Immobilization of aminoacylase on electrospun nanofibrous membrane for the resolution of dl-theanine

Li, Jian; Zhao, Zhehao; Mo, Ting; Wang, Lanfang; Li, Ping

doi:10.1016/j.molcatb.2015.03.003

Cited by 8 publications

(15 citation statements)

References 31 publications

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“…C CP MAS NMR analysis of the prepared materials was conducted in a DSX spectrometer (Bruker, Germany). A sample of about 100 mg was placed in a ZrO 2 rotator 4 mm in diameter, which enabled spinning of the sample.…”

Section: Methodsmentioning

confidence: 99%

“…Centrifugation at the magic angle was performed at a spinning frequency of 8.4 kHz. The C CP MAS NMR spectra were recorded at 100.63 MHz in a standard 4 mm MAS probe by application of single pulse excitation with high‐power proton decoupling (pulse repetition 10 s, spinning speed 10 kHz). Si MAS NMR spectra were recorded with a pulse duration of 4.5 µs, a contact time of 1.5 ms and a pulse spacing of 6 s.…”

Section: Methodsmentioning

confidence: 99%

“…In a small number of reported studies, aminoacylase has been immobilized on epoxy‐activated copolymer beads, modified Fe 3 O 4 nanoparticles, Silochrome C‐80, and electrospun nanofibrous membrane . Apart from acylase I, immobilization processes have also been carried out using penicillin G acylase (PGA) (also a member of the aminoacylase family), which has been immobilized on various types of metal‐modified systems and macro‐ and mesoporous materials …”

Section: Introductionmentioning

confidence: 99%

“…In a study by Li et al, the enzyme aminoacylase was immobilized on polyvinyl alcohol‐based nanofibrous membranes, which were produced via electrospinning. The immobilized aminoacylase exhibited better resistance to changes in temperature and pH than the free enzyme, with optimal conditions being pH 8 and 52°C.…”

Section: Introductionmentioning

confidence: 99%

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Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino‐ and carbonyl‐grafted stöber silica

Kołodziejczak-Radzimska

Zdarta

Jesionowski

2018

Biotechnology Progress

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Acylase I from Aspergillus melleus was immobilized on supports consisting of unmodified and modified silica. Modification was performed using 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The effectiveness of immobilization was investigated using the standard Bradford method in addition to a number of physicochemical techniques, including spectroscopic methods (FTIR, Si and C CP MAS NMR), porous structure and elemental analysis, and zeta potential measurement. A determination of catalytic activity was made based on the deacetylation reaction of N-acetyl-l-methionine. Furthermore, the effect of pH and temperature on the catalytic activity of the free and immobilized enzyme, as well as the reusability of the silica-bound aminoacylase, were determined. The immobilized systems demonstrated a high degree of catalytic activity. The best catalytic parameters were those of aminoacylase immobilized on silica modified with APTES (apparent activity 3937 U/g, relative activity 61.6%). © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:767-777, 2018.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino‐ and carbonyl‐grafted stöber silica

Kołodziejczak-Radzimska

Zdarta

Jesionowski

2018

Biotechnology Progress

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“…This fact may be related to the structure of the amino acids used. In the literature, besides the standard derivative of methionine, N-acetyl-l-theanine has also been used to determine the enzymatic activity of immobilized aminoacylase (Li et al 2015). In that study the immobilized aminoacylase (on electrospun nanofibrous membrane) had a relative activity of 50%.…”

Section: Physicochemical Characterization Of Supports and Biocatalytimentioning

confidence: 99%

A novel biocatalytic system obtained via immobilization of aminoacylase onto sol–gel derived ZrO2·SiO2 binary oxide material: physicochemical characteristic and catalytic activity study

Kołodziejczak-Radzimska

Ciesielczyk

Jesionowski

2019

Adsorption

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Oxide material of a new type, ZrO 2 ·SiO 2 (raw and carbonyl-grafted), was used as support in the immobilization of aminoacylase from Aspergillus melleus. The ZrO 2 ·SiO 2 was synthesized via sol-gel method. The obtained material was additionally modified with glutaraldehyde. Various physicochemical analyses were used to confirm the effectiveness of the modification and immobilization processes, including Fourier transform infrared spectroscopy, laser Doppler velocimetry and lowtemperature N 2 sorption. The immobilization process was performed within 3 h using different concentrations of enzyme solution (1, 3, 5 and 7 mg/mL), and the Bradford method was used to determine the quantity of immobilized enzyme. The resulting biocatalytic systems were then used as catalysts in the hydrolysis of different N-acetyl-dl-amino acids (leading to l-methionine, l-cysteine, l-serine and l-tryptophan). Based on this reaction the apparent and relative catalytic activities were determined. The highest activity of the immobilized enzyme was attained in the synthesis of l-methionine (the apparent activities of aminoacylase immobilized on raw and carbonyl-grafted ZrO 2 ·SiO 2 were 4112 and 4947 U/g, respectively). Furthermore, the effect of pH and temperature on catalytic activity, as well as the storage stability and reusability of the prepared biocatalytic systems were determined. Aminoacylase immobilized on carbonyl-grafted ZrO 2 ·SiO 2 retains 85% of its initial activity after 30 days of storage and 70% after five reaction cycles.

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The use of immobilized enzymes to improve functionality

Hettiarachchy

Feliz²,

Edwards

et al. 2018

Proteins in Food Processing

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Immobilization of aminoacylase on electrospun nanofibrous membrane for the resolution of dl-theanine

Cited by 8 publications

References 31 publications

Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino‐ and carbonyl‐grafted stöber silica

Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino‐ and carbonyl‐grafted stöber silica

A novel biocatalytic system obtained via immobilization of aminoacylase onto sol–gel derived ZrO2·SiO2 binary oxide material: physicochemical characteristic and catalytic activity study

The use of immobilized enzymes to improve functionality

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