Self-healing, an intrinsic property of biomineralization processes

Abstract

The sponge siliceous spicules are formed enzymatically via silicatein, in contrast to other siliceous biominerals. Originally, silicatein had been described as a major structural protein of the spicules that has the property to allow a specific deposition of silica onto their surface. More recently, it had been unequivocally demonstrated that silicatein displays a genuine enzyme activity, initiating and maintaining silica biopolycondensation at low precursor concentrations (<2 mM). Even more, as silicatein becomes embedded into the biosilica polymer, formed by the enzyme, it retains its functionality to enable a controlled biosilica deposition. The protection of silicatein through the biosilica mantel is so strong that it conserves the functionality of the enzyme for thousands of years. The implication of this finding, the preservation of the enzyme function over such long time periods, is that the intrinsic property of silicatein to display its enzymatic activity remains in the biosilica deposits. This self-healing property of sponge biosilica can be utilized to engineer novel hybrid materials, with silicatein as a functional template, which are more resistant toward physical stress and fracture. Those hybrid materials can even be used for the fabrication of silica dielectrics coupled to optical nanowires.