Immobilization of lipase onto spacer-arm attached poly(GMA-HEMA-EGDMA) microspheres

Bayramoğlu, Gülay; Kaya, Bülent; Arıca, M. Yakup

doi:10.1016/j.foodchem.2004.07.022

Cited by 94 publications

(54 citation statements)

References 32 publications

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“…The prepared polymer microspheres were used for laccase immobilization via covalent linkage. Among the great variety of enzymes, laccase has gained much attention for being capable of catalyzing a wide range of popular reactions such as delignification, waste detoxification and decontamination, decolourization of dyes, degradation of polycyclic aromatic hydrocarbons, and bioremediation and as bioreceptor in biosensors application [17,18]. Thus, laccase was chosen as an enzyme to understand the interaction of epoxy-immobilized laccase conjugated methacrylate-acrylate copolymer microspheres.…”

Section: Introductionmentioning

confidence: 99%

Effects of Temperature and pH on Immobilized Laccase Activity in Conjugated Methacrylate-Acrylate Microspheres

Mazlan

Hanifah

2017

International Journal of Polymer Science

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Immobilization of laccase on the functionalized methacrylate-acrylate copolymer microspheres was studied. Poly(glycidyl methacrylate-co-n-butyl acrylate) microspheres consisting of epoxy groups were synthesized using facile emulsion photocuring technique. The epoxy groups in poly(GMA-co-nBA) microspheres were then converted to amino groups. Laccase immobilization is based on covalent binding via amino groups on the enzyme surface and aldehyde group on the microspheres. The FTIR spectra showed peak at 1646 cm −1 assigned to the conformation of the polymerization that referred to GMA and nBA monomers, respectively. After modification of the polymer, intensity of FTIR peaks assigned to the epoxy ring at 844 cm −1 and 904 cm −1 was decreased. The results obtained from FTIR exhibit a good agreement with the epoxy content method. The activity of laccaseimmobilized microspheres increased upon increasing the epoxy content. Furthermore, poly(GMA-co-nBA) microspheres revealed uniform size below 2 m that contributes to large surface area of the microspheres to be used as a matrix, thus increasing the enzyme capacity and enzymatic reaction. Immobilized enzyme also shifted to higher pH and temperature compared to free enzyme.

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Section: Introductionmentioning

confidence: 99%

Effects of Temperature and pH on Immobilized Laccase Activity in Conjugated Methacrylate-Acrylate Microspheres

Mazlan

Hanifah

2017

International Journal of Polymer Science

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“…Transmission electron microscopy (TEM) had also been done in order to determine the structures of the silica particles obtained. Results in Figure 2 showed that a cellular structure with disordered multi-channels was found in the mesoporous silica, which would be very beneficial to immobilize the enzyme due to the increase in the surface area (Bayramoğlu et al, 2005).…”

Section: Morphology Of Nano-sized Mesoporous Silica Particlesmentioning

confidence: 99%

Preparation of Nano-Sized Mesoporous Silica and Its Application in Immobilization of β-galactosidase from Aspergillus Oryzae

Jiao¹,

Liu²,

Ge³

et al. 2017

IJC

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In alkaline conditions, monodisperse nano-sized mesoporous silica was synthesized using cetyl trimethyl ammonium bromide (CTAB) as template and tetraethoxysilane (TEOS) silica as source in ethanol / water cosolvent conditions. Using method of nitrogen adsorption, specific surface area of the dried monodisperse nano-sized mesoporous silica was about 1591 m 2 /g and the pore size was about 3.8 nm. The field-emission scanning electron microscope (SEM) micrographs showed that the silica particles obtained were spherical with an approximate diameter of 160 nm and of good dispersion. Transmission electron microscopy (TEM) revealed that the carrier had an excellent cellular structure with disordered multi-channels and smooth surface. The nano-sized mesoporous silica above was employed to immobilize β-galactosidase from aspergillus oryzae for the first time. At the experimental conditions in section 2.4, the enzyme activity and the activity yield were 535.11 U/g dry carrier and 79.63%, respectively. Kinetic data of the immobilized enzyme such as optimum temperature, pH, and thermal and pH stability among other valuable results were also determined.

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“…In this way, a vast number of very strong bonds are formed, and a considerable increase of stability is achieved due to multiple bonding. In addition, polymers containing epoxy groups can be easily modified by other activating agents such as glutaraldehyde, if the lipase activity decreases due to the formation of undesirable interactions between the enzyme and supports due to short distance (Bayramoglu et al 2005). Immobilization methods are highly specific and should be optimized for a particular lipase support system.…”

Section: Shah and Gupta Immobilizedmentioning

confidence: 99%

Biodiesel Fuel Production by Enzymatic Transesterification of Oils: Recent Trends, Challenges and Future Perspectives

Luković¹,

Knežević‐Jugović²,

Bezbradica³

2011

Alternative Fuel

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Immobilization of lipase onto spacer-arm attached poly(GMA-HEMA-EGDMA) microspheres

Cited by 94 publications

References 32 publications

Effects of Temperature and pH on Immobilized Laccase Activity in Conjugated Methacrylate-Acrylate Microspheres

Effects of Temperature and pH on Immobilized Laccase Activity in Conjugated Methacrylate-Acrylate Microspheres

Preparation of Nano-Sized Mesoporous Silica and Its Application in Immobilization of β-galactosidase from Aspergillus Oryzae

Biodiesel Fuel Production by Enzymatic Transesterification of Oils: Recent Trends, Challenges and Future Perspectives

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