Research Article
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Year 2022, , 284 - 289, 01.10.2022

Menekşe Bulut

https://doi.org/10.3153/FH22026

Abstract

References

  • Arzeni, C., Martinez, K., Zema, P., Arias, A., Perez, O.E., Pilosof, A.M.R. (2012). Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering, 108, 463-472. https://doi.org/10.1016/j.jfoodeng.2011.08.018
  • Bradford, M.M. (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. https://doi.org/10.1016/0003-2697(76)90527-3
  • Chang, K., Liu, J., Jiang, W., Fan, Y., Nan, B., Ma, S., ..., Zhang, T. (2021). Structural characteristics and foaming properties of ovalbumin-Caffeic acid complex. LWT, 146, 111383. https://doi.org/10.1016/j.lwt.2021.111383
  • Ghasemi, S., Jafari, S.M., Assadpour, E., Khomeiri, M. (2018). Nanoencapsulation of d-limonene within nanocarriers produced by pectin-whey protein complexes. Food Hydrocolloids, 77, 152-162. https://doi.org/10.1016/j.foodhyd.2017.09.030
  • Hu, H., Li-Chen, E.C.Y., Wan, L., Tian, M., Pan, S. (2003). The effect of high intensity ultrasonic pretreatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids, 32(2), 303–311. https://doi.org/10.1016/j.foodhyd.2013.01.016
  • Hussain, R., Gaiani, C., Jeandel, C., Ghanbaja, J., Scher, J. (2012). Combined effect of heat treatment and ionic strength on the functionality of whey proteins. Journal of Dairy Science, 95, 6260-6273. https://doi.org/10.3168/jds.2012-5416
  • Feng, Y., Wang, J., Hu, H., Yang, C. (2022). Effect of oxidative modification by reactive oxygen species (ROS) on the aggregation of whey protein concentrate (WPC). Food Hydrocolloids,123,10718. https://doi.org/10.1016/j.foodhyd.2021.107189
  • Jambrak, A.R., Mason, T.M., Lelas, V., Herceg, Z., Herceg, I.L. (2008). Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. Journal of Food Engineering, 86, 281-287. https://doi.org/10.1016/j.jfoodeng.2007.10.004
  • Jambrak, A.R., Mason, T.J., Lelas, V., Paniwnyk, L., Herceg, Z. (2014). Effect of ultrasound treatment on particle size and molecular weight of whey proteins. Journal of Food Engineering, 121, 15-23. https://doi.org/10.1016/j.jfoodeng.2013.08.012
  • Jiang, S., Ding, J., Andrade, J., Rababah, T.M., Almajval, 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. https://doi.org/10.1016/j.ultsonch.2017.03.046
  • Krešić, G., Lelas, V., Jambrak, A. R., Herceg, Z., Brnčić, S. R. (2008). Influence of novel food processing technologies on the rheological and thermophysical properties of whey proteins. Journal of Food Engineering, 87(1), 64-73. https://doi.org/10.1016/j.jfoodeng.2007.10.024
  • Kumar, R., Chauhan, S.K., Shinde, G., Subramanian, V., Nadanasabapathi, S. (2018). Whey Proteins: A potential ingredient for food industry- A review. Asian Journal of Dairy and Food Research, 37, 283-290. https://doi.org/10.18805/ajdfr.DR-1389
  • Lee, H., Yildiz, G., Dos Santos, L.C., Jiang, S., Andrade, J., Engeseth, N.C., Feng, H. (2016). Soy protein nano-aggregates with improved functional properties prepared by sequential pH treatment and ultrasonication. Food Hydrocolloids, 55, 200-209. https://doi.org/10.1016/j.foodhyd.2015.11.022
  • Liu, Q., Li, J., Kong, B. H., Li, P.J., Xia, X.F. (2014). Physicochemical and antioxidant properties of Maillard reaction products formed by heating whey protein isolate and reducing sugars. International Journal of Dairy Technology, 67, 220-228. https://doi.org/10.1111/1471-0307.12110
  • Martini, S., Potter, R., Walsh, M.K. (2010). Optimizing the use of power ultrasound to decrease turbidity in whey protein suspensions. Food Research International, 43, 2444-2451. https://doi.org/10.1016/j.foodres.2010.09.018
  • Mason, T.J., Paniwnyk, L., Lorimer, J.P. (1996). The uses of ultrasound in food technology. Ultrasonics Sonochemistry, 3, 253–260. https://doi.org/10.1016/S1350-4177(96)00034-X
  • Morr, C.V., Ha, E.Y.W. (1993). Whey protein concentrates and isolates: processing and functional properties. Critical Reviews in Food Science and Nutrition, 33, 431-476. https://doi.org/10.1080/10408399309527643
  • Yildiz, G., Andrade, J., Engeseth, N.C., & Feng, H. (2017). Functionalizing soy protein Nan- aggregates with pH-shifting and mano-thermo-sonication. Journal of Colloid and Interface Science, 505, 836-846. https://doi.org/10.1016/j.jcis.2017.06.088
  • Yıldız, G. (2018). Physicochemical properties of soy protein concentrate treated with ultrasound at various amplitudes. Journal of the Institute of Science and Technology, 8(4), 133-139. https://doi.org/10.21597/jist.436852
  • Zisu, B., Lee, J., Chandrapala, J., Bhaskaracharya, R., Palmer, M., Kentish, S., Ashokkumar, M. (2011). Effect of ultrasound on the physical and functional properties of reconstituted whey protein powders. Journal of Dairy Research, 78, 226-232. https://doi.org/10.1017/S0022029911000070

