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Elucidation of the effect of static and stirring heating conditions on the fibrillation of native whey proteins.

G. Rathod



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Elucidation of the effect of static and stirring heating conditions on the fibrillation of native whey proteins.
G. Rathod*, J. Amamcharla. Kansas State University Manhattan, KS.

Whey proteins (WP) got considerable attention due to their compatibility for structural modification. Conversion of globular WP to fibrils can impart novel functional properties. Several researchers have prepared fibrils by heating (75—120�C) acidified WP solutions up to 20 h in static condition and reported that 80�C for 20h as an optimum condition for fibrillation of WP. However, longer heating times can limit the practical utility and commercial scale-up. The study was aimed to compare the native WP (nWP) fibrils produced under static heating (STH) and stirring heating (SRH) conditions in terms of apparent viscosity (AP), Thioflavin T fluorescence (ThT), particle size, and fibril morphology. The protein solution (2% wt/wt) was prepared by mixing nWP in distilled water, adjusted the pH 2, and heated in a water bath at 80 � 0.5�C for up to 20 h. For STH, the nWP solution was kept undisturbed during heating while SRH was stirred using magnetic stirring at 40 rpm during heating. A representative sample was collected every hour from 2 h to 20 h and cooled immediately. The experiment was conducted in duplicate. The ThT analysis showed a steady increase in both the heating methods. At 10 h, STH produced 278 � 39 AU while SRH produced 418 � 41 AU indicating a higher degree of fibrillation with SRH. All the fibril-containing samples showed a shear thinning behavior. The AP also increased as the fibrillation proceeded during heating under both the conditions. The AP at a shear rate 120 s−1 was found to be 2.8 � 0.7 and 4.4 � 0.1 mPaS at 10h for STH and SRH, respectively. The heating type did not significantly (P < 0.05) influence the particle size during fibrillation process. It can be confirmed the growth of nWP fibrils during heating from the transmission electron micrographs. Higher degree of aggregation of fibrils was observed for STH compared with SRH method. In conclusion, heating under constant stirring potentially reduce the time required to produce matured nWP fibrils.

Keywords: native whey protein fibrils, thioflavin T, viscosity.

Biography: Gunvantsinh Rathod is a Graduate Research Assistant and Ph D scholar in Food Science at Kansas State University. He pursued his M. Tech in Dairy Technology from National Dairy Research Institute, Karnal, India and B. Tech in Dairy Technology from SMC College of Dairy Science, AAU, Anand. He is also serving as a faculty and scientist as National Dairy Research Institute, Karnal, India since 2015.