Optimization of processing time, amplitude and concentration for ultrasound-assisted modification of whey protein using response surface methodology
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Response surface methodology was used to optimize processing variable for ultrasound-assisted modification of whey protein. The process was optimized employing Box–Behnken Design with three independent variables i.e. amplitude (20–40%), time (10–20 min) and concentration (10–15%). A second order model was employed to generate response surfaces. Experimental results revealed that analyzed model solutions exhibited the significant influence on various responses signified that the applied statistical model fitted well. The optimized independent variables were found to be 19.77 min time, 20.02% amplitude and 12.78% concentration of feed. The modified whey protein had the solubility, 78.52%; heat stability, 1076.19 s; water solubility index, 92.30%; water holding capacity, 0.469; oil absorption capacity, 1.709; foaming capacity 92.27; foam stability, 27.71 and firmness, 1692.09 g. Analytical response revealed that solubility of modified whey protein exhibited significant positive correlation with water solubility index, emulsion stability index and firmness.
KeywordsUltrasound Whey protein Modification Solubility Response surface methodology
Authors are highly thankful to Department of Food Science and Technology, Punjab Agricultural University, Ludhiana for providing research oriented environment and great opportunity for successful completion of this work.
- Kentish S, Ashokkumar M (2011) The physical and chemical effects of ultrasound BT—ultrasound technologies for food and bioprocessing. In: Feng H, Barbosa-Canovas G, Weiss J (eds) Ultrasound technologies for food and bioprocessing. Springer, New York, p 1–12Google Scholar
- Kinsella JE, Rector DJ, Phillips LG (1994) Physicochemical properties of proteins: texturization via gelation, glass and film formation BT—protein structure-function relationships in foods. In: Yada RY, Jackman RL, Smith JL (eds) Protein structure–functional relationships in foods. Springer, Boston, p 1–21Google Scholar
- Liu Z, Guo B, Su M, Wang Y (2012) Effect of ultrasonic treatment on the functional properties of whey protein isolates. Adv Mat Res 443–444:660–665. https://doi.org/10.4028/www.scientific.net/AMR.443-444.660 Google Scholar
- Onwulata C, Tomasula P (2004) Whey texturization: a way forward. Food Technol 58:50–54Google Scholar
- Thakur R, Saberi B, Pristijono P, Stathopoulos CE, Golding JB, Scarlett CJ, Bowyer M, Vuong QV (2017) Use of response surface methodology (RSM) to optimize pea starch–chitosan novel edible film formulation. J Food Sci Technol 54:2270–2278. https://doi.org/10.1007/s13197-017-2664-y CrossRefGoogle Scholar
- Turgeon SL, Gauthier SF, Paquin P (1992) Emulsifying property of whey peptide fractions as a function of pH and ionic strength. J Food Sci 57:601–604. https://doi.org/10.1111/j.1365-2621.1992.tb08052.x CrossRefGoogle Scholar
- Zayas JF (1997a) Emulsifying properties of proteins BT—functionality of proteins in food. In: Zayas JF (ed) Functionality of protein in food. Springer, Berlin, Heidelberg, p 134–227Google Scholar
- Zayas JF (1997b) Solubility of proteins BT—functionality of proteins in food. In: Zayas JF (ed) Functionality of protein in food. Springer, Berlin, p 6–75Google Scholar