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The Effects of Graphene Oxide and Partially Reduced Graphene Oxide on the Enzymatic Activity of Microbial Transglutaminase in Gelatin

Published online by Cambridge University Press:  11 February 2019

Rebecca Isseroff*
Affiliation:
Stony Brook University, Stony Brook, NY
Jerry Reyes
Affiliation:
Stony Brook University, Stony Brook, NY
Roshan Reddy
Affiliation:
Stony Brook University, Stony Brook, NY
Nicholas Williams
Affiliation:
Stony Brook University, Stony Brook, NY
Miriam Rafailovich
Affiliation:
Stony Brook University, Stony Brook, NY
*
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Abstract

A significant drawback of enzyme use in industrial applications is its lack of stability. Graphene oxide (GO) has previously been investigated for enzyme immobilization and enhancement of enzymatic catalysis. Microbial transglutaminase (MTG) is an enzyme that is used to modify food proteins, increase durability of textiles, and crosslink hydrogels for drug delivery. We tested the effects of adding GO and partially reduced GO (pRGO) to water solutions of gelatin and then crosslinking it with MTG, measuring both the resulting gelatin modulus and then the time it took for the onset of gelation. We found that the presence of pRGO in a gelatin-MTG-water mixture (when using 0.75 g MTG in 10 ml of gelatin solution) significantly increases the modulus by 60% more than the control. Using this same concentration of MTG, we measured the onset of gelation time and found that pRGO in gelatin solution reduces the onset of gelation time by nearly 50% while inducing a very large increase in viscosity by three orders of magnitude, whereas the addition of GO increases the onset of gelation time by 33% and decreases the viscosity of the gel by more than one order of magnitude. The very large enhancement by pRGO of the viscosity may be due to pRGO’s electron withdrawing ability and/or may also be due to adsorption of gelatin to the pRGO platelets which effectively increases the crosslinking density through non-enzymatic processes assisting the enzymatic activity.

Type
Articles
Copyright
Copyright © Materials Research Society 2019 

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References

REFERENCES

Huisman, G.W. and Collier, S.J., Current Opinion in Chemical Biology 17, 284 (2013).CrossRefGoogle Scholar
Pavlidis, I.V., Vorhaben, T., Gournis, D., Papadopoulos, G.K., Bornscheuer, U.T., and Stamatis, H., Journal of Nanoparticle Research 14, (2012).CrossRefGoogle Scholar
Vovusha, H., Sanyal, S., and Sanyal, B., The Journal of Physical Chemistry Letters 4, 3710 (2013).CrossRefGoogle Scholar
Jin, L., Yang, K., Yao, K., Zhang, S., Tao, H., Lee, S.-T., Liu, Z., and Peng, R., ACS Nano 6, 4864 (2012).CrossRefGoogle Scholar
Mallineni, S.S.K., Shannahan, J., Raghavendra, A.J., Rao, A.M., Brown, J.M., and Podila, R., ACS Applied Materials & Interfaces 8, 16604 (2016).CrossRefGoogle Scholar
Kieliszek, M. and Misiewicz, A., Folia Microbiologica 59, 241 (2013).CrossRefGoogle Scholar
Tesfaw, A., Assefa, F., Int J Tex Sci. 3,64–9 (2014).Google Scholar
Gundersen, M.T., Keillor, J.W., and Pelletier, J.N., Applied Microbiology and Biotechnology 98, 219 (2013).CrossRefGoogle Scholar
Romeih, E. and Walker, G., Trends in Food Science & Technology 62, 133 (2017).CrossRefGoogle Scholar
Isseroff, R., Akhavan, B., Pan, C., He, H.S., Sokolov, J., and Rafailovich, M., MRS Proceedings 1658, (2014).Google Scholar
Hummers, W.S. and Offeman, R.E., Journal of the American Chemical Society 80, 1339 (1958).CrossRefGoogle Scholar
Soofi, S.S., Last, J.A., Liliensiek, S.J., Nealey, P.F., and Murphy, C.J., Journal of Structural Biology 167, 216 (2009).CrossRefGoogle Scholar
Paguirigan, A.L. and Beebe, D.J., Nature Protocols 2, 1782 (2007).CrossRefGoogle Scholar