5Q2 0.155 2.145 a5Q2 0.726 1.825 R2 0.981 0.9920.992 R2 0.963 0.975

Z7 and Z9 the ES of SESPC and Z8 and Z10 the ES of SOYPC; P = pH of the medium; Q = the concentration of SESPC or SOYPC (%); and S = concentration of oil (%). The models were resolved using a 95% condence interval.

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Fig. 5. The foaming capacity (%) as affected by sample concentration and pH for a) sesame protein concentrate (SESPC) and b) commercial soybean concentrate (SOYPC).

obtained by the simplied method has characteristics that could be of great industrial interest. The best conditions for FC of SESPC and SOYPC in function of P and Q as expressed with quadratic models are presented in the Table 3. 3.4. Foam stability The response surface interaction between SESPC concentration and pH showed that both affected FS (Fig. 6a). FS increased when SESPC concentration increased and pH decreased. The minimum FS value (50.4%) was obtained at a pH above 7.6 and a SESPC concentration of less than 10 g L 1. The maximum FS of SESPC (94%) was obtained at SESPC concentrations of more than 42 g L 1 and pH values under 2.5. The FS of SOYPC increased to a maximum of 110% at SOYPC concentrations below 24 g L 1 and in a pH range of 3.57.6. At a pH above 7.6, the FS of SOYPC decreased (Fig. 6b). The highest FS of SESPC (110%) was signicantly greater than the maximum FS for SOYPC (94%) ( b 0.05) (Fig. 6). SOYPC also showed much lower FS values (15.6%) ( b 0.05) than SESPC, especially below pH 3.0 and at a SOYPC concentration of more than 32 g L 1.

Table 4 shows quadratic models expressing the best conditions for the FS of SESPC and SOYPC as a function of P and Q. A greater amount of SESPC than SOYPC was required to obtain similar FS levels. However, SESPC can be used under a wider range of pH conditions than SOYPC; this characteristic makes SESPC more versatile. It would be worthwhile to study the behavior of SESPC at concentrations of more than 45 g L 1, as the response surface showed a tendency of concentration to increase the FS. It was found that the FS of SESPC was directly related to its FC; when FS increased so did FC

Table 3 Response surface of the form Z1 = a + a1P + a2Q + a3P2 + a4PQ + a5Q2 for foaming capacity of SESPC and SOYPC in function of P, Q and Z. I Z11 Z12 a 142.034 83.266 a1P 4.387 6.736 a2Q 13.842 13.075 a3P2 0.797 0.015 a4PQ 0.705 2.717 a5Q2 2.063 0.291 R2 0.989 0.992

Z11 the FC of SESPC and Z12 the FC of SOYPC; P = pH of the medium; Q = the concentration of SESPC or SOYPC (%). The models were resolved using a 95% condence interval.

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Fig. 6. The foaming stability (%) as affected by sample concentration and pH for a) sesame protein concentrate (SESPC) and b) commercial soybean concentrate (SOYPC).

(Figs. 5a and 6a). This tendency did not occur with SOYPC (Figs. 5b and 6b). The FC and FS of SESPC increased when its concentration increased at a lower pH. These results are different from those reported by Aoki et al. (1999). They reported that the FC of ovalbumin tended to decrease when the isoelectric point was reached. In our study, protein solubility tended to decrease when the isoelectric point was reached; this protein solubility in turn affected the FC of the protein. Protein solubility reached its lowest value (Escamilla-Silva et al., 2003) when
Table 4 Response surface of the form Z1 = a + a1P + a2Q + a3P2 + a4PQ + a5Q2 for foam stability of SESPC and SOYPC in function of P, Q and Z. I Z13 Z14 a 119.9 34.931 a1P 13.025 25.039 a2Q 6.180 0.854 a3P2 0.625 2.173 a4PQ 0.93 1.357 a5Q2 1.25 4.268 R2 0.973 0.985

the pH of SESPC reached its isoelectric pH (5.0); FC and FS, however, increased at this point (Figs. 5a and 6a). The FC of SESPC showed the same behavior reported by Aoki et al. (1999). It decreased when the pH reached its isoelectric point (Fig. 5b). Nevertheless, the FS of SOYPC increased as the pH increased. This nding contradicts the results reported by Matsudomi, Sasaki, Kato, and Kobayashi (1985). They reported that the FC of SOYPC increased when the pH decreased. 4. Conclusions The high EC found as function of protein concentration and oil concentration at basic pH levels could indicate SESPC and SOYPC globulin content (75.8% and 90%, respectively, Escamilla-Silva et al., 2003). This was in agreement with the general correlation between emulsion properties and protein solubility (Marcone & Kakuda, 1999; Deng et al., 2011) It has been reported that soy globulins show larger EC properties at basic pH levels than at acidic levels (Gueguen & Cerletti, 1994). One possible explanation for the increase in FC and FS

Z13 the FS of SESPC and Z14 the FS of SOYPC; P = pH of the medium; Q = the concentration of SESPC or SOYPC (%). The models were resolved using a 95% condence interval.

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of SESPC as pH decreased because the net charge is near minimum in the isoelectric region that induces to protein might have aggregated and destabilized the interfacial membrane (Inyang & Iduh, 1996). This reduced stability is why we are currently seeking to modify proteins to improve foam stability. In addition, some nutritional products require proteins that generate foam; increased form stability could allow for additional uses of the sesame protein (Moure et al., 2006). The presence of phytic acid in SESPC is also important; at certain concentrations phytic acid could affect the functional properties studied in this work (Rahama, Duek, Mothes, Gornitz, & Schwenke, 2000). The simplied process used in the production of SESPC did not affect the functional properties studied. These properties (e.g., ES) were often similar or superior to those of SOYPC. In addition, SESPC may ultimately be more versatile; at the extreme pH levels found in a variety of food and/or industrial products, SESPC showed important EC, ES, FC and FS characteristics. Acknowledgements We thank A. Williams for revising the English of the manuscript. This research was funded by Consejo del Sistema Nacional de Educacin Tecnolgica (COSNET) grants 581.01-PA and 290.90. References
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