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Immobilization of α‐amylase on eggshell membrane and Ag‐nanoparticle‐decorated eggshell membrane for the biotransformation of starch
Author(s) -
Du Liangwei,
Huang Meiying,
Feng JiaXun
Publication year - 2017
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.201600352
Subject(s) - eggshell membrane , glutaraldehyde , amylase , immobilized enzyme , chemistry , thermal stability , membrane , chemical engineering , chromatography , nanoparticle , starch , enzyme , food science , biochemistry , organic chemistry , engineering
Enzyme biocatalysts are very sensitive to environmental conditions. To improve their stability and operational lifetime, free enzymes are usually immobilized on a solid support. In this study, α‐amylase was immobilized on eggshell membrane (ESM) and Ag‐nanoparticle‐decorated eggshell membrane (AgNP/ESM) using glutaraldehyde as a cross‐linking agent. After immobilization, enzyme loading, activity, kinetic parameters, reusability, and storage stability were investigated. The AgNP/ESM possessed a larger enzyme loading than ESM alone. The optimal pH and temperature of immobilized α‐amylases remained at 5.0 and 55°C, but the pH tolerance and thermal stability of AgNP/ESM‐immobilized enzyme were better than those of free enzyme. K m values were 0.839, 1.227, and 1.701 mg/mL, and V max values were 220.3, 48.85, and 37.12 μmol/min/mg for free, ESM‐, and AgNP/ESM‐immobilized α‐amylases, respectively. After ten uses, AgNP/ESM‐immobilized α‐amylase exhibited better operational stability as compared with ESM immobilized enzyme. After 50 days of storage at 4°C, the losses of activity were 46.29, 35.11, and 28.74% for free, ESM‐, and AgNP/ESM‐immobilized α‐amylases, respectively. These results indicate that AgNP/ESM is a more promising support as compared with ESM for the immobilization of α‐amylase.