Enzymatic Hydrolysis of Soluble Starch with an α-Amylase from Bacillus licheniformis

• Published in: Biotechnology progress Vol. 22; no. 3; pp. 718 - 722
• Main Authors: Bravo Rodríguez, V, Jurado Alameda, E, Martínez Gallegos, J.F, Reyes Requena, A, García López, A.I
• Format: Journal Article
• Language: English
• Published: USA American Chemical Society 01-05-2006; American Institute of Chemical Engineers
• Subjects: alpha-amylase; alpha-Amylases - chemistry; Bacillus - enzymology; Bacillus - metabolism; Bacillus licheniformis; Biological and medical sciences; Biotechnology; enzymatic hydrolysis; Enzyme Activation; enzyme activity; enzyme kinetics; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; mathematical models; Models, Biological; Solubility; soluble starch; starch; Starch - chemistry; Temperature; Time Factors; Hydrolysis; Bacillales; Enzyme; Starch; Bacillus licheniformis; Glycosidases; Bacteria; Hydrolases; α-Amylase; Bacillaceae; O-Glycosidases
• ISSN: 8756-7938; 1520-6033
• DOI: 10.1021/bp060057a

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.