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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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Published in: | ACS applied materials & interfaces 2015-08, Vol.7 (33), p.18832-18842 |
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creator | Bruna, Felipe Pereira, Marita G Polizeli, Maria de Lourdes T. M Valim, João B |
description | 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. |
doi_str_mv | 10.1021/acsami.5b05668 |
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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. 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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.</description><subject>alpha-Amylases - chemistry</subject><subject>alpha-Amylases - metabolism</subject><subject>Aluminum - chemistry</subject><subject>Biocatalysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Enzymes, Immobilized - metabolism</subject><subject>Hydrolysis</subject><subject>Hydroxides - chemistry</subject><subject>Magnesium - chemistry</subject><subject>Nanostructures - chemistry</subject><subject>Starch - metabolism</subject><issn>1944-8244</issn><issn>1944-8252</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNp1kEtOwzAQhi0EolDYskRZIqS0fsRJvGzLo0gFFoV1NLEdmiqJi51IZMcVOAoX4RCchKCU7ljNaOabX5oPoTOCRwRTMgbpoMxHPMU8DOM9dEREEPgx5XR_1wfBAB07t8Y4ZBTzQzSgIeWChPERWi5rsHLlTXMjoYaidbU3BaeVZyrv6_P7_WNStkU38O9fxpPCX0Crbbe9Mk1aaG_eKmvecqW9B6jMqk1trtwJOsigcPp0W4fo-eb6aTb3F4-3d7PJwgfGcO2LLMsiRklEcURJRnWsRaCACpEJ0FIpioELCVFGlVYsEhHDXJEQuFJScMGG6KLP3Vjz2mhXJ2XupC4KqLRpXEIiFgcxDTnt0FGPSmucszpLNjYvwbYJwcmvyKQXmWxFdgfn2-wmLbXa4X_mOuCyB7rDZG0aW3Wv_pf2A_Tgf0c</recordid><startdate>20150826</startdate><enddate>20150826</enddate><creator>Bruna, Felipe</creator><creator>Pereira, Marita G</creator><creator>Polizeli, Maria de Lourdes T. 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Interfaces</addtitle><date>2015-08-26</date><risdate>2015</risdate><volume>7</volume><issue>33</issue><spage>18832</spage><epage>18842</epage><pages>18832-18842</pages><issn>1944-8244</issn><eissn>1944-8252</eissn><abstract>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.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>26259168</pmid><doi>10.1021/acsami.5b05668</doi><tpages>11</tpages></addata></record> |
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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 |
title | Starch Biocatalyst Based on α‑Amylase-Mg/Al-Layered Double Hydroxide Nanohybrids |
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