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Article

Enzymatic and Chemical Cross-Linking of Bacterial Cellulose/Fish Collagen Composites—A Comparative Study

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Department of Chemistry, Technology and Biotechnology of Food, Chemical Faculty, Gdańsk University of Technology, Narutowicza 11/12 St., 80-233 Gdańsk, Poland
2
Laboratory of Molecular Diagnostics and Biochemistry, Plant Breeding and Acclimatization Institute—National Research Institute, Bonin Research Center, Bonin 3, 76-009 Bonin, Poland
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Department of Automotive Engineering, Faculty of Mechanical Engineering and Ship Technology, Gdańsk University of Technology, Narutowicza 11/12 St., 80-233 Gdańsk, Poland
4
Faculty of Chemistry, Jagiellonian University, Gronostajowa 2, 30-387 Kraków, Poland
*
Author to whom correspondence should be addressed.
Academic Editor: Roberto Fernandez-Lafuente
Int. J. Mol. Sci. 2021, 22(7), 3346; https://doi.org/10.3390/ijms22073346
Received: 8 February 2021 / Revised: 17 March 2021 / Accepted: 23 March 2021 / Published: 25 March 2021
(This article belongs to the Section Macromolecules)
This article compares the properties of bacterial cellulose/fish collagen composites (BC/Col) after enzymatic and chemical cross-linking. In our methodology, two transglutaminases are used for enzymatic cross-linking—one recommended for the meat and the other proposed for the fish industry—and pre-oxidated BC (oxBC) is used for chemical cross-linking. The structure of the obtained composites is characterized by scanning electron microscopy, thermogravimetric analysis, X-ray diffraction, and Fourier transform infrared spectroscopy, and their functional properties by mechanical and water barrier tests. While polymer chains in uncross-linked BC/Col are intertwined by H-bonds, new covalent bonds in enzymatically cross-linked ones are formed—resulting in increased thermal stability and crystallinity of the material. The C2–C3 bonds cleavage in D-glucose units, due to BC oxidation, cause secondary alcohol groups to vanish in favor of the carbonyl groups’ formation, thus reducing the number of H-bonded OHs. Thermal stability and crystallinity of oxBC/Col remain lower than those of BC/Col. The BC/Col formation did not affect tensile strength and water vapor permeability of BC, but enzymatic cross-linking with TGGS improved them significantly. View Full-Text
Keywords: bacterial cellulose; collagen; ex situ modification; cross-linking; structural characteristics bacterial cellulose; collagen; ex situ modification; cross-linking; structural characteristics
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MDPI and ACS Style

Sommer, A.; Dederko-Kantowicz, P.; Staroszczyk, H.; Sommer, S.; Michalec, M. Enzymatic and Chemical Cross-Linking of Bacterial Cellulose/Fish Collagen Composites—A Comparative Study. Int. J. Mol. Sci. 2021, 22, 3346. https://doi.org/10.3390/ijms22073346

AMA Style

Sommer A, Dederko-Kantowicz P, Staroszczyk H, Sommer S, Michalec M. Enzymatic and Chemical Cross-Linking of Bacterial Cellulose/Fish Collagen Composites—A Comparative Study. International Journal of Molecular Sciences. 2021; 22(7):3346. https://doi.org/10.3390/ijms22073346

Chicago/Turabian Style

Sommer, Agata, Paulina Dederko-Kantowicz, Hanna Staroszczyk, Sławomir Sommer, and Marek Michalec. 2021. "Enzymatic and Chemical Cross-Linking of Bacterial Cellulose/Fish Collagen Composites—A Comparative Study" International Journal of Molecular Sciences 22, no. 7: 3346. https://doi.org/10.3390/ijms22073346

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