Modification of the activity of an alpha-amylase from Bacillus licheniformis by several surfactants

• Published in: Electronic Journal of Biotechnology Vol. 9; no. 5
• Main Authors: Bravo Rodríguez, Vicente, Jurado Alameda, Encarnación, Martínez Gallegos, Juan Francisco, Reyes Requena, Antonia, García López, Ana Isabel, Sampaio Cabral, Joaquim Manuel, Fernandes, Pedro, Pina da Fonseca, Luis Joaquim
• Format: Journal Article
• Language: Portuguese
• Published: Pontificia Universidad Católica de Valparaíso 01.10.2006
• Subjects: BIOTECHNOLOGY & APPLIED MICROBIOLOGY; alpha-amylase; linear alkyl benzene sulfonate; alkyl polyglycosides; enzymatic activity; fatty alcohol ethoxylates; nonyl phenol ethoxylate
• ISSN: 0717-3458; 0717-3458
• DOI: 10.4067/S0717-34582006000500012

The influence of different commercial surfactants on the enzymatic activity of a commercial alpha-amylase from Bacillus licheniformis (Termamyl 300 L) has been studied. As non-ionic surfactants, alkyl polyglycosides (Glucopon® 215, Glucopon® 600 and Glucopon® 650) were studied, as were fatty alcohol ethoxylates (Findet 1214N/23 and Findet 10/15), and nonyl phenol ethoxylate (Findet 9Q/21.5NF). Also, an anionic surfactant, linear alkyl benzene sulfonate (LAS) was assayed. In general, none of the non-ionic surfactants studied, except Findet 10/15, vary substantially the enzymatic activity. Findet 10/15 has the strongest hydrophobic character and reduces the enzymatic activity more significantly the greater its concentration. Regarding LAS, this surfactant significantly depressed enzymatic activity, presumably due to the electrostatic interactions caused by its anionic character.