Characterization of β-glucosidase immobilized on chitosan-multiwalled carbon nanotubes (MWCNTS) and their application on tea extracts for aroma enhancement

Çelik, Akile; Dinçer, Ayşe; Aydemir, Tülin

doi:10.1016/j.ijbiomac.2016.05.008

Cited by 55 publications

(15 citation statements)

References 35 publications

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“…However, the V max value of the free Tm-β-Glu was 31.06 U mg −1 protein, whereas the V max value of the immobilized enzyme was 26.67 U mg −1 protein, which can be noticed in Table 2. Çelik et al found that the K m and V max values of the free enzyme was 2.04 mM and 5.12 U mg −1 ; but the K m value increased to 5.55 mM, and the V max value increased to 7.14 U mg −1 after the immobilization of β-Glu on MNPs while utilizing pNPG as a synthetic substrate 32 .…”

Section: Storage Stability Of Free and Immobilized Tm-β-glu-tt-chbd mentioning

confidence: 99%

Immobilization of β-Glucosidase from Thermatoga maritima on Chitin-functionalized Magnetic Nanoparticle via a Novel Thermostable Chitin-binding Domain

Alnadari

Xue

Zhou

et al. 2020

Sci Rep

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Enzyme immobilization is a powerful tool not only as a protective agent against harsh reaction conditions but also for the enhancement of enzyme activity, stability, reusability, and for the improvement of enzyme properties as well. Herein, immobilization of β-glucosidase from Thermotoga maritima (tm-β-Glu) on magnetic nanoparticles (Mnps) functionalized with chitin (ch) was investigated. This technology showed a novel thermostable chitin-binding domain (Tt-ChBD), which is more desirable in a wide range of large-scale applications. This exclusive approach was fabricated to improve the Galacto-oligosaccharide (GOS) production from a cheap and abundant by-product such as lactose through a novel green synthesis route. Additionally, SDS-PAGE, enzyme activity kinetics, transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FT-IR) revealed that among the immobilization strategies for Thermotoga maritime-β-Glucosidase thermostable chitinbinding domain (tm-β-Glu-Tt-ChBD) on the attractive substrate; Ch-MNPs had the highest enzyme binding capacity and GOS production ratio when compared to the native enzyme. More interestingly, a magnetic separation technique was successfully employed in recycling the immobilized Tm-β-Glu for repetitive batch-wise GOS without significant loss or reduction of enzyme activity. This immobilization system displayed an operative stability status under various parameters, for instance, temperature, pH, thermal conditions, storage stabilities, and enzyme kinetics when compared with the native enzyme. Conclusively, the GOS yield and residual activity of the immobilized enzyme after the 10 th cycles were 31.23% and 66%, respectively. Whereas the GOS yield from native enzyme synthesis was just 25% after 12 h in the first batch. This study recommends applying Tt-ChBD in the immobilization process of tm-β-Glu on Ch-MNPs to produce a low-cost GOS as a new eco-friendly process besides increasing the biostability and efficiency of the immobilized enzyme.

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Section: Storage Stability Of Free and Immobilized Tm-β-glu-tt-chbd mentioning

confidence: 99%

Immobilization of β-Glucosidase from Thermatoga maritima on Chitin-functionalized Magnetic Nanoparticle via a Novel Thermostable Chitin-binding Domain

Alnadari

Xue

Zhou

et al. 2020

Sci Rep

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“…These enzymes constitute a significant group among glycoside hydrolases, and the possibility of their use in various biotechnological processes has been intensely explored. Considering industrial applications, β -glucosidases are currently used in: production of biodegradable nonionic surfactants and other compounds [ 8 ]; synthesis of diverse oligosaccharides, glycoconjugates, alkyl- and amino-glycosides [ 5 ]; detoxification of cassava [ 9 ]; removal of cyanogenic glucosides from sorghum malt used in the production of African beer [ 10 ]; enzymatic release of aroma compounds from glucosidic precursors present in fruit juices during winemaking [ 11 ]; enhancement of tea extracts aroma [ 12 ], among others. These enzymes can play a critical role in the generation of potentially sustainable energy sources (e.g., glucose, ethanol, hydrogen, and methane) from biomass conversion [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Penicillium citrinum UFV1 β-glucosidases: purification, characterization, and application for biomass saccharification

