ABSTRACT
Protein-functionalized cellulose fibrils, having various amounts of covalently bonded proteins at their surface, were successfully extracted from the tunic of Pyura chilensis tunicates using successive alkaline extractions. Pure cellulose fibrils were also obtained by further bleaching and were used as reference material. Extraction yields of protein-functionalized cellulose fibrils were within the range of 62-76% by weight based on the dry initial tunic powder. Fourier-transform infrared and Raman spectroscopy confirmed the preservation of residual protein at the surface of cellulose fibrils, which was then quantified by X-ray photoelectron spectroscopy. The protein-functionalized cellulose fibrils were found to have relatively high crystallinity and their cellulose I crystalline structure was preserved upon applying alkaline treatments. The extracted cellulosic materials were found to be constituted of fibrils having a ribbon-like morphology with widths ranging from â¼30 nm up to â¼400 nm. These protein-functionalized cellulose fibrils were found to have outstanding thermal stability with one of them having onset and peak degradation temperatures of â¼350 and 374 °C, respectively. These values were found to be 24 and 41 °C higher than for bleached cellulose.
