Preparation of Carriers Based on ZnO Nanoparticles Decorated on Graphene Oxide (GO) Nanosheets for Efficient Immobilization of Lipase from Candida rugosa

Zhang, Shan; Shi, Jie; Deng, Qianchun; Zheng, Minghui; Wan, Chuyun; Chang, Zheng; Li, Ya; Huang, Fenghong

doi:10.3390/molecules22071205

Cited by 26 publications

(21 citation statements)

References 44 publications

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“…The 2.0 MK possesses larger pore size than the 2.0 NK, which is why better endurance can be observed when CRL-2.0 MK was in continuous use. This is in agreement with the findings by most researchers, that support materials with larger pore sizes are usually better carriers in promoting better enzyme reusabilities [18,67,68]. This clearly suggests that organo-modified metakaolin was able to better entrap lipase and retain its catalytic activity even after several uses, as compared to organo-modified kaolin.…”

Section: Reusability Of Immobilized Lipasessupporting

confidence: 92%

Comparative Study on Lipase Immobilized onto Organo-Cation Exchanged Kaolin and Metakaolin: Surface Properties and Catalytic Activity

Elgubbi

Othman

Harun

2021

Bull. Chem. React. Eng. Catal.

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Clay mineral has received much attention to be used as biocatalysts as it is cheaper, easily available and environmentally friendly. However, the use of unmodified clay, in particular kaolin for enzyme immobilization showed unsuitability of this support due to its negative charge. In this study, the hydrophobic properties of kaolin and metakaolin (kaolin heated to 650 °C) were adjusted by the intercalation with benzyltriethylammonium chloride (BTEA-Cl), at concentrations 2.0 times the cation exchange capacities (CEC) of the clays. The supports were then used for immobilization of lipase from Candida rugosa (CRL). From the study, the highest percentage of lipase immobilization was achieved (70.14%), when organo-modified metakaolin (2.0 MK) was used. The supports as well as the immobilized biocatalysts were then characterized by X-ray diffraction, Fourier transform infrared spectroscopy, scanning electron microscopy, and nitrogen adsorption techniques. Comparisons of the efficiencies of immobilized with free CRL in the synthesis of nonyl hexanoate showed that immobilized CRL achieved enzymatic activities of between 5.24×10−3 to 3.63×10−3 mmol/min/mg, while free CRL achieved enzymatic activity of 3.27×10−3 mmol/min/mg after 5 h of reaction at 30 ℃. The immobilized CRLs also maintained 70.81% – 80.59% thermostabilities at 70 ℃ as compared to the free CRL (28.13%). CRL immobilized on 2.0 NK and 2.0 MK also maintained 38.54% and 62.56%, respectively, of the initial activities after 10 continuous cycles, showing the excellent stability and reusability of the immobilized lipases, suitable as substitute for expensive, hazardous catalysts used in industries. Copyright © 2021 by Authors, Published by BCREC Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).

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Section: Reusability Of Immobilized Lipasessupporting

confidence: 92%

Comparative Study on Lipase Immobilized onto Organo-Cation Exchanged Kaolin and Metakaolin: Surface Properties and Catalytic Activity

Elgubbi

Othman

Harun

2021

Bull. Chem. React. Eng. Catal.

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“…1B , which were considered to be the agglomerate shape of CRL consistent with previous reports, and proved that CRL was bonded with C 3 N 4 -NS. 9 This point could be confirmed by the nitrogen adsorption–desorption isotherm observations of C 3 N 4 -NS and C 3 N 4 -NS@CRL in Fig. 1C .…”

Section: Resultssupporting

confidence: 69%

“…In addition, the TGA curve of CRL showed two major weight loss steps at 80 °C and 260 °C. The weight loss onset around 80 °C indicated the evaporation of absorbed water, while the decomposition at 260 °C could be accredited to denaturation of the CRL structure, 9 compared with the TGA curve of free CRL. It is worth noting that both C 3 N 4 -NS and C 3 N 4 -NS@CRL showed no obvious weight loss (less than 4%) from 80 °C to 300 °C, which could prove the enhanced thermostability of C 3 N 4 -NS@CRL when CRL was immobilized on the C 3 N 4 -NS.…”

Section: Resultsmentioning

confidence: 99%

Candida rugosa lipase covalently immobilized on facilely-synthesized carbon nitride nanosheets as a novel biocatalyst

Ruan

Zheng

et al. 2018

RSC Adv.

