Abstract
Crystallization of enzymes in presence of impurities is important for clarifying the role of enzymes in natural world. Although it is proposed that impurities inhibit nucleation of enzyme crystallization, details are unclear. In this study, crystallization of cellobiohydrolase from Aspergillus niger was investigated by dynamic and time-resolved static light scattering using cellobiose as an impurity. We aimed to clarify how cellobiose inhibits cellobiohydrolase crystallization and to crystallize cellobiohydrolase in concentrated cellobiose without using seeds.
Cite
CITATION STYLE
Onuma, K., Furubayashi, N., Shibata, F., Kobayashi, Y., Kaito, S., Ohnishi, Y., & Inaka, K. (2014). Crystallization of Cellobiohydrolase in the Presence of Cellulose-Degraded Cellobiose: Analysis of Intermolecular Interactions and Association Dynamics. Journal of Crystallization Process and Technology, 04(01), 1–13. https://doi.org/10.4236/jcpt.2014.41001
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.