- By:
- Kosgallana, Chathurika J; Leite, Wellington C; Yuan, Yue ; Meilleur, Flora
- Page Number:
- 1-7
- Book Title:
- Proceedings of the 2025 Biocatalyst Interactions with Gases (BIG) Research Symposium
- Publication Date:
- March 12, 2026
- Publisher Location:
- SSRN, Netherlands
- Conference Name:
- Biocatalyst Interactions with Gases (BIG) Research Symposium
- Conference Location:
- Raleigh, North Carolina, United States of America
- Conference Sponsor:
- Novo Nordisk Foundation
- View DOI Listing:
- https://doi.org/10.2139/ssrn.5333316
Abstract
Immobilizing enzymes in polysaccharide-based matrices has been shown to improve both their stability and their catalytic efficiency. Among available materials, chitosan was selected for its abundance, biocompatibility, and versatility in a range of applications. While the broader aim of this work is to study chitosan as a matrix for immobilizing carbonic anhydrase (CA) for CO₂ capture, this study focused on determining the contrast match point (CMP) of hydrogenated and deuterated chitosan in D₂O:H₂O mixtures to enable future structural investigations using small-angle neutron scattering (SANS). Previous work successfully synthesized deuterated chitosan from Rhizopus oryzae mycelia and assessed the degree of deuteration using Fourier-transform infrared spectroscopy (FTIR) and nuclear magnetic resonance (NMR). Building on this foundation, the current study determined the CMPs of both H-chitosan and D-chitosan by performing SANS measurements across a range of D₂O:H₂O solvent contrasts. The extracted CMPs for both forms correlated well with their respective calculated scattering length densities (SLDs), validating the experimental approach. These results establish a critical reference for selective contrast matching in future SANS studies of carbonic anhydrase immobilized in chitosan matrices, enabling detailed structural analysis of enzyme–matrix interactions.
