ArticleFrontiers in bioengineering and biotechnology2021
Hydrogel-Based Enzyme and Cofactor Co-Immobilization for Efficient Continuous Transamination in a Microbioreactor.
Article in Frontiers in bioengineering and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 42 citations in OpenAlex.
- Development of Sustainable Biocatalytic Furfurylamine Production in a Magnetic Field-Assisted Microfluidic Reactor.ACS sustainable chemistry & engineering · 2025Article
- Development of a Microbioreactor forMicromachines · 2024Article
- Tuning Mechanical Characteristics and Permeability of Alginate Hydrogel by Polyvinyl Alcohol and Deep Eutectic Solvent Addition.Bioengineering (Basel, Switzerland) · 2024Article
- Enzymatic Routes for Chiral Amine Synthesis: Protein Engineering and Process Optimization.Biologics : targets & therapy · 2024Review
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2 authors at 1 institution in 1 country.
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Abstract
A microbioreactor was developed in which selected amine transaminase was immobilized together with the cofactor pyridoxal phosphate (PLP) to allow efficient continuous transamination. The enzyme and cofactor were retained in a porous copolymeric hydrogel matrix formed in a two-plate microreactor with an immobilization efficiency of over 97%. After 10 days of continuous operation, 92% of the initial productivity was retained and no leaching of PLP or enzyme from the hydrogel was observed. The microbioreactor with co-immobilized cofactor showed similar performance with and without the addition of exogenous PLP, suggesting that the addition of PLP is not required during the process. The space-time yield of the microbioreactor was 19.91 g L
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