Effect of pulsed electric field treatment on the kinetics of rehydration, textural properties, and the extraction of intracellular compounds of dried chickpeas.

This study investigated the effect of pulsed electric fields (PEF) pretreatment on rehydration kinetics, firmness, and release of intracellular components of dried chickpeas during rehydration at 35 to 65°C. After soaking preconditioning, chickpeas were subjected to PEF treatments (2.5 and 3.3 kV/cm, 0.2 to 12.0 kJ/kg, 15 µs pulse width, 20 Hz frequency). PEF treated and untreated chickpeas were dried in crossflow air dryer and their rehydration at constant seed/water ratio of 1:5 was studied for 24 hr. During rehydration, moisture, firmness, and concentration of released proteins, carbohydrates and raffinose family oligosaccharides (RFO) were determined and described using appropriate mathematical models. PEF treatment led to up to 70% higher rehydration rates of dried chickpeas. This increase corresponds to rehydration time of approximately 1.5 hr, as opposed to 5 hr for untreated samples. Firmness of PEF treated chickpeas (for energy inputs higher than 3 kJ/kg) during rehydration decreased up to 30% compared to untreated samples. The firmness of untreated samples after 300 min of rehydration was achieved at much shorter times (up to 30 min) for PEF treated samples. At the end of 300 min of rehydration, more than 47.7%, 76.1%, and 86.6% of total raffinose, stachyose, and verbascose, respectively has been extracted, but only 0.03% of nutritionally valuable proteins from PEF treated chickpeas. Consequently, this study demonstrates that PEF processing could be implemented in dried chickpeas processing as pretreatment, for the reduction of rehydration time prior to cooking and of intestinal discomfort caused by RFO.

A novel thermophile ß-galactosidase from Thermothielavioides terrestris producing galactooligosaccharides from acid whey.

ß-Galactosidases are key enzymes in the food industry. Apart from the hydrolysis of the saccharide bond of lactose, they also catalyze transgalactosylation reactions, producing galactooligosaccharides (GOS) with prebiotic activity. Here we report the heterologous production in Pichia pastoris of a novel ß-galactosidase from the fungus Thermothielavioides terrestris. The enzyme (TtbGal1) was purified and characterized, showing optimal activity at 60 °C and pH 4. TtbGal1 is thermostable, retaining almost full activity for 24 h at 50 °C. It was applied to the production of GOS from defined lactose solutions and acid whey, a liquid waste from the Greek yoghurt industry, reaching yields of 19.4 % and 14.8 %, respectively. HILIC-ESI-QTOF-MS analysis revealed the production of GOS with up to 4 saccharide monomers. The results demonstrate efficient GOS production catalyzed by TtbGal1, valorizing acid whey, a waste with a heavy polluting load from the dairy industry.