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EnglishThis study presents a computational analysis of the structures of lipase B from Candida antarctica (CalB) and two penicillin G acylases (PGAs), from eukaryotic and prokaryotic sources, respectively. Molecular simulations were used to point out the regions of the enzymes that are prone to interact with immobilisation supports. In order to evaluate the accessibility of the active site, the location of the amino acid residues involved in the formation of covalent bonds with the polymers was visualised. The mappingof the distribution of hydrophobic and hydrophilic regions on the enzyme surface provided a view of the areas of the protein that can establish either hydrophobic or hydrophilic interactions with the carriers. Experimental data obtained from the immobilisation of the enzymes on supports bearing different chemical functionalities suggest the involvement of the glycan moiety in enzyme–polymer interactions. In the case of PGA the glycan moiety can constitute an extra site for the co
| Titolo: | In silico analysis of enzyme surface and glycosylation effect as a tool for efficient covalent immobilization of CalB and PGA on Sepabeads® |
| Autori: | |
| Data di pubblicazione: | 2007 |
| Rivista: | |
| Abstract: | This study presents a computational analysis of the structures of lipase B from Candida antarctica (CalB) and two penicillin G acylases (PGAs), from eukaryotic and prokaryotic sources, respectively. Molecular simulations were used to point out the regions of the enzymes that are prone to interact with immobilisation supports. In order to evaluate the accessibility of the active site, the location of the amino acid residues involved in the formation of covalent bonds with the polymers was visualised. The mappingof the distribution of hydrophobic and hydrophilic regions on the enzyme surface provided a view of the areas of the protein that can establish either hydrophobic or hydrophilic interactions with the carriers. Experimental data obtained from the immobilisation of the enzymes on supports bearing different chemical functionalities suggest the involvement of the glycan moiety in enzyme–polymer interactions. In the case of PGA the glycan moiety can constitute an extra site for the co |
| Handle: | http://hdl.handle.net/11368/1690707 |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1002/adsc.200600337 |
| Appare nelle tipologie: | 1.1 Articolo in Rivista |
