Starch Biocatalyst Based on α‑Amylase-Mg/Al-Layered Double Hydroxide Nanohybrids

The design of new biocatalysts through the immobilization of enzymes, improving their stability and reuse, plays a major role in the development of sustainable methodologies toward the so-called green chemistry. In this work, α-amylase (AAM) biocatalyst based on Mg3Al-layered double-hydroxide (LDH)...

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Bibliographic Details
Published in:ACS applied materials & interfaces 2015-08, Vol.7 (33), p.18832-18842
Main Authors: Bruna, Felipe, Pereira, Marita G, Polizeli, Maria de Lourdes T. M, Valim, João B
Format: Article
Language:English
Subjects:
alpha-Amylases - chemistry
alpha-Amylases - metabolism
Aluminum - chemistry
Biocatalysis
Electrophoresis, Polyacrylamide Gel
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Hydrolysis
Hydroxides - chemistry
Magnesium - chemistry
Nanostructures - chemistry
Starch - metabolism
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Summary:The design of new biocatalysts through the immobilization of enzymes, improving their stability and reuse, plays a major role in the development of sustainable methodologies toward the so-called green chemistry. In this work, α-amylase (AAM) biocatalyst based on Mg3Al-layered double-hydroxide (LDH) matrix was successfully developed with the adsorption method. The adsorption process was studied and optimized as a function of time and enzyme concentration. The biocatalyst was characterized, and the mechanism of interaction between AAM and LDH, as well as the immobilization effects on the catalytic activity, was elucidated. The adsorption process was fast and irreversible, thus yielding a stable biohybrid material. The immobilized AAM partially retained its enzymatic activity, and the biocatalyst rapidly hydrolyzed starch in an aqueous solution with enhanced efficiency at intermediate loading values of ca. 50 mg/g of AAM/LDH. Multiple attachments through electrostatic interactions affected the conformation of the immobilized enzyme on the LDH surface. The biocatalyst was successfully stored in its dry form, retaining 100% of its catalytic activity. The results reveal the potential usefulness of a LDH compound as a support of α-amylase for the hydrolysis of starch that may be applied in industrial and pharmaceutical processes as a simple, environmentally friendly, and low-cost biocatalyst.
ISSN:1944-8244
1944-8252
DOI:10.1021/acsami.5b05668