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

Identificadores
URI: http://hdl.handle.net/10481/32690
ISSN: 0717-3458
Exportar
RISMendeleyBibtex
Estadísticas
View Usage Statistics
Metadata
Show full item record
Author
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
Editorial
Pontificia Universidad Católica de Valparaíso (Chile)
Materia
α-amylase
 
Alkyl polyglycosides
 
Enzymatic activity
 
Fatty alcohol ethoxylates
 
Linear alkyl benzene sulfonate
 
Nonyl phenol ethoxylate
 
Date
2006
Referencia bibliográfica
Bravo Rodríguez, V.; et al. Modification of the activity of an a-amylase from Bacillus licheniformis by several surfactants. Electronic Journal of Biotechnology, 9(5): 566-571 (2006). [http://hdl.handle.net/10481/32690]
Sponsorship
Fellowship awarded to Juan Francisco Martínez Gallegos by Spanish Ministry of Science and Education, FPU fellowships program.
Abstract
The influence of different commercial surfactants on the enzymatic activity of a commercial α-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.
Collections