Surface engineering of polyester-degrading enzymes to improve efficiency and tune specificity

被引：50
作者：
Biundo, Antonino [1 ]
Ribitsch, Doris [1 ,2 ]
Guebitz, Georg M. [1 ,2 ]
机构：
[1] Austrian Ctr Ind Biotechnol, Tulln An Der Donau, Austria
[2] Univ Nat Resources & Life Sci BOKU, Inst Environm Biotechnol, Tulln An Der Donau, Austria
来源：
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2018年 / 102卷 / 08期
关键词：
Carboxylesterases; Polyesters; Enzyme engineering; Hydrolysis; PET; Polyesterases; CUTINASE-CATALYZED HYDROLYSIS; THERMOBIFIDA-FUSCA CUTINASE; POLYETHYLENE TEREPHTHALATE; ENZYMATIC-HYDROLYSIS; PET; POLY(ETHYLENE-TEREPHTHALATE); HYDROLASE; ESTERASE; FUSION; FUNCTIONALIZATION;
D O I：
10.1007/s00253-018-8850-7
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Certain members of the carboxylesterase superfamily can act at the interface between water and water-insoluble substrates. However, nonnatural bulky polyesters usually are not efficiently hydrolyzed. In the recent years, the potential of enzyme engineering to improve hydrolysis of synthetic polyesters has been demonstrated. Regions on the enzyme surface have been modified by using site-directed mutagenesis in order to tune sorption processes through increased hydrophobicity of the enzyme surface. Such modifications can involve specific amino acid substitutions, addition of binding modules, or truncation of entire domains improving sorption properties and/or dynamics of the enzyme. In this review, we provide a comprehensive overview on different strategies developed in the recent years for enzyme surface engineering to improve the activity of polyester-hydrolyzing enzymes.
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收藏
页码：3551 / 3559
页数：9
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