Reduction of Streptococcus thermophilus in a whey protein isolate by low moisture extrusion cooking without loss of functional properties

A whey protein isolate powder (WPI) (4–5% water) inoculated with 5x10⁵ viable Streptococcus thermophilus per g, was continuously processed in a twin screw extruder under the following conditions (barrel length = 500 or 1000 mm; screw profile = forward transport and compression elements; moisture content during extrusion = 4–5%; feed rate = 10 kg h^-1; barrel temperature ( T_b ) = 80–204°C; speed of screw rotation = 50 r.p.m.). The minimum residence time determined by pulse injection of erythrosin was 20–25 s (500 mm barrel) or 35–40 s (1000 mm barrel).
Reduction values of viable Streptococcus thermophilus of 10^4.2-fold (500 mm barrel, T_b = 143°C) or 10^4.9-fold (1000 mm barrel, T_b = 133°C) were obtained without any modification of protein solubility or gelling properties. WPI extruded at the highest barrel temperatures (182–204°C) underwent limited browning and reduction of protein solubility. Gel permeation and hydrophobic interaction chromatography of the soluble constituents did not show any aggregates of β-lactoglobulin or α-lactalbumin.
Gels prepared from control or extruded WPI ( T_b 143°C with a barrel length = 500 mm or T_b 133°C with a barrel length = 1000 mm) were identical, as judged by scanning electron microscopy and rheological evaluations.