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

被引：36

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

来源：

BIOTECHNOLOGY JOURNAL | 2017年 / 12卷 / 08期

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.

引用

页数：7

共 27 条

[1] Surface Engineering of a Cutinase From Thermobifida Cellulosilytica for Improved Polyester Hydrolysis [J].

Acero, Enrique Herrero ;

Ribitsch, Doris ;

Dellacher, Anita ;

Zitzenbacher, Sabine ;

Marold, Annemarie ;

Steinkellner, Georg ;

Gruber, Karl ;

Schwab, Helmut ;

Guebitz, Georg M. .

BIOTECHNOLOGY AND BIOENGINEERING, 2013, 110 (10) :2581-2590

[2] Tailoring cutinase activity towards polyethylene terephthalate and polyamide 6,6 fibers [J].

Araujo, Rita ;

Silva, Carla ;

O'Neill, Alexandre ;

Micaelo, Nuno ;

Guebitz, Georg ;

Soares, Claudio M. ;

Casal, Margarida ;

Cavaco-Paulo, Artur .

JOURNAL OF BIOTECHNOLOGY, 2007, 128 (04) :849-857

[3]

Asti A, 2014, INT J ARTIF ORGANS, V37, P187, DOI [10.5301/ijao.5000307, 10.530/ijao.5000307]

[4] Characterization of a poly(butylene adipate-co-terephthalate)-hydrolyzing lipase from Pelosinus fermentans [J].

Biundo, Antonino ;

Hromic, Altijana ;

Pavkov-Keller, Tea ;

Gruber, Karl ;

Quartinello, Felice ;

Haernvall, Karolina ;

Perz, Veronika ;

Arrell, Miriam S. ;

Zinn, Manfred ;

Ribitsch, Doris ;

Guebitz, Georg M. .

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2016, 100 (04) :1753-1764

[5]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[6] Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability [J].

Choi, WC ;

Kim, MH ;

Ro, HS ;

Ryu, SR ;

Oh, TK ;

Lee, JK .

FEBS LETTERS, 2005, 579 (16) :3461-3466

[7] Two Novel Class II Hydrophobins from Trichoderma spp. Stimulate Enzymatic Hydrolysis of Poly(Ethylene Terephthalate) when Expressed as Fusion Proteins [J].

Espino-Rammer, Liliana ;

Ribitsch, Doris ;

Przylucka, Agnieszka ;

Marold, Annemarie ;

Greimel, Katrin J. ;

Acero, Enrique Herrero ;

Guebitz, Georg M. ;

Kubicek, Christian P. ;

Druzhinina, Irina S. .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2013, 79 (14) :4230-4238

[8] Enzymes go big: surface hydrolysis and functionalisation of synthetic polymers [J].

Guebitz, Georg M. ;

Cavaco-Paulo, Artur .

TRENDS IN BIOTECHNOLOGY, 2008, 26 (01) :32-38

[9] Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase [J].

Jeong, ST ;

Kim, HK ;

Kim, SJ ;

Chi, SW ;

Pan, JG ;

Oh, TK ;

Ryu, SE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (19) :17041-17047

[10] Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolution [J].

Kitadokoro, Kengo ;

Thumarat, Uschara ;

Nakamura, Ryota ;

Nishimura, Kousuke ;

Karatani, Hajime ;

Suzuki, Hideyuki ;

Kawai, Fusako .

POLYMER DEGRADATION AND STABILITY, 2012, 97 (05) :771-775

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