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The immobilization of lipase on solid supports provides a significant improvement to the stability and reusability of lipase. During immobilization, the restricted surface area and inferior separation capacity of matrix materials are crucial for obtaining high-quality immobilized lipase. Carbon nitride nanosheets (C 3 N 4 -NS) as a type of two-dimensional nanomaterial have attracted various attentions for their prominent 2D planar nanostructure, characteristic surface area, thermostability and biocompatibility.Herein, we report a rational design and fabrication of immobilized Candida rugosa lipase based on pH-flexibility, thermostability (after 180 min at 50 C, 67% of the initial activity remained) and recyclability (after 10 runs, 72% of the initial activity remained). When compared with the free CRL, all experimental data indicate that C 3 N 4 -NS@CRL exhibited improved stability and enhanced practicability. To our knowledge, this is the first report of the application of carbon nitride nanosheets to enzyme immobilization.

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“…A number of suggested lipase immobilization techniques [18], including covalent bonding [19], entrapment [20,21] and physical adsorption [22][23][24][25] with different supports, have assorted advantages and disadvantages to make a comparison difficult. Encapsulating lipase has the drawbacks of mass transfer limitations and low enzyme loading, while strong covalent attachment may cause lipase to be irreversibly deactivated to some extent [4].…”

Section: Introductionmentioning

confidence: 99%

Novel amphiphilic polyvinylpyrrolidone functionalized silicone particles as carrier for low-cost lipase immobilization

Zhang¹,

Deng²,

Li³

et al. 2018

R. Soc. open sci.

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The high catalytic activity, specificity and stability of immobilized lipase have been attracting great interest. How to reduce the cost of support materials has always been a hot topic in this field. Herein, for the development of low-cost immobilized lipase, we demonstrate an amphiphilic polyvinylpyrrolidone (PVP) grafted on silicone particle (SP) surface materials (SP-PVP) with a rational design based on interfacial activation and solution polymerization. Meanwhile, hydrophilic pristine SP and hydrophobic polystyrene-corded silicone particles (SP-Pst) were also prepared for lipase immobilization. SP-PVP was characterized by X-ray diffraction, scanning electron microscopy, X-ray photoelectron spectroscopy, Fourier transform infrared spectroscopy and thermogravimetry. Our results indicated that the lipase loading amount on the SP-PVP composites was about 215 mg of protein per gram. In the activity assay, the immobilized lipase SP-PVP@CRL exhibited higher catalysis activity and better thermostability and reusability than SP@CRL and SP-Pst@CRL. The immobilized lipase retained more than 54% of its initial activity after 10 times of re-use and approximately trended to a steady rate in the following cycles. By introducing the interesting amphiphilic polymer to this cheap and easily obtained SP surface, the relative performance of the immobilized lipase can be significantly improved, facilitating interactions between the low-cost support materials and lipase.

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Preparation of Carriers Based on ZnO Nanoparticles Decorated on Graphene Oxide (GO) Nanosheets for Efficient Immobilization of Lipase from Candida rugosa

Cited by 26 publications

References 44 publications

Comparative Study on Lipase Immobilized onto Organo-Cation Exchanged Kaolin and Metakaolin: Surface Properties and Catalytic Activity

Comparative Study on Lipase Immobilized onto Organo-Cation Exchanged Kaolin and Metakaolin: Surface Properties and Catalytic Activity

Candida rugosa lipase covalently immobilized on facilely-synthesized carbon nitride nanosheets as a novel biocatalyst

Novel amphiphilic polyvinylpyrrolidone functionalized silicone particles as carrier for low-cost lipase immobilization

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