55536-07-7Relevant academic research and scientific papers
Synthesis of a superparamagnetic ultrathin FeCO3 nanorods-enzyme bionanohybrid as a novel heterogeneous catalyst
Benavente, Rocio,Lopez-Tejedor, David,Palomo, Jose M.
supporting information, p. 6256 - 6259 (2018/06/22)
Herein we report a straightforward synthesis of an ultrathin protein-iron(ii) carbonate nanorods (FeCO3-NRs) heterogeneous bionanohybrid at room temperature and in aqueous media. The enzyme induced the in situ formation of well-dispersed FeCO3 NRs on a protein network. The addition of NaBH4 as a reducing agent allowed us to obtain nanorods (5 × 40 nm) with superparamagnetic properties. This bionanohybrid showed excellent catalytic results in reduction, oxidation and C-C bond reactions.
Studies in Bile Salt Solutions. XIV. Electronic, Charge and Steric Substrate-Effects on the Esterase Activity of Bile-Salt-Stimulated Human Milk Lipase. Hydrolysis of 4-Substituted Phenyl Propionates
O'Connor, Charmian J.,Mitha, Amin S. H.
, p. 259 - 269 (2007/10/02)
The rate constants of hydrolysis of series of 4-substituted phenyl propionates, catalysed by bile-salt-stimulated human milk lipase in the absence and presence of cholate or taurocholate stimulation, have been measured at pH 7.3, 310.5 K.There is little evidence for an alkyl site electronic interaction in the rate-determining step of the esterolytic reaction.However, a negatively charged substrate or an amido-substituent caused an inhibition of unstimulated esterase activity.In the presence of the bile-salt cofactors, esterolytic activity against charged substrates may be stimulated or inhibited, depending on the proximity of the charge to the steroidal side chain and the subsequent substrate-interaction within the surrounding environment of the active site.It has been confirmed that bile-salt-stimulated lipase is not an amidase, but that an amide, of the correct geometry, may occupy the active site and restrict esterase activity.
