ABSTRACT
Proteins appear to protect the native structure of chitins from attack by chitinases and seemingly guard the chains from collapse of native structure under certain ambient conditions. Clearly, ultrastructure from the original chitinous structure can be retained through purification steps when animal chitin is processed correctly from carapace via Compacted Chitin to Linear Chitin. Chitin has been known to science for almost two centuries, but elucidation of its precise behavior via-à-vis specific enzymes has been slow. Freeze-drying strands of chitin formed under correct conditions gives a white, friable powder that is termed Linear Chitin. A consequence of this would be that chitin recovered after complete protein removal should be somewhat basic; the author is unaware that this type of experiment was ever conducted. The ester bonds therefore must form internal cross-links in Linear Chitin, thus accounting for the much greater volume:mass ratio for Linear Chitin than for other chitin preparations.
