V. Bravo Rodríguez

Enzymatic hydrolysis of soluble starch with an α-amylase from Bacillus licheniformis

The enzymatic hydrolysis of soluble starch with an α‐amylase from Bacillus licheniformis (commercial enzyme Termamyl 300 L Type DX) have been experimentally studied at pH 7.5, within the temperature range of 37–75 °C, at initial substrate concentrations of between 0.25 and 2.00 g/L, and enzyme concentrations of between 0.575 × 10−4 and 13.8 × 10−4 g/L. To follow the reaction a procedure based on the iodometric method for measuring α‐amylase activity was used. The kinetics of the enzymatic hydrolysis was fitted to the Michaelis‐Menten equation using the integral method, taking into account that the thermal deactivation of the enzyme follows a second‐order kinetic. These parameters were fitted to the Arrhenius equation obtaining activation energies of 24.4 and 41.7 kJ/mol and preexponential factors of 734.9 g/L and 1.74 × 108 min−1 for KM and k, respectively.

Formation of complexes between alkyl polyglycosides and potato starch.

The formation of complexes between soluble potato starch and three commercial alkyl polyglycosides has been studied by means of surface tension measurements at 37 degrees C. All surfactants assayed form complexes with starch, the quantity of bound surfactant being proportional to the amount of starch present in the solution. For all alkyl polyglycoside-starch systems tested, there is a direct proportional relationship between the bound and total surfactant concentrations, so that the formation of the surfactant-starch complex continues until the minimum surface tension is reached without detectable starch saturation prior to the occurrence of surfactant micelles. Binding isotherms and Scatchard plots support the idea that alkyl polyglycosides are bound to amylose by positive cooperative binding and to amylopectin by non-cooperative Langmuir-type binding.