Enzymatic and Chemical Cross-Linking of Bacterial Cellulose/Fish Collagen Composites—A Comparative Study
Abstract
:1. Introduction
2. Results and Discussion
2.1. Composites Preparation
2.2. Structural Characteristics
2.2.1. Morphological Properties
2.2.2. Thermal Properties
2.2.3. Crystalline Properties
2.2.4. Chemical Structure
2.3. Functional Properties
2.3.1. Mechanical Properties
2.3.2. Water Vapor Permeability
3. Materials and Methods
3.1. Materials
3.2. Modification of BC
3.3. Structural Characterization
3.3.1. Scanning Electron Microscopy
3.3.2. Thermal Analysis
3.3.3. X-ray Diffractometry
3.3.4. Attenuated Total Reflectance (ATR) Fourier Transformation Infrared Spectroscopy
3.4. Mechanical Tests
3.5. Water Vapor Permeability
3.6. Statistical Analysis
4. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
Abbreviations
BC. | Bacterial cellulose |
Col | Collagen |
CrI | Crystallinity index |
DTG | Differential thermogravimetric curve |
EDC | 1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide |
FT-IR | Fourier transform infrared spectroscopy |
oxBC | Oxidized bacterial cellulose |
RH | Relative humidity |
SEM | Scanning electron microscopy |
TG | Thermogravimetric curve |
TGase | Transglutaminase |
TGGS | Transglutaminase dedicated for the fish industry |
TGWM | Transglutaminase proposed for the meat industry |
XRD | X-ray diffraction |
WVP | Water Vapor Permeability |
ε | Elongation at break |
σ | Tensile strength |
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Sample * | Temperature Range [°C] | Weight Loss [%] ** | DTG [°C] |
---|---|---|---|
BC | 40–200 200–400 400–700 | 1.9 84.1 6.6 | 363.0 |
Col | 40–200 200–400 400–700 | 8.8 48.4 10.0 | 313.1 |
BC/Col | 40–200 200–400 400–700 | 1.3 86.3 6.3 | 363.8 |
BC/Col/TGWM15 | 40–200 200–400 400–700 | 2.3 74.4 6.8 | 365.7 |
BC/Col/TGWM120 | 40–200 200–400 400–700 | 2.2 75.1 6.3 | 364.0 |
BC/Col/TGGS15 | 40–200 200–400 400–700 | 2.5 74.4 5.6 | 364.5 |
BC/Col/TGGS120 | 40–200 200–400 400–700 | 2.6 72.3 7.0 | 364.0 |
oxBC | 40–200 200–400 400–700 | 11.5 59.0 8.9 | 172.2 288.0 |
oxBC/Col | 40–200 200–400 400–700 | 6.4 73.9 7.9 | 205.8 331.7 |
Sample x | d-Spacing (nm) | CrI (%) | A1228/A1441 | AAmide A /AAmide I | ||
---|---|---|---|---|---|---|
110 | 110 | 200 | ||||
d1 | d2 | d3 | ||||
Col | – | – | – | – | 1.04 | 1.27 |
BC | 6.06 | 5.52 | 3.92 | 86.0 | – | – |
BC/Col | 6.05 | 5.22 | 3.86 | 85.7 | 0.93 | 1.83 |
BC/Col/TGWM15 | 6.03 | 5.41 | 3.90 | 85.8 | 0.97 | 1.36 |
BC/Col/TGWM120 | 6.01 | 5.43 | 3.86 | 85.3 | 0.97 | 1.28 |
BC/Col/TGGS15 | 6.13 | 5.43 | 3.92 | 87.5 | 1.01 | 0.96 |
BC/Col/TGGS120 | 6.05 | 5.32 | 3.89 | 86.2 | 0.97 | 0.66 |
oxBC | 6.09 | 5.21 | 3.89 | 79.1 | 0.99 | – |
oxBC/Col | 5.99 | 5.34 | 3.89 | 82.2 | 0.93 | 1.63 |
BC | Col | ||
---|---|---|---|
Position in cm−1 and Intensity * | Band Assignment | Position in cm−1 and Intensity * | Band Assignment |
3395 sh | νOH intramolecular H-bonds for 3OH–O5 and 2OH–O6 | 3302 s | Amide A νNH, νOH |
3346 s | νOH intramolecular H-bonds for 3OH–O5 | 3074 m | Amide B νNH |
3242 m | νOH intermolecular H-bonds for 6OH–O3′ | 2929 m | asym νCH2– |
2895 m | νCH | 1633 s | Amide I νC=O, νNH |
1649 w | νC=O, δOH polymer bound water | 1531 s | Amide II δNH, νC–N, νC–C |
1425 w | δCH2, δOH | 1441 m | δCH2 |
1363 w | νCH, δCOO | 1228 m | Amide III νC–N, δNH |
1163 w | δC–O–C of C1–O–C4, δOH | ||
1105 m | νC–OH of C2–OH | ||
1055 vs | δC–OH of C3–OH | ||
1028 vs | νC–O of C6–OH | ||
1003 vs | νC–OH | ||
999 vs | β-glycosidic linkage | ||
899 w | δCH2 |
Sample * | σ [MPa] ** | ε [%] ** | WVP [g∙mm∙kPa−1∙h−1∙m−2] *** |
---|---|---|---|
BC | 48 ± 3 b | 4.1 ± 0.8 a | 0.083 ± 0.010 bc |
BC/Col | 45 ± 7 b | 1.4 ± 0.5 c | 0.086 ± 0.007 bc |
oxBC | 28 ± 8 c | 1.6 ± 0.4 bc | 0.075 ± 0.003 abc |
oxBC/Col | 27 ± 3 c | 2.3 ± 0.5 b | 0.093 ± 0.019 c |
BC/Col /TGWM15 | 45 ± 9 b | 1.8 ± 0.6 bc | 0.066 ± 0.008 abc |
BC/Col /TGWM120 | 36 ± 4 c | 1.9 ± 0.6 bc | 0.061 ± 0.009 ab |
BC/Col /TGGS15 | 63 ± 9 a | 1.6 ± 0.3 bc | 0.074 ± 0.006 abc |
BC/Col /TGGS120 | 60 ± 7 a | 2.1 ± 0.3 bc | 0.055 ± 0.004 a |
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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
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 StyleSommer, 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