Enzyme mimicry is a topic of considerable interest in the development of multifunctional biomimetic materials. Mimicking enzyme activity is a major challenge in biomaterials research, and artificial analogs that simultaneously recapitulate the catalytic and metabolic activity of native enzymes are considered to be the ultimate goal of this field. This consensus may be challenged by self‐assembling multifunctional nanostructures to develop close‐to‐fidelity enzyme mimics. Here, the ability of fullerene nanostructures decorated with active units to form enzyme‐like materials that can mimic phosphatases in a metal‐free manner is presented. These nanostructures self‐assemble into nanoclusters forming multiple random active sites that can cleave both phosphomonoesters and phosphodiesters while being more specific for the phosphomonoesters. Moreover, they are reusable and show an increase in catalytic activity over multiple cycles similar to their natural counterparts. In addition to having enzyme‐like catalytic properties, these nanocatalysts imitate the biological functions of their natural analogs by inducing biomineralization and osteoinduction in preosteoblast and mesenchymal stem cells in vitro studies.

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The pectin isolation technique from sugar beet pulp was optimized to acquire high-quality bioactive pectin with the highest yield and low esterification degree. The influence of each isolation parameter on the success of pectin production was investigated by analytical characterization methods. With this step-by-step analytic investigation, we could be able to achieve ~ 45% yield with a ~ 10% low esterification degree. In addition to compositional quality, bioactivity and anticancer profile of the obtained sugar beet pulp pectin (SBPP) was investigated on SaOS-2 osteosarcoma cell line. In comparison with citrus pectin (CP), which is frequently applied pectin derivative as an anticancer agent, SBPP revealed prolonged antiproliferative profile for cancer cells. In addition to proliferation, intracellular reactive oxygen species (ROS) level and Bcl-2 anti-apoptotic gene expression were surveyed in vitro. Interestingly, the lower concentration of SBPP (0.25%) induced a significant rise in intracellular ROS level and anti-apoptotic gene Bcl-2 expression on the contrary to CP. All results demonstrated that different pectin types can lead different biological mechanism of action and the isolated SBPP by using optimized protocol exhibited great potential for biomedical applications without requirement of additional post-modification after isolation.