Enzyme loading in the support and medium composition during immobilization alter activity, specificity and stability of octyl agarose-immobilized Eversa Transform

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 295, P. 139667 - 139667

Published: Jan. 9, 2025

Language: Английский

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The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading

Catalysts, Journal Year: 2024, Volume and Issue: 14(2), P. 105 - 105

Published: Jan. 26, 2024

The lipases from Thermomyces lanuginosus (TLL) and Candida antarctica (B) (CALB) were immobilized on octyl-agarose beads at 1 mg/g (a loading under the capacity of support) by overloading support with enzymes. These biocatalysts compared in their stabilities 10 mM sodium phosphate, HEPES, Tris-HCl pH 7. Lowly loaded CALB was more stable than highly preparation, while TLL this effect smaller. Phosphate very negative for stability biocatalyst moderately using both loadings. enzymes HEPES presented a different response as function enzyme (e.g., lowly CALB, similar buffers, but it clearly smaller biocatalysts). Moreover, specific activity versus p-nitrophenol butyrate, triacetin R- or S-methyl mandelate depended buffer, loading, interaction between them. In some cases, almost twice expected could be obtained octyl-CALB, depending buffer. A co-interaction effects specificity buffer nature detected.

Language: Английский

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The effects of the chemical modification on immobilized lipase features are affected by the enzyme crowding in the support

Biotechnology Progress, Journal Year: 2023, Volume and Issue: 40(1)

Published: Oct. 12, 2023

In this article, we have analyzed the interactions between enzyme crowding on a given support and its chemical modification (ethylenediamine via carbodiimide route picryl sulfonic (TNBS) of primary amino groups) activity stability. Lipase from Thermomyces lanuginosus (TLL) lipase B Candida antarctica (CALB) were immobilized octyl-agarose beads at two very different loadings, one them exceeding capacity support, well under capacity. Chemical modifications highly loaded lowly biocatalysts gave results in terms stability, which could increase or decrease depending loading. For example, both increased their after while effect was opposite for biocatalysts. Additionally, with TNBS CALB biocatalyst stability activity.

Language: Английский

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Immobilization and Stabilization of D-allulose 3-epimerase for Continuous D-allulose Synthesis in Packed-Bed Reactors

Food Bioscience, Journal Year: 2025, Volume and Issue: unknown, P. 105959 - 105959

Published: Jan. 1, 2025

Language: Английский

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Functionalized mesoporous biosilica for immobilizing D-allulose 3-epimerase: A multienzyme cascade strategy for calorie reduction in fruit tea drinks

Food Bioscience, Journal Year: 2024, Volume and Issue: unknown, P. 105331 - 105331

Published: Oct. 1, 2024

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Tuning almond lipase features by the buffer used during immobilization: The apparent biocatalysts stability depends on the immobilization and inactivation buffers and the substrate utilized

Journal of Biotechnology, Journal Year: 2024, Volume and Issue: 391, P. 72 - 80

Published: June 13, 2024

The lipase from Prunus dulcis almonds was inactivated under different conditions. At pH 5 and 9, enzyme stability remained similar the studied buffers. However, when inactivation performed at 7, there were some clear differences on depending buffer used. more stable in Gly than Tris employed for inactivation. Then, immobilized methacrylate beads coated with octadecyl groups 7 presence of Gly, Tris, phosphate HEPES. Its activity assayed versus triacetin S-methyl mandelate. biocatalyst prepared active mandelate, while other ones triacetin. depends used immobilization. substrate determined activity. For example, glycine that promoted lowest or highest stabilities to quantify activities.

Language: Английский

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Tailored magnetic silica-immobilized D-allulose 3-epimerase with enhanced stability and recyclability for efficient D-allulose production

International Journal of Biological Macromolecules, Journal Year: 2024, Volume and Issue: unknown, P. 137896 - 137896

Published: Nov. 1, 2024

Language: Английский

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A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives

International Journal of Molecular Sciences, Journal Year: 2024, Volume and Issue: 25(10), P. 5084 - 5084

Published: May 7, 2024

The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers chiral drugs in reactions carried out organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it extremely important develop optimal procedures achieve high enantioselectivity biocatalysts medium. Our paper describes new approach biocatalysis performed solvent with CALB-octyl-agarose including application polypropylene reactor, appropriate buffer immobilization (Tris base-pH 9, 100 mM), drying step, then storage lipases climatic chamber or refrigerator. An B from Candida antarctica (CALB) was used kinetic resolution (R,S)-flurbiprofen by enantioselective esterification methanol, reaching enantiomeric excess (eep = 89.6 ± 2.0%). As part optimization, influence different buffers investigated. effect reactor material reaction medium activity also studied. Moreover, stability lipases: rugosa (CRL) CALB during various temperature humidity conditions (climatic refrigerator) tested. allowed receiving over 9-fold higher conversion values compared results achieved when conducting glass as well approximately 30-fold comparison free lipase. good demonstrated. After 7 days refrigerator (with protection humidity) 60% were obtained observed form that had not been stored. involving indicates significant role polymer being achieving catalytic activity.

Language: Английский

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