This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Thanks to enzyme-based biocatalysis, an enormous range of pharmaceutical active ingredients and other complex molecules can be synthesized in an environmentally friendly manner. Researchers at the Karlsruhe Institute of Technology (KIT) have now developed a technology that allows to assemble enzymes into millimeter-sized, storable beads.
In this process, the enzymes not only act as catalysts but also constitute the beads' material itself. In a further variant, the enzyme networks can be combined with living cells. A patent application has been filed for the technology.
The results have been published in Advanced Materials. In biocatalysis, enzymes are used to accelerate reactions instead of chemical catalysts, which are often toxic. This saves raw materials and energy.
To ensure that this technology can be used as widely as possible in the chemical industry, the biocatalysts must be available continuously and in large quantities. Moreover, they must be storable, transportable and easy to dose. To meet all these requirements, a team headed by professor Christof Niemeyer from KIT's Institute for Biological Interfaces 1 has refined the so-called AEH (all-enzyme hydrogels) concept.
It involves equipping enzymes with complementary molecular binding modules. "When the complementary building blocks come together, they organize themselves into three-dimensional protein networks," said Niemeyer. "Thus, the enzymes are catalysts and the structural material of the beads at the same time—a great advantage over conventional methods.
We avoid inactive support material, increasing the efficiency of the desired chemical reaction." The researchers used these properties to synthesize easy-to-handle beads in two steps. First, they combined complementary enzyme building blocks within liquid droplets and consolidated them by rapid freezing in liquid nitrogen. Subsequent freeze-drying yielded mechanically robust, porous protein beads of a defined size.
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