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Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26.

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-? interactions and hydrogen bonds. Here, we present the data article related to the interaction of one LaCBM26 and some mutated proteins with soluble ?-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 ?-amylase CBM26-starch interaction" (Armenta et al., 2019).

SUBMITTER: Armenta S

PROVIDER: S-EPMC6260227 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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Data concerning secondary structure and alpha-glucans-binding capacity of the <i>La</i>CBM26.

Armenta Silvia S Sánchez-Cuapio Zaira Z Farrés Amelia A Manoutcharian Karen K Hernandez-Santoyo Alejandra A Sánchez Sergio S Rodríguez-Sanoja Romina R

Data in brief 20181114

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 <i>La</i>CBM26 and some mutated proteins with soluble α-glucans determined by enzyme-linked carbohydrate-binding assay, isothermal titration calorimetry (ITC), and affinity gel electrophoresis (AGE). Th ...[more]

PMID: 30519620

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