Covalent immobilization of cellulase in application of biotransformation of ginsenoside Rb1

Yuan, Ying; Luan, Xiaoning; Rana, XiaoKu; Dou, Deqiang

doi:10.1016/j.molcatb.2017.05.004

Cited by 30 publications

(15 citation statements)

References 19 publications

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“…From these data, it was revealed that the processes of amination, activation, and immobilization were successful. These results were in agreement with the results obtained by other published results (Yuan et al 2016). Díaz-Hernández et al (2018) reported that the change in intensity as well as the displacement of the NH 2 , C-O, and Fe bands after cross-linking suggests the formation of covalent bonds between enzymes and the magnetic beads.…”

Section: Discussionsupporting

confidence: 93%

“…3. The reaction happened between the NH 2 group found in the enzyme protein molecule and the free C=O group located on GA (the cross-linker) forming C=N-bond as reported by Yuan et al (2016). Magnetic nano-particles have unique properties as high affinity to proteins and ability to be chemically modified with reactive functional groups (Atacan et al 2016).…”

Section: Discussionmentioning

confidence: 90%

“…After that, the polymer solution was sprayed into cross-linking solution of NaOH 5% (w/v), through a nozzle of 300 μm using the Inotech Encapsulator. The prepared beads were hardened in cross-linking solutions for 3 h. To modify the gel beads for covalent immobilization of enzyme, the gel beads were soaked in a solution of 4% (v/v) polyethylenimine (PEI) at pH 9.5 for 3 h, followed by soaking in glutaraldehyde (GA) 2.5% for 3 h, and after washing, the gel beads was ready for immobilization (Yuan et al 2016).…”

Section: Preparation Of Chitosan-magnetic Nano-particles (Ch-mnp) Beadsmentioning

confidence: 99%

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Statistical optimization of chemical modification of chitosan-magnetic nano-particles beads to promote Bacillus subtilis MK1 α-amylase immobilization and its application

et al. 2020

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Background: α-Amylase randomly hydrolyzes starch molecule to produce oligosaccharides of different chain length. It is among the most significant hydrolytic enzymes used in industrial applications. Enzyme immobilization is the simplest way to solve the stability problem of protein under industrial harsh conditions. Magnetic nano-particles considered suitable for immobilization due to their unique characteristics. The polymer nanocarriers still the feature of modifiable surfaces of carriers for further conjugation with biomolecule. This study aims to promote the immobilization of Bacillus subtilis MK1 α-amylase using the statistical optimization of the chemical modification of the chitosan-magnetic nano-magnetic particle beads and their ability to apply. Results: B. subtilis MK1 α-amylase was successfully immobilized on chitosan-magnetic nano-particles using a method combining the advantages of both physical adsorption and covalent binding. The beads were chemically modified using polyethyleneimine (PEI) followed by glutaraldehyde (GA). Aminated beads by (PEI), activated beads by (GA), and immobilized enzyme on activated beads were characterized using FTIR. Morphological examinations of the beads surface before and after conjugation with the α-amylase enzyme were carried out using scanning electron microscope (SEM). Chemical modification parameters of the beads were optimized using response surface methodology based on central composite design. Statistical approach enhanced the immobilization yield (IY%) by 1.5-fold. The application of immobilized enzyme in the baking process enhanced dough-raising about 2.3-fold and can be reused for 5 cycles with 100% activity. Conclusions: Statistical methods are an important way to improve immobilization yield and efficiency. The ANOVA data confirmed the fitness of the model which possessed R 2 value (0.975) and the adjusted R 2 value (0.940). The results confirm the ability to reuse the immobilized enzyme in industrial processes.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 90%

Section: Preparation Of Chitosan-magnetic Nano-particles (Ch-mnp) Beadsmentioning

confidence: 99%

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Statistical optimization of chemical modification of chitosan-magnetic nano-particles beads to promote Bacillus subtilis MK1 α-amylase immobilization and its application

et al. 2020

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“…Highest pH tolerance, either in acidic or more alkaline pH values, was observed when γFe was used as immobilization support. The increased pH stability of the enzyme might be due to its covalent bonding to the support (Yuan et al, 2016).…”

