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When the paper is incinerated under the multi oxygen environment: state of the oxidation, cellulose fiber with paper does the combustion as carbon dioxide also under the low degree temperature. On the other hand, when the paper is resolved under the small oxygen environment: state of reduction, cellulose is carbonized. The pyrolysis residue, as for tar, the china clay and Talc, etc. are changed the crystal grain and came to be also different compose chemically with the raw material. Then, authors have been studying the optimum carbonization method of cellulose and the use of the products. In this report, we deal with the result of using the pyrolysis residue to purify the waste fluid.

Bacterial cellulose (BC) synthesized by Gluconacetobacter sucrofermentans CECT 7291 seems to be a good option for the restoration of degraded paper. In this work BC layers are cultivated and purified by two different methods an alkaline treatment when the culture media contains ethanol and a thermal treatment if the media is free from ethanol. The main goal of these tests was the characterization of BC layers measured in terms of tear and burst indexes, optical properties, SEM, X-ray diffraction, FTIR, degree of polymerization, static and dynamic contact angles, and mercury intrusion porosimetry. The BC layers were also evaluated in the same terms after an aging treatment. Results showed that BC has got high crystallinity index, low internal porosity, good mechanical properties and high stability over time, especially when purified by the alkaline treatment. These features make BC an adequate candidate for degraded paper reinforcement. © 2014 Elsevier Ltd.

Endoglucanase CenA of Cellulomonas fimi comprises an N-terminal cellulose-binding domain and a C-terminal catalytic domain joined together by a sequence of 23 proline and threonine residues (the Pro-Thr box). The domains function independently when separated by proteolysis. TnphoA has been used to generate cenA′-′phoA fusions. CenA′-′PhoA fusion polypeptides which contain the entire cellulose-binding domain of CenA bind to cellulose, allowing their purification from periplasmic extracts in a single, facile step. This result has implications for purification or immobilisation of chimeric proteins on a cheap cellulose matrix.