| Summary: | By means of consecutive alkaline and proteolytic treatments of the organic framework’s interlamellar layers extracted from the nacre of H. rufescens, we have exposed a core of aligned parallel chitin fibers. Our findings both verify basic elements of the interlamellar layer structural model of Levi-Kalisman et al. (2001) and extend the more detailed model of Bezares et al. (2008, 2010). We observe via SEM imaging of square millimeter sized samples, which include numerous interlamellar layers and micron sized, yet nanocrystalline, CaCO3 tiles whose native orientation within the shell was first documented, that the chitin fibers in all layers are aligned normal to the growth direction of the shell. Similar alignment has been suggested in the literature for two other classes of mollusks, viz. N. rupertus and P. martensii (Weiner and Traub, 1983; Wada, 1958), suggesting that this may be a more general motif. We find that in order to expose the chitin core it is necessary to first remove protein by an alkaline treatment followed by enzymatic digestion with proteinase-K. We also observe what appear to be the points of traversal of the exposed chitin core by mineral bridges. The implications of these findings touch directly and most specifically upon the expected mechanical properties of organic framework layers such as stiffness and relaxation time constants, viz. they should be planeorthotropic. Single interlamellar layers extracted from nacre should, by implication, also exhibit an orthotropic stiffness. These novel findings provide the structural picture required for a complete anisotropic, time dependent, constitutive description of nacre long thought to be a paradigm of structural optimization. Such a model is briefly described herein and is developed, in full, in Part II of this series.
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