Section: Effect Of Temperature and Ph On The Activity Of Immobilized Bglmentioning

confidence: 99%

Hybrid Nanomaterials of Magnetic Iron Nanoparticles and Graphene Oxide as Matrices for the Immobilization of β-Glucosidase: Synthesis, Characterization, and Biocatalytic Properties

et al. 2018

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Hybrid nanostructures of magnetic iron nanoparticles and graphene oxide were synthesized and used as nanosupports for the covalent immobilization of β-glucosidase. This study revealed that the immobilization efficiency depends on the structure and the surface chemistry of nanostructures employed. The hybrid nanostructure-based biocatalysts formed exhibited a two to four-fold higher thermostability as compared to the free enzyme, as well as an enhanced performance at higher temperatures (up to 70 • C) and in a wider pH range. Moreover, these biocatalysts retained a significant part of their bioactivity (up to 40%) after 12 repeated reaction cycles.

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“…This improved pH-stability may be because of the covalent bond formed and possible secondary interactions between the enzyme and the functional groups of the carrier, which enhance the stability of the molecular structure of the immobilized enzyme at various pH values [26]. This behavior could be explained by influence of the partition effects on the enzymatic activities of the immobilized protein, which were from different concentrations of charged species in the micro-environment of the immobilized protein and reaction solution [27].…”

Section: Effect Of Ph On the Activity Of Hsph Zz And Immhsph Zzmentioning

confidence: 99%

Highly Efficient Synthesis of 2,5-Dihydroxypyridine using Pseudomonas sp. ZZ-5 Nicotine Hydroxylase Immobilized on Immobead 150

et al. 2018

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In this report, the use of immobilized nicotine hydroxylase from Pseudomonas sp. ZZ-5 (HSPHZZ) for the production of 2,5-dihydroxypyridine (2,5-DHP) from 6-hydroxy-3-succinoylpyridine (HSP) in the presence of nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FAD) is described. HSPHZZ was covalently immobilized on Immobead 150 (ImmHSPHZZ). ImmHSPHZZ (obtained with 5–30 mg of protein per gram of support) catalyzed the hydrolysis of HSP to 2,5-DHP. At a protein loading of 15 mg g−1, ImmHSPHZZ converted 93.6% of HSP to 2,5-DHP in 6 h. The activity of ImmHSPHZZ was compared with that of free HSPHZZ under various conditions, including pH, temperature, enzyme concentration, substrate concentration and stability over time, and kinetic parameters were measured. The results showed that ImmHSPHZZ performed better over wider ranges of pH and temperature when compared with that of HSPHZZ. The optimal concentrations of ImmHSPHZZ and substrate were 30 mg L−1 and 0.75 mM, respectively. Under optimal conditions, 94.5 mg L−1 of 2,5-DHP was produced after 30 min with 85.4% conversion. After 8 reaction cycles and 6 days of storage, 51.3% and 75.0% of the initial enzyme activity remained, respectively. The results provide a framework for development of commercially suitable immobilized enzymes that produce 2,5-DHP.

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Covalent immobilization of cellulase in application of biotransformation of ginsenoside Rb1

Cited by 30 publications

References 19 publications

Statistical optimization of chemical modification of chitosan-magnetic nano-particles beads to promote Bacillus subtilis MK1 α-amylase immobilization and its application

Statistical optimization of chemical modification of chitosan-magnetic nano-particles beads to promote Bacillus subtilis MK1 α-amylase immobilization and its application

Hybrid Nanomaterials of Magnetic Iron Nanoparticles and Graphene Oxide as Matrices for the Immobilization of β-Glucosidase: Synthesis, Characterization, and Biocatalytic Properties

Highly Efficient Synthesis of 2,5-Dihydroxypyridine using Pseudomonas sp. ZZ-5 Nicotine Hydroxylase Immobilized on Immobead 150

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