Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Husain, Qayyum; Ansari, Shakeel Ahmed; Alam, Fahad; Azam, Ameer

doi:10.1016/j.ijbiomac.2011.03.011

Cited by 137 publications

(62 citation statements)

References 32 publications

(39 reference statements)

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“…Maximum adsorption of the enzyme on bulk ZnO (20 U) and ZnO NPs (29 U) was achieved with 100 mg for both of the support. A similar behavior has also been observed by other investigators [26].…”

Section: Optimization Of Immobilized B-galactosidase On Bulk Zno and supporting

confidence: 91%

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Ethiraj

Mohanasrinivasan

Devi

et al. 2015

Bioprocess Biosyst Eng

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β-Galactosidase from Lactobacillus plantarum HF571129 was immobilized on zinc oxide nanoparticles (ZnO NPs) using adsorption and cross-linking technique. Immobilized β-galactosidase showed broad-spectrum pH optima at pH 5-7.5 and temperature 50-60 °C. Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that β-galactosidase successfully immobilized onto supports. Due to the limited diffusion of high molecular weight substrate, K m of immobilized enzyme slightly increased from 6.64 to 10.22 mM, while V max increased from 147.5 to 192.4 µmol min(-1) mg(-1) as compared to the soluble enzyme. The cross-linked adsorbed enzyme retained 90 % activity after 1-month storage, while the native enzyme showed only 74 % activity under similar incubation conditions. The cross-linked β-galactosidase showed activity until the seventh cycle and maintained 88.02 % activity even after the third cycle. The activation energy of thermal deactivation from immobilized biocatalyst was 24.33 kcal/mol with a half-life of 130.78 min at 35 °C. The rate of lactose hydrolysis for batch and packed bed was found to be 0.023 and 0.04 min(-1).

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Section: Optimization Of Immobilized B-galactosidase On Bulk Zno and supporting

confidence: 91%

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Ethiraj

Mohanasrinivasan

Devi

et al. 2015

Bioprocess Biosyst Eng

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“…The immobilization yield of this enzyme on nano ZnO was superior as compared to immobilization obtained on native ZnO. Nano ZnO bound enzyme was also remarkably more stable as compared to enzyme bound on native ZnO [27]. Moreover, nanosupports containing magnetic properties are very easy to collect from the reaction mixture.…”

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confidence: 94%

Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review

Husain¹

2017

Biocatalysis

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Numerous types of nanoparticles and nanocomposites have successfully been employed for the immobilization and stabilization of amylolytic enzymes; α-amylases, β-amylases, glucoamylases and pullulanases. Nano-support immobilized amylolytic enzymes retained very high activity and yield of immobilization. The immobilization of these enzymes, particularly α-amylases and pullulanases, to the nanosupports is helpful in minimizing the problem of steric hindrances during binding of substrate to the active site of the enzyme. The majority of nano-support immobilized amylolytic enzymes exhibited very high resistance to inactivation induced by different kinds of physical and chemical denaturants and these immobilized enzyme preparations maintained very high activity on their repeated and continuous uses. Amylolytic enzymes immobilized on nano-supports have successfully been applied in food, fuel, textile, paper and pulp, detergent, environmental, medical, and analytical fields.

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“…The functionalized nanocarriers allow enzymes to be assembled in ordered structures, which act as a nanoscale information storage and processing system. Research has shown that nanostructured materials possess the requirements of the NBCs and provide large surface areas that allow a higher enzyme loading and reduce mass transfer resistance for substrates [1]. The NBC is a specifically functionalized enzyme-nanocarrier assembly, which promises exciting advantages in improving enzyme stability, capability and engineering performances, and allowing creation of a microenvironment surrounding the enzyme catalysts for maximal reaction efficiencies.…”

Section: Introductionmentioning

confidence: 99%

Nanobiocatalyst advancements and bioprocessing applications

Misson

Zhang

Jin

2015

J. R. Soc. Interface.

211

108

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The nanobiocatalyst (NBC) is an emerging innovation that synergistically integrates advanced nanotechnology with biotechnology and promises exciting advantages for improving enzyme activity, stability, capability and engineering performances in bioprocessing applications. NBCs are fabricated by immobilizing enzymes with functional nanomaterials as enzyme carriers or containers. In this paper, we review the recent developments of novel nanocarriers/nanocontainers with advanced hierarchical porous structures for retaining enzymes, such as nanofibres (NFs), mesoporous nanocarriers and nanocages. Strategies for immobilizing enzymes onto nanocarriers made from polymers, silicas, carbons and metals by physical adsorption, covalent binding, cross-linking or specific ligand spacers are discussed. The resulting NBCs are critically evaluated in terms of their bioprocessing performances. Excellent performances are demonstrated through enhanced NBC catalytic activity and stability due to conformational changes upon immobilization and localized nanoenvironments, and NBC reutilization by assembling magnetic nanoparticles into NBCs to defray the high operational costs associated with enzyme production and nanocarrier synthesis. We also highlight several challenges associated with the NBC-driven bioprocess applications, including the maturation of large-scale nanocarrier synthesis, design and development of bioreactors to accommodate NBCs, and long-term operations of NBCs. We suggest these challenges are to be addressed through joint collaboration of chemists, engineers and material scientists. Finally, we have demonstrated the great potential of NBCs in manufacturing bioprocesses in the near future through successful laboratory trials of NBCs in carbohydrate hydrolysis, biofuel production and biotransformation.

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Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Cited by 137 publications

References 32 publications

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Nanomaterials as novel supports for the immobilization of amylolytic enzymes and their applications: A review

Nanobiocatalyst advancements and bioprocessing applications

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