Abstract
The development of protein anti-degradation strategies is important for storage at ambient conditions, for example in vaccine storage. Despite that it is known that biominerals, typical inorganic-organic composites, can preserve proteins at room temperature for a long time, it is unclear the extent of protein degradation under high temperatures. In this study, we examined remaining proteins in the toasted abalone shell under high temperatures (200 and 300°C) by biomineral proteomics method. Surprisingly, 21 proteins including carbonic anhydrase, hemocyanin, actin can still be identified from shells even after toasting under 300°C, not much decreased compared to that in the 200°C-treated and the native shell. However, the microstructure and composition (both mineral and organic matrix) of shells were altered significantly revealed by scanning electron microscopy, infrared spectroscopy, and X-ray diffraction. The well-preserved proteins may be partially due to the sacrifice of mineral/organic interfaces and the formation of nanopores in the shell at high temperatures. Moreover, the extracted proteins from both groups were able to affect calcium carbonate in vitro, indicating certain remaining bioactivities of proteins. This study has potential implications in various fields such as protein storage at high temperatures and palaeoproteomics.
Highlights
Proteins are usually prone to be degraded under ambient temperatures let alone high temperatures (Bischof and He, 2006)
In the native abalone shell, the classical “brick-andmotor” structure composed of stacking nanoscale tablets was observed by Scanning electron microscopy (SEM) (Figures 2A,B)
These nanopores were observed when sea urchin skeleton made of calcium carbonate was treated at high temperatures, in which the authors ascribed the pore formation to the transformation of amorphous calcium carbonate (ACC) to crystalline calcite (Albéric et al, 2018)
Summary
Proteins are usually prone to be degraded under ambient temperatures let alone high temperatures (Bischof and He, 2006). A typical mollusk shell biomineral, is composed of 95% calcium carbonate and 5% organics (proteins, polysaccharides, and lipids) (Addadi et al, 2006). In recent past two decades, by proteomic methods, dozens of proteins were identified in various mollusk biominerals (Marie et al, 2012; Liao et al, 2015; Liu et al, 2015; Marin, 2020; Liu and Zhang, 2021). Proteins in bone or dental enamel fossils, which have been preserved for as long as thousands of years or even millions of years (Weiner et al, 1976), are employed to perform phylogenetic analysis (Welker et al, 2015) of humans or to reconstruct people’s life in the past (Hendy et al, 2018; Cappellini et al, 2019; Sakalauskaite et al, 2019; Welker et al, 2019)
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