The β-galactosidase immobilization protocol determines its performance as catalysts in the kinetically controlled synthesis of lactulose

Neto, Carlos Alberto Chaves Girão; Silva, Natan Câmara Gomes e; Costa, Thaís de Oliveira; Albuquerque, Tiago Lima de; Gonçalves, Luciana Rocha Barros; Fernández‐Lafuente, Roberto; Rocha, Maria Valderez Ponte

doi:10.1016/j.ijbiomac.2021.02.078

Cited by 20 publications

(3 citation statements)

References 67 publications

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“…101 Furthermore, in many instances, only a properly immobilized enzyme will be able to perform the target reaction in an adequate way. 114–118 Hence, immobilization may still be critical to the application of enzymes in many processes.…”

Section: Introductionmentioning

confidence: 99%

Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization

2022

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Section: Introductionmentioning

confidence: 99%

Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization

2022

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“…The immobilization of enzymes onto nanomaterials has revolutionized the use of these macromolecules in various industrial fields, which have been more recently enhanced by the advent of metal-organic frameworks [247]. The efficient immobilization of enzymes, i.e., its support and methods, is the result of perfect matching of factors depending on the enzyme [248]. Furthermore, the choice and success of the immobilization methods in the reaction depends of the different properties of the substrates and products, as well as the diversified applications of the products obtained.…”

Section: Enzyme Immobilization With Metal-organic Framework (Mofs)mentioning

confidence: 99%

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

et al. 2022

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Enzymatic biocatalysis is a sustainable technology. Enzymes are versatile and highly efficient biocatalysts, and have been widely employed due to their biodegradable nature. However, because the three-dimensional structure of these enzymes is predominantly maintained by weaker non-covalent interactions, external conditions, such as temperature and pH variations, as well as the presence of chemical compounds, can modify or even neutralize their biological activity. The enablement of this category of processes is the result of the several advances in the areas of molecular biology and biotechnology achieved over the past two decades. In this scenario, metal–organic frameworks (MOFs) are highlighted as efficient supports for enzyme immobilization. They can be used to ‘house’ a specific enzyme, providing it with protection from environmental influences. This review discusses MOFs as structures; emphasizes their synthesis strategies, properties, and applications; explores the existing methods of using immobilization processes of various enzymes; and lists their possible chemical modifications and combinations with other compounds to formulate the ideal supports for a given application.

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“…One likely application may be the simultaneous modification of the fats and lactose of milk to produce free-lactose milk (or lactose enriched in prebiotic galactosides) − that could also bear flavors produced by the lipase action, decrease the triglyceride concentration, − or be protected by the presence of some free fatty acids with antimicrobial agent activity. − Other application may be the production of galactosyl-diglycerides using lipase to produce specific diglycerides from the corresponding triglyceride (e.g., 1,2 diacetin) and the β-galactosidase from A. oryzae as the catalyst to produce the O-link ,− between galactose and diglyceride via kinetically controlled synthesis. − In this instance, the high concentration inside the particle of the diglyceride may be critical to have good reaction yields, and the immediate modification can prevent the fact that the acyl migration results in 1,3 diacetin …”

Section: Introductionmentioning

confidence: 99%

Reutilization of the Most Stable Coimmobilized Enzyme Using Glutaraldehyde Chemistry to Produce a New Combi-biocatalyst When the Coimmobilized Enzyme with a Lower Stability Is Inactivated

Carballares,

Abellanas-Perez,

de Andrades

et al. 2024

ACS Sustainable Chem. Eng.

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In the present article, glutaraldehyde was used to covalently coimmobilize the lipase Eversa Transform 2.0 and the β-galactosidase from Aspergillus oryzae. Both enzymes were adsorbed on amino supports and modified with glutaraldehyde. However, the first enzyme remained almost fully active under stress conditions, while the β-galactosidase lost a large percentage of its activity. To prevent the necessity of discarding both enzymes, the lipase was covalently immobilized following this immobilization strategy. The biocatalyst was reduced to eliminate its chemical reactivity, and the β-galactosidase was then coimmobilized via ion exchange. The incubation at high concentrations of salt desorbed the β-galactosidase from the support. This combi-biocatalyst was used in three inactivation/rebuilding cycles where the inactivated β-galactosidase was liberated from the combi-biocatalyst by washing at high ionic strength and replaced with a fresh enzyme, while the immobilized lipase maintained its activity throughout the 3 cycles. That way, it was possible to use this strategy to reuse the immobilized Eversa Transform 2.0 to build new combi-biocatalysts after β-galactosidase inactivation.

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The β-galactosidase immobilization protocol determines its performance as catalysts in the kinetically controlled synthesis of lactulose

Cited by 20 publications

References 67 publications

Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization

Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization

The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems

Reutilization of the Most Stable Coimmobilized Enzyme Using Glutaraldehyde Chemistry to Produce a New Combi-biocatalyst When the Coimmobilized Enzyme with a Lower Stability Is Inactivated

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