The effect of ultrasound times and amplitudes on the solubility and turbidity of whey protein concentrate

Year 2022, , 284 - 289, 01.10.2022

Menekşe Bulut

https://doi.org/10.3153/FH22026

Abstract

The current work was conducted to explore the influence of ultrasound times and amplitudes on the solubility and turbidity of whey protein concentrate (WPC). Ultrasound (US) application was employed using VC-750 ultrasonic power equipment with the frequency of 20 kHz at various times (10, 20, and 30 minutes at 50% amplitude) and amplitudes (60%, 80%, and 100% for 5 min). The outcomes exhibited that the US process have a significant impact on both solubility and turbidity (p<0.05). The highest protein recovery was obtained for the samples exposed to 30 min the US at 100% amplitude (65.56%). WPC samples treated at 100% amplitude showed higher solubility compared to the other samples at 60% and 80% amplitudes. While the solubility of WPC samples treated with 10 min showed the lowest solubility (9.13%), samples treated with 30 min showed the highest solubility (38.14%). There is a negative relationship between solubility and turbidity. All US-treated samples showed less turbidity and higher solubility where the control WPC samples showed the most turbid structure (0.88 NTU) with the lowest solubility (4.15%). Overall, US treatment with 30-minutes at 100 % amplitude showed the highest solubility (65.56%) and least turbidity (0.26 NTU) compared to the other sonication times and amplitudes. 

Keywords

Ultrasound Amplitude Protein solubility Turbidity Whey protein concentrate.

