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Applied and Environmental Microbiology, June 2007, p. 3833-3837, Vol. 73, No. 12
0099-2240/07/$08.00+0 doi:10.1128/AEM.02628-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

L. Linares,
R. Pérez,
J. Morlon,
B. Ruiz,
S. Sánchez, and
R. Rodríguez-Sanoja*
Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, A.P. 70228, Ciudad Universitaria, Coyoacán 04510, México D.F., México
Received 10 November 2006/ Accepted 22 April 2007
The Lactobacillus amylovorus alpha-amylase starch binding domain (SBD) is a functional domain responsible for binding to insoluble starch. Structurally, this domain is dissimilar from other reported SBDs because it is composed of five identical tandem modules of 91 amino acids each. To understand adsorption phenomena specific to this SBD, the importance of their modular arrangement in relationship to binding ability was investigated. Peptides corresponding to one, two, three, four, or five modules were expressed as His-tagged proteins. Protein binding assays showed an increased capacity of adsorption as a function of the number of modules, suggesting that each unit of the SBD may act in an additive or synergic way to optimize binding to raw starch.
Published ahead of print on 27 April 2007.
Present address: Facultad de Ciencias Marinas, Universidad Autónoma de Baja California, Km. 103, Carretera Tijuana-Ensenada, 22800 Baja California, México.
Present address: Unité Mixte de Recherche 5539 CNRS, Case 107, Département Biologie-Sante, Université Montpellier II, 34095 Montpellier, France.
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