Title
Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
Author
Silvia Armenta, Zaira Sánchez-Cuapio, Amelia Farrés, Karen Manoutcharian, Alejandra Hernandez-Santoyo, Sergio Sánchez, Romina Rodríguez-Sanoja
Year
2018
Journal
Data In Brief
Abstract
Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present the data article related to the interaction of one LaCBM26 and some mutated proteins with soluble α-glucans determined by enzyme-linked carbohydrate-binding assay, isothermal titration calorimetry (ITC), and affinity gel electrophoresis (AGE). The data of the behavior of proteins in presence and absence of substrate analyzed by circular dichroism CD and thermofluor are also presented. These results are complementary to the research article “The role of conserved non-aromatic residues in the Lactobacillus amylovorus α-amylase CBM26-starch interaction” (Armenta et al., 2019).
Instrument
J-710
Keywords
Circular dichroism, Secondary structure, Protein folding, Ligand binding, Biochemistry