Journal
APPLIED CLAY SCIENCE
Volume 183, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.clay.2019.105329
Keywords
Montmorillonite; Organoclay; Lipase; Biocatalyst; Enzyme immobilization
Funding
- National Natural Science Foundation of China [41672039]
- Sichuan Science and Technology Program [2019JDJQ0056]
- Longshan Academic Talent Research Support Program of the Southwest University of Science and Technology [17LZX419, 18LZX405]
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Clay minerals provide an excellent platform for enzyme immobilization, which can improve enzyme activity and stability for industrial applications. In this study, lipase from Aspergillus oryzae was immobilized on 3-amino-propyltriethoxysilane (APTES) amphiphilic functionalized montmorillonite (Mt) support via 1-(3-Dimethylaminopropyl)-3-ethyl-carbodiimide hydrochloride (EDC) spacer. The APTES-Mt and APTES-Mt based nanostructured biocatalyst (lipase-Mt) were characterized by XRD, FT-IR, TEM, SEM and contact angle analysis. Optimal immobilization conditions were determined considering parameters of EDC concentration, initial lipase concentration, pH, and reaction time. The results indicated that lipase-Mt activity was 40.65 U/mg, which was nearly 4-fold higher than that of free lipase under optimal conditions. The Michaelis-Menten constant (K-m) were found as 0.357 mM and 3.406 mM for free and lipase-Mt, respectively. The maximum reaction rate (V-max) for the free and lipase-Mt were calculated as 63.69 mM/(L.min) and 312.5 mM/(L.min), respectively. Further, the interfacial activation by amphiphilic surface of APTES-Mt and enlarged catalytic interface contributed to the improved activity and storage stability of lipase-Mt. Thus, this work demonstrate an economically viable method for constructing nanostructured biocatalyst for industrial applications based on covalent immobilization of enzyme onto clay minerals.
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