The precise assignments of cross polarization/magic angle spinning (CP/MAS) (13)C NMR spectra of cellulose I(alpha) and I(beta) were performed by using (13)C labeled cellulose biosynthesized by Acetobacter xylinum (A. xylinum) ATCC10245 strain from culture medium containing D-[1,3-(13)C]glycerol or D-[2-(13)C]glucose as a carbon source. On the CP/MAS (13)C NMR spectrum of cellulose from D-[1,3-(13)C]glycerol, the introduced (13)C labeling were observed at C1, C3, C4, and C6 of the biosynthesized cellulose. In the case of cellulose biosynthesized from D-[2-(13)C]glucose, the transitions of (13)C labeling to C1, C3, and C5 from C2 were observed. With the quantitative analysis of the (13)C transition ratio and comparing the CP/MAS (13)C NMR spectrum of the Cladophora cellulose with those of the (13)C labeled celluloses, the assignments of the cluster of resonances which belong to C2, C3, and C5 of cellulose, which have not been assigned before, were performed. As a result, all carbons of cellulose I(alpha) and I(beta) except for C1 and C6 of cellulose I(alpha) and C2 of cellulose I(beta) were shown in equal intensity of doublet in the CP/MAS spectrum of the native cellulose, which suggests that two inequivalent glucopyranose residues were contained in the unit cells of both cellulose I(alpha) and I(beta) allomorphs.

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The improvement of the thermal stability of gel prepared from salmon atelocollagen (SC) was studied. The denaturation temperature (Td) of the SC solution was found to be 18.6 degrees C. Neutral buffer including 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) was mixed with acidic SC solution at 4 degrees C, resulting in the introduction of EDC cross-linking during fibril formation. The mechanical strength and thermal stability of the resultant cross-linked SC fibrillar gels reached maximum values at an EDC concentration of 50 mM (f-50 gel). In particular, the melting temperature of the f-50 gel was 47 degrees C, much higher than that of the EDC cross-linked SC gel without fibril formation at the same EDC concentration. The proliferation rate of human periodontal ligament cells on the f-50 gel was higher than that of a porcine atelocollagen fibrillar gel. These results suggest that the gel employed for biomaterials can be fabricated from low Td fish collagen by EDC cross-linking during fibril formation.

To date, collagen for biomedical uses has been obtained from mammalian sources. The purpose of this study was to evaluate the in vivo biological responses and bioresorption of collagen obtained from tilapia (Oreochromis niloticas) scales as compared to those of collagen from porcine dermis. Collagen sponges with micro-porous structures were fabricated from reconstituted collagen fibrils using freeze-drying and cross-linked by dehydrothermal treatment (DHT treatment) or additional treatment with a water-soluble carbodiimide (WSC treatment). The mechanical properties of the tilapia collagen sponges were similar to those of porcine collagen sponges with the same cross-linking methods, where WSC treatment remarkably improved the properties over DHT treatment alone. The pellet implantation tests into the paravertebral muscle of rabbits demonstrated that tilapia collagen caused rare inflammatory responses at 1- and 4-week implantations, statistically similar to those of porcine collagen and a high-density polyethylene as a negative control. The bioresorption rates of both the collagen implants were similar, except for the DHT-treated tilapia collagen sponges at 1-week implantation. These results suggest that tilapia collagen is a potential alternative to conventional mammalian collagens in biomedical uses.