Abstract：
:Cutinase from Fusarium solani pisi was genetically modified near the active site, by site-directed mutagenesis, to enhance its activity towards polyethylene terephthalate (PET) and polyamide 6,6 (PA 6,6) fibers. The mutations L81A, N84A, L182A, V184A and L189A were done to enlarge the active site in order to better fit a larger polymer chain. Modeling studies have shown enhanced free energy stabilization of model substrate tetrahedral intermediate (TI) bound at the enzyme active site for all mutants, for both model polymers. L81A and L182A showed an activity increase of four- and five-fold, respectively, when compared with the wild type, for PET fibers. L182A showed the one- and two-fold higher ability to biodegrade aliphatic polyamide substrates. Further studies in aliphatic polyesters seem to indicate that cutinase has higher ability to recognize aliphatic substrates.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Araújo R,Silva C,O'Neill A,Micaelo N,Guebitz G,Soares CM,Casal M,Cavaco-Paulo Adoi
10.1016/j.jbiotec.2006.12.028subject
Has Abstractpub_date
2007-03-10 00:00:00pages
849-57issue
4eissn
0168-1656issn
1873-4863pii
S0168-1656(07)00035-1journal_volume
128pub_type
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journal_title：Journal of biotechnology
pub_type： 杂志文章
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更新日期：2014-03-20 00:00:00
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更新日期：2011-08-20 00:00:00
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