Bioaffinity studies

Several studies have demonstrated the improved stability of peroxidases when they were subjected to immobilization. Akhtar and Husain observed that bitter gourd peroxidase (BGP) was able to remove higher percentage of phenols over a wider range of pH when immobilized on a bioaffinity support [37]. Sasaki et al. highlighted an improvement of thermal stability of MnP immobilized on FSM-16 mesoporous material [59]. Furthermore, some other studies demonstrated a protective effect of peroxidase immobilization against inactivation by H202 [7, 20]. The different behavior of immobilized peroxidases with respect to soluble ones points out the necessity of an optimization of the process conditions when immobilized enzyme is used. Nevertheless, the possible improvement in stability should balance the usual decrease in kinetic rates, due to substrate transfer limitations to reach the enzyme inside the support. 

Bonnici, P.J. Damen, M. Waterval, J.C.M. Heck, A.J.R. Formation and Efficacy of Vancomycin Group Glycopeptide Antibiotic Stereoisomers Studied by Capillary Electrophoresis and Bioaffinity Mass Spectrometry, Anal. Biochem. 290,292-301 (2001). 

Bioaffinity chromatography is also a useful tool for the solution of the mechanism of enzymatic processes [140]. Akanuma et al. [141] employed this method for the study of the binding site of bovine carboxypeptidase B on the basis of a complex formation with immobilized substrate analogues of basic and aromatic amino acids. The problem of determining peptides of the active sites of enzymes or antibodies can be solved by the isolation of labelled specific peptides as is shown in section 4.7.5.7. Bioaffinity chromatography was also applied to the study of the molecular structures of human fibroblast and leucocyte interpherones [142]. 

Bioaffinity sensors are suitable for the characterization of environmental estrogens. The ability to prepare bioaffinity surfaces with predefined functions provides accurate and highly specific identification and quantitation of EDCs in complex environments. It is envisaged that this approach will provide a viable alternative to the characterization of potential environmental estrogens in lieu of the existing long-term animal studies. 

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