Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability

Zeyadi, Mustafa; Almulaiky, Yaaser Q.

doi:10.1016/j.heliyon.2023.e21169

Cited by 10 publications

(1 citation statement)

References 48 publications

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“…To increase the viability of employing enzymes in industrial applications, several efforts have focused on enhancing their stability. Directed evolution, site-directed mutagenesis, enzyme fusion, surface display, and enzyme immobilization are just a few of the approaches utilized to enhance the capabilities of enzymes [6,7]. Among these strategies, enzyme immobilization on solid supports is considered the most successful for enhancing enzyme activity, affinity, selectivity, and stability [8].…”

Section: Introductionmentioning

confidence: 99%

Sustainable Immobilization of β-Glucosidase onto Silver Ions and AgNPs-Loaded Acrylic Fabric with Enhanced Stability and Reusability

Almulaiky,

Alkabli,

El-Shishtawy

2023

Polymers

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Modified polymer design has attracted significant attention for enzyme immobilization, offering promising applications. In this study, amine-terminated polymers were synthesized by incorporating functional groups into polyacrylonitrile using hexamethylenediamine. This work highlights the successful enzyme immobilization strategy using modified polymers, offering improved stability and expanded operational conditions for potential biotechnological applications. The resulting amino groups were utilized to capture silver ions, which were subsequently converted to silver nanoparticles (AgNPs). The obtained materials, AgNPs@TA-HMDA (acrylic textiles coated silver nanoparticles AgNPs) and Ag(I)@TA-HMDA (acrylic textiles coated with Ag ion) were employed as supports for β-glucosidase enzyme immobilization. The highest immobilization yields (IY%) were achieved with AgNPs@TA-HMDA at 92%, followed by Ag(I)@TA-HMDA at 79.8%, resulting in activity yields (AY%) of 81% and 73%, respectively. Characterization techniques such as FTIR, FE-SEM, EDX, TG/DTG, DSC, and zeta potential were employed to investigate the structural composition, surface morphologies, elemental composition, thermal properties, and surface charge of the support materials. After 15 reuses, the preservation percentages decreased to 76% for AgNPs@TA-HMDA/β-Glu and 65% for Ag(I)@TA-HMDA/β-Glu. Storage stability revealed that the decrease in activity for the immobilized enzymes was smaller than the free enzyme. The optimal pH for the immobilized enzymes was broader (pH 5.5 to 6.5) compared to the free enzyme (pH 5.0), and the optimal temperature for the immobilized enzymes was 60 °C, slightly higher than the free enzyme’s optimal temperature of 50 °C. The kinetic analysis showed a slight increase in Michaelis constant (Km) values for the immobilized enzymes and a decrease in maximum velocity (Vmax), turnover number (Kcat), and specificity constant (Kcat/Km) values compared to the free enzyme. Through extensive characterization, we gained valuable insights into the structural composition and properties of the modified polymer supports. This research significantly contributes to the development of efficient biotechnological processes by advancing the field of enzyme immobilization and offering valuable knowledge for its potential applications.

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Section: Introductionmentioning

confidence: 99%

Sustainable Immobilization of β-Glucosidase onto Silver Ions and AgNPs-Loaded Acrylic Fabric with Enhanced Stability and Reusability

Almulaiky,

Alkabli,

El-Shishtawy

2023

Polymers

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Magnetically separable spent coffee grounds as a potential novel support for the covalent immobilization of β‐glucosidase for cellobiose hydrolysis

Bhardwaj,

Mishra,

Ghosh

et al. 2024

J of Chemical Tech & Biotech

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BACKGROUNDThe industrial‐scale application of enzymes faces obstacles due to elevated costs and difficulties in stability and reuse. In this study, magnetic spent coffee grounds, an ecotoxic waste, have been utilized successfully for the first time to immobilize β‐glucosidase to overcome these challenges.RESULTSThe spent coffee grounds were magnetized and amine‐functionalized, followed by characterization using various techniques. Under optimized conditions, forming an imine bond between the functionalized support and β‐glucosidase resulted in a 62% immobilization yield (92.81 mg g−1 enzyme loading) and 12.5 U mg−1 activity after immobilization. A relatively small kinetic change was observed in the Km value (902 to 946 μmol L−1) after immobilization, suggesting minimal hindrance by AMSCG3 on substrate access or product release. Moreover, Glu@AMSCG3 showed exceptional stability (>90% residual activity) within a pH range of 3 to 6 after 2 h of incubation at 25 °C. A residual activity of 87.94% was maintained even at 80 °C and pH 5 after 2 h of incubation compared to the free β‐glucosidase, which showed only 6.5% residual activity at the same temperature. When cellobiose was hydrolyzed using Glu@AMSCG3 under optimum conditions, 91.33% cellobiose conversion was achieved initially, and over 79% conversion was maintained for 10 reusability cycles.CONCLUSIONThe improved stability of β‐glucosidase after covalent immobilization on amine‐modified magnetically separable spent coffee grounds indicates their potential as a support matrix for application in enzyme immobilization. © 2024 Society of Chemical Industry (SCI).

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Aptamer Encapsulated Inside the Array Channel of Ni‐MOF for Bisphenol A Determination in Multi‐interference System

Zhang,

Yan

et al. 2024

ChemistrySelect

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As an endocrine disruptor, bisphenol A (BPA) has many adverse effects on environmental safety and human health. Aiming at the existing problems at the current detection methods, herein, a 3D metal‐organic framework (Ni‐MOF) was fabricated as a carrier to achieve BPA aptamers immobilization inside its array channels under Mg2+ regulation. Based on the reversible quenching of 6‐FAM (6‐carboxyfluorescein) fluorescence labeled on the BPA aptamers during the encapsulation process, a fluorescent aptamer sensing platform was constructed for the quantitative detection of BPA in water. Morphology analysis, VASP (Vienna ab‐initio simulation package) and other kinetic simulations were performed to elaborate the mechanism of the influence of pore size, medium ions, etc. on the recognition process. Due to the in‐hole fixation strategy of aptamers, Ni‐MOF played an obvious protection aptamers. Not only the activity of BPA aptamer@MOF composite was maintained more than 50 % in complex environments such as pH 3.0–11.0, 30–70 °C and organic solvents, but also the aptamer was protected from nuclease hydrolysis under physiological conditions. The stability and application range of the sensor are greatly improved, detection limit of 0.34 μM. The result was expected to provide theoretical guidance for the rapid detection of pollutants in complex environments.

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Chitosan‐Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability

Cited by 10 publications

References 48 publications

Sustainable Immobilization of β-Glucosidase onto Silver Ions and AgNPs-Loaded Acrylic Fabric with Enhanced Stability and Reusability

Sustainable Immobilization of β-Glucosidase onto Silver Ions and AgNPs-Loaded Acrylic Fabric with Enhanced Stability and Reusability

Magnetically separable spent coffee grounds as a potential novel support for the covalent immobilization of β‐glucosidase for cellobiose hydrolysis

Aptamer Encapsulated Inside the Array Channel of Ni‐MOF for Bisphenol A Determination in Multi‐interference System

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