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

alkyl polyglycosides
enzymatic activity
fatty alcohol ethoxylates
linear alkyl benzene sulfonate
nonyl phenol ethoxylate

How to Cite

1.
Bravo Rodríguez V, Jurado Alameda E, Martínez Gallegos JF, Reyes Requena A, García López AI, Sampaio Cabral JM, Fernandes P, Pina da Fonseca LJ. Modification of the activity of an α-amylase from Bacillus licheniformis by several surfactants. Electron. J. Biotechnol. [Internet]. 2006 Oct. 15 [cited 2024 Sep. 20];9(5):0-. Available from: https://preprints.pucv.cl/index.php/ejbiotechnology/article/view/v9n5-16

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.

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