This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rodríguez-Sanoja, R.
Right arrow Articles by Sanchez, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rodríguez-Sanoja, R.
Right arrow Articles by Sanchez, S.
Agricola
Right arrow Articles by Rodríguez-Sanoja, R.
Right arrow Articles by Sanchez, S.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, January 2005, p. 297-302, Vol. 71, No. 1
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.1.297-302.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Starch-Binding Domain Affects Catalysis in Two Lactobacillus {alpha}-Amylases

R. Rodríguez-Sanoja,* B. Ruiz, J. P. Guyot, and S. Sanchez

Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico

Received 25 August 2004/ Accepted 28 August 2004

A new starch-binding domain (SBD) was recently described in {alpha}-amylases from three lactobacilli (Lactobacillus amylovorus, Lactobacillus plantarum, and Lactobacillus manihotivorans). Usually, the SBD is formed by 100 amino acids, but the SBD sequences of the mentioned lactobacillus {alpha}-amylases consist of almost 500 amino acids that are organized in tandem repeats. The three lactobacillus amylase genes share more than 98% sequence identity. In spite of this identity, the SBD structures seem to be quite different. To investigate whether the observed differences in the SBDs have an effect on the hydrolytic capability of the enzymes, a kinetic study of L. amylovorus and L. plantarum amylases was developed, with both enzymes acting on several starch sources in granular and gelatinized forms. Results showed that the amylolytic capacities of these enzymes are quite different; the L. amylovorus {alpha}-amylase is, on average, 10 times more efficient than the L. plantarum enzyme in hydrolyzing all the tested polymeric starches, with only a minor difference in the adsorption capacities.

* Corresponding author. Mailing address: Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, UNAM A. P. 70228, 04510 Mexico City, Mexico. Phone: 52 55 56 22 38 67. Fax: 52 55 56 22 38 55. E-mail: romina{at}correo.biomedicas.unam.mx.

Applied and Environmental Microbiology, January 2005, p. 297-302, Vol. 71, No. 1
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.1.297-302.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Guillen, D., Santiago, M., Linares, L., Perez, R., Morlon, J., Ruiz, B., Sanchez, S., Rodriguez-Sanoja, R. (2007). Alpha-Amylase Starch Binding Domains: Cooperative Effects of Binding to Starch Granules of Multiple Tandemly Arranged Domains. Appl. Environ. Microbiol. 73: 3833-3837 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»