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Investigating adsorption of bovine serum albumin on cellulosic substrates using magnetic resonance imaging
- Lavenson, David M., Tozzi, Emilio J., McCarthy, Michael J., Powell, Robert L., Jeoh, Tina
- Cellulose 2011 v.18 no.6 pp. 1543-1554
- absorption, adsorption, binding sites, biofuels, biomass, bovine serum albumin, cellulose, digestion, enzymatic hydrolysis, glycosidases, lignin, magnetic resonance imaging
- Cellulosic biomass is recalcitrant to enzymatic hydrolysis which greatly reduces the efficiency of biofuels production. Specifically, the lignin component of biomass is thought to provide non-productive binding sites for glycosyl hydrolases, effectively disabling the enzymes from completing further digestion. A thorough understanding of the adsorption rates of protein molecules on celluloses—especially lignocelluloses—is crucial to improving the cyclic steps of adsorption, diffusion, and reaction. We use magnetic resonance imaging (MRI) to detect concentrations of bovine serum albumin (BSA) in equilibrium with various cellulose substrates, including delignified and acid-treated lignocellulosic substrates. BSA is believed to be an effective adsorption blocker during enzymatic hydrolysis of lignocellulosics, and has been correlated with an increase in reaction yield. We found BSA to have little adsorption onto the chosen cellulose substrates in the low concentration range studied. Ultraviolet (UV) absorption measurements of reaction supernatants at 280 nm were used to confirm the MRI results for each of the substrate types. The advantages of the MRI technique are compared with that of the traditional UV measurement.