References

  • Arzeni, C., Martinez, K., Zema, P., Arias, A., Perez, O.E., Pilosof, A.M.R. (2012). Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering, 108, 463-472. https://doi.org/10.1016/j.jfoodeng.2011.08.018
  • Bradford, M.M. (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. https://doi.org/10.1016/0003-2697(76)90527-3
  • Chang, K., Liu, J., Jiang, W., Fan, Y., Nan, B., Ma, S., ..., Zhang, T. (2021). Structural characteristics and foaming properties of ovalbumin-Caffeic acid complex. LWT, 146, 111383. https://doi.org/10.1016/j.lwt.2021.111383
  • Ghasemi, S., Jafari, S.M., Assadpour, E., Khomeiri, M. (2018). Nanoencapsulation of d-limonene within nanocarriers produced by pectin-whey protein complexes. Food Hydrocolloids, 77, 152-162. https://doi.org/10.1016/j.foodhyd.2017.09.030
  • Hu, H., Li-Chen, E.C.Y., Wan, L., Tian, M., Pan, S. (2003). The effect of high intensity ultrasonic pretreatment on the properties of soybean protein isolate gel induced by calcium sulfate. Food Hydrocolloids, 32(2), 303–311. https://doi.org/10.1016/j.foodhyd.2013.01.016
  • Hussain, R., Gaiani, C., Jeandel, C., Ghanbaja, J., Scher, J. (2012). Combined effect of heat treatment and ionic strength on the functionality of whey proteins. Journal of Dairy Science, 95, 6260-6273. https://doi.org/10.3168/jds.2012-5416
  • Feng, Y., Wang, J., Hu, H., Yang, C. (2022). Effect of oxidative modification by reactive oxygen species (ROS) on the aggregation of whey protein concentrate (WPC). Food Hydrocolloids,123,10718. https://doi.org/10.1016/j.foodhyd.2021.107189
  • Jambrak, A.R., Mason, T.M., Lelas, V., Herceg, Z., Herceg, I.L. (2008). Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. Journal of Food Engineering, 86, 281-287. https://doi.org/10.1016/j.jfoodeng.2007.10.004
  • Jambrak, A.R., Mason, T.J., Lelas, V., Paniwnyk, L., Herceg, Z. (2014). Effect of ultrasound treatment on particle size and molecular weight of whey proteins. Journal of Food Engineering, 121, 15-23. https://doi.org/10.1016/j.jfoodeng.2013.08.012
  • Jiang, S., Ding, J., Andrade, J., Rababah, T.M., Almajval, 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. https://doi.org/10.1016/j.ultsonch.2017.03.046
  • Krešić, G., Lelas, V., Jambrak, A. R., Herceg, Z., Brnčić, S. R. (2008). Influence of novel food processing technologies on the rheological and thermophysical properties of whey proteins. Journal of Food Engineering, 87(1), 64-73. https://doi.org/10.1016/j.jfoodeng.2007.10.024
  • Kumar, R., Chauhan, S.K., Shinde, G., Subramanian, V., Nadanasabapathi, S. (2018). Whey Proteins: A potential ingredient for food industry- A review. Asian Journal of Dairy and Food Research, 37, 283-290. https://doi.org/10.18805/ajdfr.DR-1389
  • Lee, H., Yildiz, G., Dos Santos, L.C., Jiang, S., Andrade, J., Engeseth, N.C., Feng, H. (2016). Soy protein nano-aggregates with improved functional properties prepared by sequential pH treatment and ultrasonication. Food Hydrocolloids, 55, 200-209. https://doi.org/10.1016/j.foodhyd.2015.11.022
  • Liu, Q., Li, J., Kong, B. H., Li, P.J., Xia, X.F. (2014). Physicochemical and antioxidant properties of Maillard reaction products formed by heating whey protein isolate and reducing sugars. International Journal of Dairy Technology, 67, 220-228. https://doi.org/10.1111/1471-0307.12110
  • Martini, S., Potter, R., Walsh, M.K. (2010). Optimizing the use of power ultrasound to decrease turbidity in whey protein suspensions. Food Research International, 43, 2444-2451. https://doi.org/10.1016/j.foodres.2010.09.018
  • Mason, T.J., Paniwnyk, L., Lorimer, J.P. (1996). The uses of ultrasound in food technology. Ultrasonics Sonochemistry, 3, 253–260. https://doi.org/10.1016/S1350-4177(96)00034-X
  • Morr, C.V., Ha, E.Y.W. (1993). Whey protein concentrates and isolates: processing and functional properties. Critical Reviews in Food Science and Nutrition, 33, 431-476. https://doi.org/10.1080/10408399309527643
  • Yildiz, G., Andrade, J., Engeseth, N.C., & Feng, H. (2017). Functionalizing soy protein Nan- aggregates with pH-shifting and mano-thermo-sonication. Journal of Colloid and Interface Science, 505, 836-846. https://doi.org/10.1016/j.jcis.2017.06.088
  • Yıldız, G. (2018). Physicochemical properties of soy protein concentrate treated with ultrasound at various amplitudes. Journal of the Institute of Science and Technology, 8(4), 133-139. https://doi.org/10.21597/jist.436852
  • Zisu, B., Lee, J., Chandrapala, J., Bhaskaracharya, R., Palmer, M., Kentish, S., Ashokkumar, M. (2011). Effect of ultrasound on the physical and functional properties of reconstituted whey protein powders. Journal of Dairy Research, 78, 226-232. https://doi.org/10.1017/S0022029911000070
There are 20 citations in total.

Details

Primary Language English
Subjects Food Engineering
Journal Section Research Articles
Authors

Menekşe Bulut 0000-0003-3902-6403

Publication Date October 1, 2022
Submission Date November 14, 2021
Published in Issue Year 2022

Cite

APA Bulut, M. (2022). The effect of ultrasound times and amplitudes on the solubility and turbidity of whey protein concentrate. Food and Health, 8(4), 284-289. https://doi.org/10.3153/FH22026

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