CFD Simulations of Microreactors for the Hydrolysis of Cellobiose to Glucose by β-Glucosidase Enzyme

Venezia, Virginia; Califano, Valeria; Pota, Giulio; Costantini, A.; Landi, Gianluca; Benedetto, Almerinda Di

doi:10.3390/mi11090790

Cited by 9 publications

(4 citation statements)

References 31 publications

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“…With this enzymatic multi-channel microreactor, we achieved a p-NP production of 0.074 µmol/min, which is 4.6-fold higher than that observed in the single-channel microreactor (0.016 µmol/min for the single-channel microreactor). It is worth noting that further optimization of the enzymatic microreactor performance could be achieved through CFD simulations as indicated in the work of Venezia et al regarding β-glucosidase [59].…”

Section: Development Of a Multi-channel Microreactormentioning

confidence: 99%

Biocatalytic Performance of β-Glucosidase Immobilized on 3D-Printed Single- and Multi-Channel Polylactic Acid Microreactors

Vasios,

Skonta,

Patila

et al. 2024

Micromachines

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Microfluidic devices have attracted much attention in the current day owing to the unique advantages they provide. However, their application for industrial use is limited due to manufacturing limitations and high cost. Moreover, the scaling-up process of the microreactor has proven to be difficult. Three-dimensional (3D) printing technology is a promising solution for the above obstacles due to its ability to fabricate complex structures quickly and at a relatively low cost. Hence, combining the advantages of the microscale with 3D printing technology could enhance the applicability of microfluidic devices in the industrial sector. In the present work, a 3D-printed single-channel immobilized enzyme microreactor with a volume capacity of 30 μL was designed and created in one step via the fused deposition modeling (FDM) printing technique, using polylactic acid (PLA) as the printing material. The microreactor underwent surface modification with chitosan, and β-glucosidase from Thermotoga maritima was covalently immobilized. The immobilized biocatalyst retained almost 100% of its initial activity after incubation at different temperatures, while it could be effectively reused for up to 10 successful reaction cycles. Moreover, a multi-channel parallel microreactor incorporating 36 channels was developed, resulting in a significant increase in enzymatic productivity.

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Section: Development Of a Multi-channel Microreactormentioning

confidence: 99%

Biocatalytic Performance of β-Glucosidase Immobilized on 3D-Printed Single- and Multi-Channel Polylactic Acid Microreactors

Vasios,

Skonta,

Patila

et al. 2024

Micromachines

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“…The release of glucose by β-glucosidases is vital because glucose is a treasure trove of energy and a crucial building block for the synthesis of biofuels. It has been demonstrated that immobilizing β-glucosidases on appropriate substrates enhances their catalytic activity, which may have consequences for a range of industrial uses, such as the generation of biofuel [41], [42], [43].…”

Section: Endoglucanases and Exoglucanasesmentioning

confidence: 99%

Enzymatic hydrolysis in food processing: biotechnological advancements, applications, and future perspectives

Akimova,

Kakimov,

Suychinov

et al. 2024

Potr. S. J. F. Sci.

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In food processing, enzymatic hydrolysis has become a revolutionary biotechnological instrument that provides consistency and sustainability that are unmatched by traditional techniques. This work thoroughly analyzes current developments in enzymatic hydrolysis and examines its uses in various food processing contexts. The biotechnological aspects—such as substrate specificity, enzyme engineering, and sustainable process optimization—are the main focus. The historical background and development of enzymatic hydrolysis in food processing are explored at the study's outset, highlighting the process's transformation from a specialized use to a critical component of contemporary biotechnological food production. A thorough literature review underscores the specificity of enzymes in dissolving various dietary components, offering insights into the biotechnological nuances controlling substrate-enzyme interactions. A careful examination of the many enzymes used in enzymatic hydrolysis and a full assessment of their uses and specificities are provided. Enzymatic hydrolysis selection criteria are outlined, taking regulatory compliance, thermostability, pH sensitivity, and substrate specificity into account. The integration of enzymatic hydrolysis into workflows for food processing is also covered, focusing on compatibility with current infrastructure and processing parameters. The case studies that demonstrate the effective use of enzymatic hydrolysis in various food production situations are the core of the research. These examples illustrate the adaptability and effectiveness of enzymatic processes in improving food quality, from developing gluten-free products to optimizing fermentation in baked goods. In its futuristic conclusion, the article imagines how enzymatic hydrolysis will continue to influence food processing in the years to come. The biotechnological viewpoint strongly emphasizes current research directions, such as integrating enzymatic processes into sustainable food production techniques and engineering enzymes for increased specificity. This biotechnological investigation highlights how enzymatic hydrolysis may completely change the food processing industry by providing accuracy, sustainability, and creativity in pursuing wholesome, nutrient-dense, and aesthetically pleasing food items.

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“…Optimal operating conditions and appropriate reactor design, integrating kinetic parameters, can be computationally guided to avoid time‐consuming and expensive experiments. Several examples of model‐based design optimization methods have been published [95–98] …”

Section: Immobilized Enzyme Reactors: a Portfolio Of Optionsmentioning

confidence: 99%

Wall‐Immobilized Biocatalyst vs. Packed Bed in Miniaturized Continuous Reactors: Performances and Scale‐Up

Michaud,

Nonglaton,

Anxionnaz‐Minvielle

2024

ChemBioChem

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Sustainable biocatalysis syntheses have gained considerable popularity over the years. However, further optimizations – notably to reduce costs – are required if the methods are to be successfully deployed in a range of areas. As part of this drive, various enzyme immobilization strategies have been studied, alongside process intensification from batch to continuous production. The flow bioreactor portfolio mainly ranges between packed bed reactors and wall‐immobilized enzyme miniaturized reactors. Because of their simplicity, packed bed reactors are the most frequently encountered at lab‐scale. However, at industrial scale, the growing pressure drop induced by the increase in equipment size hampers their implementation for some applications. Wall‐immobilized miniaturized reactors require less pumping power, but a new problem arises due to their reduced enzyme‐loading capacity. This review starts with a presentation of the current technology portfolio and a reminder of the metrics to be applied with flow bioreactors. Then, a benchmarking of the most recent relevant works is presented. The scale‐up perspectives of the various options are presented in detail, highlighting key features of industrial requirements. One of the main objectives of this review is to clarify the strategies on which future study should center to maximize the performance of wall‐immobilized enzyme reactors.

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CFD Simulations of Microreactors for the Hydrolysis of Cellobiose to Glucose by β-Glucosidase Enzyme

Cited by 9 publications

References 31 publications

Biocatalytic Performance of β-Glucosidase Immobilized on 3D-Printed Single- and Multi-Channel Polylactic Acid Microreactors

Biocatalytic Performance of β-Glucosidase Immobilized on 3D-Printed Single- and Multi-Channel Polylactic Acid Microreactors

Enzymatic hydrolysis in food processing: biotechnological advancements, applications, and future perspectives

Wall‐Immobilized Biocatalyst vs. Packed Bed in Miniaturized Continuous Reactors: Performances and Scale‐Up

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