Document Type
Article
Publication Date
2-2014
Source Publication
Journal of Molecular Catalysis B: Enzymatic
Source ISSN
1381-1177
Abstract
The cobalt-type nitrile hydratase from Pseudonocardia thermophila JCM 3095 (PtNHase) was successfully encapsulated in tetramethyl orthosilicate sol–gel matrices to produce a PtNHase:sol–gel biomaterial. The PtNHase:sol–gel biomaterial catalyzed the conversion of 600 mM acrylonitrile to acrylamide in 60 min at 35 °C with a yields of >90%. Treatment of the biomaterial with proteases confirmed that the catalytic activity is due to the encapsulated enzyme and not surface bound NHase. The biomaterial retained 50% of its activity after being used for a total of 13 consecutive reactions for the conversion of acrylonitrile to acrylamide. The thermostability and long-term storage of the PtNHase:sol–gel are substantially improved compared to the soluble NHase. Additionally, the biomaterial is significantly more stable at high concentrations of methanol (50% and 70%, v/v) as a co-solvent for the hydration of acrylonitrile than native PtNHase. These data indicate that PtNHase:sol–gel biomaterials can be used to develop new synthetic avenues involving nitriles as starting materials given that the conversion of the nitrile moiety to the corresponding amide occurs under mild temperature and pH conditions.
Recommended Citation
Martinez, Salette; Kuhn, Misty L.; Russell, James T.; Holz, Richard C.; and Elgren, Timothy E., "Acrylamide Production Using Encapsulated Nitrile Hydratase from Pseudonocardia thermophila in a Sol–gel Matrix" (2014). Chemistry Faculty Research and Publications. 295.
https://epublications.marquette.edu/chem_fac/295
Comments
Accepted version. Journal of Molecular Catalysis B: Enzymatic, Vol. 100 (February 2014): 19-24. DOI. © 2013 Elsevier B.V. Used with permission.