Shopping Cart
There are no more items in your cart
News
ABT has been awarded the "Innovative SME" label by the Spanish Ministry of Science, Innovation and Universities
This seal confirms the company's commitment to research, custom development and innovation in the field of bioprocessing.
Read more
Next stop: The industry's top trade shows
Agarose Bead Technologies (ABT) is excited to announce our participation in several important trade fairs this October.
Read more
Agarose Bead Technologies expands facility to meet rising global demand for novel therapies market
Agarose Bead Technologies has enhanced its Burgos facility by boosting its agarose resin production to 100,000 liters annually to position itself as a powerhouse in the novel therapies market.
Read moreSee you at Bioprocess International Conference and Exhibition 2024
ABT will be exhibiting at one of the most prestigious events in the bioprocessing industry, the Bioprocess International Conference. This prestigious event will be held...
Read more
"ABT’s beads allowed fine control over immobilization conditions, including surface functionalization, porosity, and loading capacity."
In this study, a self-sufficient heterogeneous biocatalyst was developed for the asymmetric reduction of β-keto esters, employing the enzyme Tt27-HBDH from Thermus thermophilus HB27.
A key factor in the success of this system was the immobilization strategy (Figure 1) on porous agarose beads supplied by Agarose Bead Technologies (ABT).
IMMOBILIZATION ON FUNCTIONALIZED AGAROSE BEADS
The Tt27-HBDH enzyme was immobilized using different strategies on agarose-based functionalized supports (6% BCL and 4% BCL), evaluating both reversible methods (such as ionic adsorption on agarose activated with polyethyleneimine, PEI, or with polyallylamine, PAA) and covalent methods (agarose activated with aldehyde groups, AG–G). Covalent immobilization on AG–G proved to be the most robust and effective, with yields exceeding 94% and recovered activity ranging from 50–85%, depending on the method.
A key step was the subsequent coating with PEI, which not only enhanced enzyme stability under extreme conditions (such as 60 °C, pH 4.5, and 20% isopropanol) but also enabled co-immobilization of the NADH cofactor. This polymeric coating creates a hydrophilic, positively charged environment that stabilizes the quaternary structure of the enzyme and facilitates cofactor retention.
Figure 1. (A) Electrostatic surface of Tt27-HBDH hexamer 3D-model using Bluues server. (B) Asymmetric reduction of EAA catalysed by soluble and immobilised multi-functional biocatalysts.
CUSTOMIZATION ADVANTAGES
Selecting the appropriate agarose resin proved to be critical. At ABT, the customization service offers partners a close collaboration with our organic chemists, who not only help design the tailored bead but also provide ongoing support throughout the development process, working alongside you to ensure optimal results.
ABT’s beads allowed fine control over immobilization conditions, including surface functionalization, porosity, and loading capacity. This highlights the value of ABT's customization service, which allows for the adaptation of key parameters such as:
- Particle size
- Ligand type
- Ligand concentration
- Porosity
- Activation chemistry
These features make ABT's supports ideal for applications where stability, reusability, and efficiency of the biocatalyst are essential.
- Alejandro H. Orrego, Daniel Andrés-Sanz, Susana Velasco-Lozano, Mercedes Sanchez-Costa, José Berenguer, José M. Guisan, Javier Rocha-Martin and Fernando López-Gallego. Self-sufficient asymmetric reduction of β-ketoesters catalysed by a novel and robust thermophilic alcohol dehydrogenase co-immobilised with NADH. Catal. Sci. Technol., 2021, 11, 3217-3230.