Meso-molding three-dimensionally ordered macroporous alumina: A new platform to immobilize enzymes with high performance
Autor: | Liya Gao, Li Ma, Yanjun Jiang, Jiaojiao Li, Ying He, Luyan Yin, Liya Zhou, Xucong Luo |
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Rok vydání: | 2019 |
Předmět: |
0106 biological sciences
0303 health sciences Environmental Engineering biology Immobilized enzyme Biomedical Engineering Bioengineering biology.organism_classification 01 natural sciences 03 medical and health sciences chemistry.chemical_compound chemistry Chemical engineering Nitrile hydratase 010608 biotechnology Copolymer Candida antarctica Thermal stability Polystyrene Glutaraldehyde Mesoporous material 030304 developmental biology Biotechnology |
Zdroj: | Biochemical Engineering Journal. 146:60-68 |
ISSN: | 1369-703X |
DOI: | 10.1016/j.bej.2019.03.002 |
Popis: | The meso-molding three-dimensionally ordered macroporous alumina (3DOM/m-Al) was synthesized via a dual-templating approach (polystyrene (PS) colloidal crystals as hard template and triblock copolymer P123 as soft template) with hydrous aluminum isopropoxide as precursor. The obtained 3DOM/m-Al was characterized, and the results showed that 3DOM/m-Al had ordered macropores (ca. 300 nm in diameter) with wormhole-like mesopores, relatively high surface areas (338.1 m2/g), large pore volumes (0.4030 cm3/g) and tunable pore sizes. The amino functionalized 3DOM/m-Al by aminopropyltriethoxysilane (APTES) was activated by glutaraldehyde and used as support for the immobilization of three different commercial enzymes (Lipase B from Candida antarctica (CALB), penicillin G acylase (PGA) and nitrile hydratase (NHase)). The result of confocal laser scanning microscopy (CLSM) indicated that the enzyme was successfully immobilized onto glutaraldehyde-activated NH2-3DOM/m-Al. The effect of the immobilized conditions on the specific activity of enzymes was investigated. Compared with free enzymes, the immobilized enzymes exhibited enhanced thermal stability. The three immobilized enzymes (CALB@NH2-3DOM/m-Al, PGA@NH2-3DOM/m-Al and NHase@NH2-3DOM/m-Al) were applied for the synthesis of palmitic acid, 6-aminopenicillanic acid (6-APA) and acrylamide, respectively. After recycling 10 times, CALB@NH2-3DOM/m-Al, PGA@NH2-3DOM/m-Al and NHase@NH2-3DOM/m-Al retained approximately 76%, 87% and 52% of their initial activities, respectively, indicating that the immobilized enzymes had good operational stability. Therefore, this work documented herein provides a versatile platform for enzyme immobilization with several inherent advantages. |
Databáze: | OpenAIRE |
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