Immobilization of α-amylase onto poly(glycidyl methacrylate) grafted electrospun fibers by ATRP

Oktay, Burcu; Demir, Serap; Kayaman‐Apohan, Nilhan

doi:10.1016/j.msec.2015.02.033

Cited by 42 publications

(22 citation statements)

References 43 publications

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“…The resulting K m values were calculated as 0.839, 1.227, and 1.701 mg/mL, whereas V max values were 220.3, 48.85, and 37.12 mmol/min/mg for free, ESM-, and AgNP/ESM-immobilized a-amylases, respectively. The increase of K m and decrease of V max after immobilization showed the decrease of affinity between enzyme and substrate, which was consistent with previous reports [3,6,21,22]. This could be explained by the diffusional limitation of the substrate due to steric hindrance from the immobilizing supports, which caused lower accessibility of substrate to the active sites of the immobilized enzymes or conformational changes of the enzyme occurring in the immobilizing process which re sulted in a lower possibility of substrate-enzyme complex formation [3,8,20].…”

Section: Enzyme Kinetics Of Free and Immobilized A-amylasessupporting

confidence: 93%

Immobilization of α-amylase on eggshell membrane and Ag-nanoparticle-decorated eggshell membrane for the biotransformation of starch

Huang

Feng

2017

Starch - Stärke

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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. Km values were 0.839, 1.227, and 1.701 mg/mL, and Vmax 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.

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Section: Enzyme Kinetics Of Free and Immobilized A-amylasessupporting

confidence: 93%

Immobilization of α-amylase on eggshell membrane and Ag-nanoparticle-decorated eggshell membrane for the biotransformation of starch

Huang

Feng

2017

Starch - Stärke

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“…Atom transfer radical polymerization (ATRP) is one of CRP, where a rapid dynamic equilibrium is created between a predominant amount of dormant chains and a low concentration of active propagating chains. Unexpected radical termination is not observed in this process .…”

Section: Introductionmentioning

confidence: 73%

Preparation and thermal properties of Alkoxy Silane functionalized polyether sulfone/well‐defined poly(trimethoxysilyl) propyl methacrylate‐based hybrid materials

Oktay

Baştürk

Kahraman

et al. 2017

Polymer Engineering & Sci

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In this study, novel polyethersulfone (PES) and poly(trimethoxysilyl) propyl methacrylate (PMPS) containing hybrid materials were prepared. PES was functionalized with trimethoxysilane groups by UV‐induced grafting reaction. PMPS was synthesized by atom transfer radical polymerization. In the followed process, the functionalized PES mixed with different amount of PMPS, thermally treated to promote sol–gel crosslinking process to prepare the PES‐based hybrid materials. The trimethoxysilane grafted PES chains are covalently bonded with the well‐defined trimethoxysilane groups of PMPS. The chemical structure of the prepared PES and PMPS is confirmed by Fourier transform infrared analysis. The morphology of the hybrids was investigated by scanning electron microscopy. The results of thermogravimetric analysis show that the thermal stability of the hybrid materials was significantly affected with the addition of PMPS. POLYM. ENG. SCI., 58:1346–1352, 2018. © 2017 Society of Plastics Engineers

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“…Immobilized α-amylase retained 60% of the enzyme activity even after its 10 repeated uses. Oktay et al [57] described the immobilization of α-amylase onto polyvinyl alcohol-nanofibers functionalized with 2-bromoisobutyryl bromide and followed by surface initiated atom transfer radical polymerization of glycidyl methacrylate in a single step. The thermal stability of the enzyme was improved upon immobilization and its pH-optimum was shifted from pH 6.0 to 6.5.…”

Section: α-Amylasementioning

confidence: 99%

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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Immobilization of α-amylase onto poly(glycidyl methacrylate) grafted electrospun fibers by ATRP

Cited by 42 publications

References 43 publications

Immobilization of α-amylase on eggshell membrane and Ag-nanoparticle-decorated eggshell membrane for the biotransformation of starch

Immobilization of α-amylase on eggshell membrane and Ag-nanoparticle-decorated eggshell membrane for the biotransformation of starch

Preparation and thermal properties of Alkoxy Silane functionalized polyether sulfone/well‐defined poly(trimethoxysilyl) propyl methacrylate‐based hybrid materials

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

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