Costa

Pereira

Teixeira-Ferreira

et al. 2018

Biotechnol Biofuels

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Backgroundβ-Glucosidases are components of the cellulase system, a family of enzymes that hydrolyze the β-1,4 linkages of cellulose. These proteins have been extensively studied due to the possibility of their use in various biotechnological processes. They have different affinities for substrates (depending on their source) and their activities can be used for saccharification of different types of biomass. In this context, the properties and the synergistic capacity of β-glucosidases from different organisms, to supplement the available commercial cellulase cocktails, need a comprehensive evaluation.ResultsTwo β-glucosidases belonging to GH3 family were secreted by Penicillium citrinum UFV. PcβGlu1 (241 kDa) and PcβGlu2 (95 kDa) presented acidic and thermo-tolerant characteristics. PcβGlu1 showed Michaelis–Menten kinetics for all substrates tested with Km values ranging from 0.09 ± 0.01 (laminarin) to 1.7 ± 0.1 mM (cellobiose, C2) and kcat values ranging from 0.143 ± 0.005 (laminarin) to 8.0 ± 0.2 s−1 (laminaribiose, Lb). PcβGlu2 showed substrate inhibition for 4-methylumbelliferyl-β-d-glucopyranoside (MUβGlu), p-nitrophenyl-β-d-glucopyranoside (pNPβGlu), cellodextrins (C3, C4, and C5), N-octil-β-d-glucopyranoside, and laminaribiose, with Km values ranging from 0.014 ± 0.001 (MUβGlu) to 0.64 ± 0.06 mM (C2) and kcat values ranging from 0.49 ± 0.01 (gentiobiose) to 1.5 ± 0.2 s−1 (C4). Inhibition constants (Ki) for PcβGlu2 substrate inhibition ranged from 0.69 ± 0.07 (MUβGlu) to 10 ± 1 mM (Lb). Glucose and cellobiose are competitive inhibitors of PcβGlu1 and PcβGlu2 when pNPβGlu is used as a substrate. For PcβGlu1 inhibition, Ki = 1.89 ± 0.08 mM (glucose) and Ki = 3.8 ± 0.1 mM (cellobiose); for PcβGlu2, Ki = 0.83 ± 0.05 mM (glucose) and Ki = 0.95 ± 0.07 mM (cellobiose). The enzymes were tested for saccharification of different biomasses, individually or supplementing a Trichoderma reesei commercial cellulose preparation. PcβGlu2 was able to hydrolyze banana pseudostem and coconut fiber with the same efficiency as the T. reesei cocktail, showing significant synergistic properties with T. reesei enzymes in the hydrolysis of these alternative biomasses.ConclusionsThe β-glucosidases from P. citrinum UFV1 present different enzymatic properties from each other and might have potential application in several biotechnological processes, such as hydrolysis of different types of biomass.Electronic supplementary materialThe online version of this article (10.1186/s13068-018-1226-5) contains supplementary material, which is available to authorized users.

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“…A lot of researchers have focused on β ‐glucosidase immobilization. Recently, β ‐glucosidase was immobilized on chitosan‐multiwalled carbon nanotubes and nanoscale latex and silicone polymeric thin films , to enhance the aroma in different tea samples. Glucoamylase was also immobilized on SiO 2 nanoparticles to improve the sugarcane juice properties.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of β‐Glucosidase BglC on Decanedioic Acid‐Modified Magnetic Nanoparticles

Wang

et al. 2018

Chem Eng & Technol

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β‐Glucosidase BglC from Thermobifida fusca was efficiently immobilized on decanedioic acid‐modified magnetic nanoparticles (DMNP). Interestingly, the immobilized BglC showed much higher organic solvent stability than the free enzyme, indicating that this enzyme immobilized on DMNP should be especially suitable for catalyzing reactions in organic solvents. Additionally, the immobilized BglC also showed better thermal stability, storage stability, and mechanical stability than the free counterpart. Moreover, the reuse times were satisfactory and even crude plant materials (e.g., rice husk and corn cob) were used as substrates, which should be valuable for the decomposition of natural organic materials and the full utilization of bioresources.

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Characterization of β-glucosidase immobilized on chitosan-multiwalled carbon nanotubes (MWCNTS) and their application on tea extracts for aroma enhancement

Cited by 55 publications

References 35 publications

Immobilization of β-Glucosidase from Thermatoga maritima on Chitin-functionalized Magnetic Nanoparticle via a Novel Thermostable Chitin-binding Domain

Immobilization of β-Glucosidase from Thermatoga maritima on Chitin-functionalized Magnetic Nanoparticle via a Novel Thermostable Chitin-binding Domain

Penicillium citrinum UFV1 β-glucosidases: purification, characterization, and application for biomass saccharification

Immobilization of β‐Glucosidase BglC on Decanedioic Acid‐Modified Magnetic Nanoparticles

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