Öz
This research was conducted to investigate the influence of ultrasound amplitude on the
physicochemical properties of soy protein concentrate. Soy protein concentrates (SPC, Acron SM) were treated
with a frequency of 20 kHz ultrasound and three different amplitudes of 50, 80, and 100% for 5 min. Untreated and
ultrasound-treated soy protein concentrate samples were evaluated in terms of recovery of soluble protein, particle
size, surface hydrophobicity, free sulfhydryl groups, turbidity and microstructure. The environmental scanning
electron microscope images of the treated and untreated soy protein concentrate samples were taken in order to
analyze the microstructure of the samples. The findings showed that the ultrasound treatment have a significant
effect on all physicochemical characteristics (p<0.05). All ultrasound treated samples showed significantly higher
solubility compared to the untreated soy protein concentrates. In addition, the highest protein solubility was
determined for the samples treated with 100% amplitude. Ultrasound treatment reduced the size of all proteins.
The sample which has the highest solubility also showed the lowest particle size compared to the others. Moreover,
ultrasound treated (100% amplitude) soy protein concentrate was resulted with highest surface hydrophobicity and
free sulfhydryl groups. Microscope images of the soy protein concentrates showed a spherical morphology with
particle diameters which closely corresponding to the results obtained by dynamic light scattering. It was clearly
seen that increasing ultrasound amplitude enhance the functionality of soy protein concentrates.
Anahtar Kelimeler
Ultrasound amplitude soy protein concentrate particle size protein solubility surface hydrophobicity free sulfhydryl group
Kaynakça
- Adachi M, Kanamori J, Masuda T, 2003. Crystal structure of soybean 11S globulin: Glycinin A3B4 homotrimer. Proceedings of the National Academy of Sciences USA, 100: 7395–7400.
- Arzeni C, Martinez K, Zema P, Arias A, Perez OE, Pilosof AMR, 2012. Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering, 108 (3): 463–472.
- Bradford MM, 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72: 248–254.
- Campbell MF, Kraut CW, Yackel WC, Yang HS, 1985. Soy Protein Concentrate, in New Protein Foods. Altschul and Wilke Eds. Vol. 5, p 301.
- Gregory J, 1998. Turbidity and beyond. Filtration & Separation. 35 (1): 63–67.
- Howard PA, Campbell MF, and Zollinger DT, 1980. U.S. Patent 4,234,620.
- Hu H, Li-Chen ECY, Wan L, Tian M, Pan S, 2003. The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids, 32 (2): 303–311.
- Jambrak AR, Mason TM, Lelas V, Herceg Z, Herceg IL, 2008. Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. Journal of Food Engineering, 86: 281–287
- Jambrak AR, Lelas V, Mason TJ, Kresic G, Badanjak M, 2009. Physical properties of ultrasound treated soy proteins. Journal of Food Engineering, 93 (4): 386–393.
- Jiang J, Xiong YL, Chen J, 2011. Role of ß-conglycinin and glycinin subunits in the pH-shifting-induced structural and physicochemical changes of soy protein isolate. Journal of Food Science, 76 (2): 293–302.
- Jiang S, Ding J, Andrade J, Rababah TM, Almajwal A, Abulmeaty M.M, Feng H, 2017. Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrasonics Sonochemistry, 38: 835–842.
- Karki B, Lamsal BP, Jung S, van Leeuwen J, Pometto AL, Grewell D, Khanal SK, 2010. Enhancing protein and sugar release from defatted soy flakes using ultrasound technology. Journal of Food Engineering, 96 (2): 270–278.
- Kinsella JE, 1979. Functional properties of soy proteins. Journal of the American Oil Chemists’ Society, 56: 242–258.
- Lee H, Yildiz G, Dos Santos LC, Jiang S, Andrade J, Engeseth NC, Feng H, 2016. Soy protein nano-aggregates with improved functional properties prepared by sequential pH treatment and ultrasonication. Food Hydrocolloids, 55: 200–209.
