Polyester hydrolysis is enhanced by a truncated esterase: Less is more

被引:32
作者
Biundo, Antonino [1 ]
Ribitsch, Doris [1 ,2 ]
Steinkellner, Georg [2 ]
Gruber, Karl [2 ,3 ]
Guebitz, Georg M. [1 ,2 ]
机构
[1] Univ Nat Resources & Life Sci BOKU, Inst Environm Biotechnol, Konrad Lorenz Str 22, A-3430 Tulln An Der Donau, Austria
[2] ACIB, Tulln An Der Donau, Austria
[3] Karl Franzens Univ Graz, Inst Mol Biosci, Graz, Austria
基金
欧盟地平线“2020”;
关键词
Biocatalysis; Enzyme engineering; Modeling; Polymers; Recombinant proteins; POLYETHYLENE TEREPHTHALATE; THERMOBIFIDA-CELLULOSILYTICA; STEAROTHERMOPHILUS L1; CUTINASE; SURFACE; BINDING; FUSION; POLY(ETHYLENE-TEREPHTHALATE); FUNCTIONALIZATION; HYDROPHOBINS;
D O I
10.1002/biot.201600450
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
An esterase from Clostridium botulinum (Cbotu_EstA) previously reported to hydrolyze the biodegradable polyester poly(butylene adipate-co-terephthalate) was redesigned to improve the hydrolysis of synthetic polyesters. Increased activity was indeed observed for del71Cbotu_EstA variant, which performed activity on the widespread polyester polyethylene terephthalate, which was not able to be attacked by the wild-type enzyme Cbotu_EstA. Analysis of the 3D structure of the enzyme showed that removing 71 residues at the N-terminus of the enzyme exposed a hydrophobic patch on the surface and improved sorption of hydrophobic polyesters concomitantly facilitating the access of the polymer to the active site. These results show a new route for enhancing enzyme activity for hydrolysis and modification of polyesters.
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页数:7
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