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.     

Microcoagulation of a Whey Protein Isolate by Extrusion Cooking at Acid pH

A whey protein isolate (WPI) was coagulated by thermomechanical processing in a twin screw extruder. Nonaggregated semi-solid spreads were obtained only in the pH range 3.5–3.9, at ca 20% protein (77% water), a barrel temperature of 90–100°C and a screw speed of 100–200 rpm. WPI extrusion-coagulated at pH 3.9 displayed a high nitrogen solubility (NSI) (43–47%). Electrophoresis indicated that the β-lactoglobulin constituent was entirely soluble in 1% SDS, while scanning calorimetry revealed about 82% protein unfolding. WPI extrusion-coagulated at pH 4.5–6.8 displayed lower NSI (25%), were less soluble in 1% SDS, were 88% unfolded and had grainy texture. Light microscopy, centrifugation in glycerol solutions, and laser diffractometry indicated the acid spread (pH 3.9) was composed of small coagulated particles, mean diameter 11.5 μm (volume basis).     

THERMAL PROCESS CALCULATION USING ARTIFICIAL NEURAL NETWORKS AND OTHER TRADITIONAL METHODS

This work aimed to develop a method of thermal process calculation of canned food based on an artificial neural network and to compare it to the traditional Ball and Stumbo methods. A back‐propagation through time network was used as a model of heat conduction occurring in canned food, in order to predict the cold point temperature as a function of the autoclave and the initial product temperature. For training the network, a dataset of the cold point and retort temperature along time was obtained by processing a paste‐based product in autoclave. The network architecture (5‐8‐9‐1) was selected, presenting an excellent generalization capacity, with a mean relative error of 2.2% between the calculated F‐values of the observed and predicted time–temperature data. The Ball and Stumbo methods presented higher errors as the retort temperature was not constant. Neural network showed a great potential for online process calculation by having advantages such as precision and simplicity.     

Gelling properties of whey protein isolate: influence of calcium removal by dialysis or diafiltration at acid or neutral pH

Dialysis of whey protein isolates (WPI) removed much more calcium when carried out at an acid pH (close to 4.0) than at neutral pH. Diafiltration at acid pH was also effective. The characteristics of thermally-induced gels prepared from WPI dialysed at acid or neutral pH were studied at pH 3.75 or pH 7.0, respectively, and at calcium concentrations ranging from 0 to about 60mM (with addition of calcium chloride). The water-holding capacity (WHC) and elasticity of gels increased with decreasing calcium concentration, at both pHs. Gel firmness was maximum at 10–20 mM calcium. The solubility of the protein constituents of WPI gels in a pH 8.0 buffer was high in the case of acid gels (especially at calcium concentrations lower or equal to 20 mM) and low for neutral gels at all calcium concentrations. Protein solubility values in the presence or absence of denaturing and reducing agents reflect the existence of intermolecular disulphide bonds in neutral gels and their absence in acid gels.