- Liu K, 1997. Chemical composition of seed. In: Liu K (ed.) Soybean, Chemistry, Technology, and Utilization, New York, NY: Chapman and Hall.
- Mason TJ, Paniwnyk L, Lorimer JP, 1996. The uses of ultrasound in food technology. Ultrasonics Sonochemistry, 3: 253–260.
- Molina E, Papadopoulou A, Ledward DA, 2001. Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins. Food Hydrocolloids, 15: 263–269
- Moore SL, Yang HS, and Yackel WC, 1980. In Proc. Eur. Meet. Meat Res. 26th, 1980, p. 325.
- Moreira MA, Hermodson MA, Larkins BA, and Nielsen NC, 1979. Partial characterization of the acidic and basic polypeptides of glycinin. Journal of Biological Chemistry, 10: 9921–9926.
- Palazolo GG, Sorgentini DA, Wagner JR, 2005. Coalescence and flocculation in o/w emulsions of native and denatured whey proteins in comparison with soy protein isolates. Food Hydrocolloids, 19: 595–604
- Puppo MC, Speroni F, Chapleau N, De Lamballerie-Anton M, Anon MC, Anton M, 2005. Effect of high-pressure treatment on emulsifying properties of soybean proteins. Food Hydrocolloids, 19: 289–296
- Santiago LG, Gonzalez RJ, Remondetto GE, Bonaldo AG, 1998. Emulsifying ability of proteins evaluated by response surface methodology. Lebensmittel-Wissenshaft und- Technologie, 31: 259–264
- Yildiz G, Andrade J, Engeseth NJ, Feng H, 2017. Functionalizing soy protein nano-aggregates with pH-shifting and mano-thermo-sonication. Journal of Colloid and Interface Science, 505: 836-846.
Öz
This research was conducted to investigate the influence of ultrasound amplitude on the
physicochemical properties of soy protein concentrate. Soy protein concentrates (SPC, Acron SM) were treated
with a frequency of 20 kHz ultrasound and three different amplitudes of 50, 80, and 100% for 5 min. Untreated and
ultrasound-treated soy protein concentrate samples were evaluated in terms of recovery of soluble protein, particle
size, surface hydrophobicity, free sulfhydryl groups, turbidity and microstructure. The environmental scanning
electron microscope images of the treated and untreated soy protein concentrate samples were taken in order to
analyze the microstructure of the samples. The findings showed that the ultrasound treatment have a significant
effect on all physicochemical characteristics (p<0.05). All ultrasound treated samples showed significantly higher
solubility compared to the untreated soy protein concentrates. In addition, the highest protein solubility was
determined for the samples treated with 100% amplitude. Ultrasound treatment reduced the size of all proteins.
The sample which has the highest solubility also showed the lowest particle size compared to the others. Moreover,
ultrasound treated (100% amplitude) soy protein concentrate was resulted with highest surface hydrophobicity and
free sulfhydryl groups. Microscope images of the soy protein concentrates showed a spherical morphology with
particle diameters which closely corresponding to the results obtained by dynamic light scattering. It was clearly
seen that increasing ultrasound amplitude enhance the functionality of soy protein concentrates.
Anahtar Kelimeler
Ultrasound amplitude soy protein concentrate particle size protein solubility surface hydrophobicity free sulfhydryl group
Kaynakça
- Adachi M, Kanamori J, Masuda T, 2003. Crystal structure of soybean 11S globulin: Glycinin A3B4 homotrimer. Proceedings of the National Academy of Sciences USA, 100: 7395–7400.
- Arzeni C, Martinez K, Zema P, Arias A, Perez OE, Pilosof AMR, 2012. Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering, 108 (3): 463–472.
- Bradford MM, 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72: 248–254.
- Campbell MF, Kraut CW, Yackel WC, Yang HS, 1985. Soy Protein Concentrate, in New Protein Foods. Altschul and Wilke Eds. Vol. 5, p 301.
- Gregory J, 1998. Turbidity and beyond. Filtration & Separation. 35 (1): 63–67.
- Howard PA, Campbell MF, and Zollinger DT, 1980. U.S. Patent 4,234,620.
- Hu H, Li-Chen ECY, Wan L, Tian M, Pan S, 2003. The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids, 32 (2): 303–311.
- Jambrak AR, Mason TM, Lelas V, Herceg Z, Herceg IL, 2008. Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. Journal of Food Engineering, 86: 281–287
- Jambrak AR, Lelas V, Mason TJ, Kresic G, Badanjak M, 2009. Physical properties of ultrasound treated soy proteins. Journal of Food Engineering, 93 (4): 386–393.
- Jiang J, Xiong YL, Chen J, 2011. Role of ß-conglycinin and glycinin subunits in the pH-shifting-induced structural and physicochemical changes of soy protein isolate. Journal of Food Science, 76 (2): 293–302.
- Jiang S, Ding J, Andrade J, Rababah TM, Almajwal A, Abulmeaty M.M, Feng H, 2017. Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrasonics Sonochemistry, 38: 835–842.
- Karki B, Lamsal BP, Jung S, van Leeuwen J, Pometto AL, Grewell D, Khanal SK, 2010. Enhancing protein and sugar release from defatted soy flakes using ultrasound technology. Journal of Food Engineering, 96 (2): 270–278.
- Kinsella JE, 1979. Functional properties of soy proteins. Journal of the American Oil Chemists’ Society, 56: 242–258.
- Lee H, Yildiz G, Dos Santos LC, Jiang S, Andrade J, Engeseth NC, Feng H, 2016. Soy protein nano-aggregates with improved functional properties prepared by sequential pH treatment and ultrasonication. Food Hydrocolloids, 55: 200–209.
- Liu K, 1997. Chemical composition of seed. In: Liu K (ed.) Soybean, Chemistry, Technology, and Utilization, New York, NY: Chapman and Hall.
- Mason TJ, Paniwnyk L, Lorimer JP, 1996. The uses of ultrasound in food technology. Ultrasonics Sonochemistry, 3: 253–260.
- Molina E, Papadopoulou A, Ledward DA, 2001. Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins. Food Hydrocolloids, 15: 263–269
- Moore SL, Yang HS, and Yackel WC, 1980. In Proc. Eur. Meet. Meat Res. 26th, 1980, p. 325.
- Moreira MA, Hermodson MA, Larkins BA, and Nielsen NC, 1979. Partial characterization of the acidic and basic polypeptides of glycinin. Journal of Biological Chemistry, 10: 9921–9926.
- Palazolo GG, Sorgentini DA, Wagner JR, 2005. Coalescence and flocculation in o/w emulsions of native and denatured whey proteins in comparison with soy protein isolates. Food Hydrocolloids, 19: 595–604
- Puppo MC, Speroni F, Chapleau N, De Lamballerie-Anton M, Anon MC, Anton M, 2005. Effect of high-pressure treatment on emulsifying properties of soybean proteins. Food Hydrocolloids, 19: 289–296
- Santiago LG, Gonzalez RJ, Remondetto GE, Bonaldo AG, 1998. Emulsifying ability of proteins evaluated by response surface methodology. Lebensmittel-Wissenshaft und- Technologie, 31: 259–264
- Yildiz G, Andrade J, Engeseth NJ, Feng H, 2017. Functionalizing soy protein nano-aggregates with pH-shifting and mano-thermo-sonication. Journal of Colloid and Interface Science, 505: 836-846.
Ayrıntılar
| Birincil Dil | İngilizce |
|---|---|
| Konular | Gıda Mühendisliği |
| Bölüm | Gıda Mühendisliği / Food Engineering |
| Yazarlar | |
| Yayımlanma Tarihi | 30 Aralık 2018 |
| Gönderilme Tarihi | 25 Haziran 2018 |
| Kabul Tarihi | 27 Temmuz 2018 |
| Yayımlandığı Sayı | Yıl 2018 Cilt: 8 Sayı: 4 |