Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica-Reference-Cited by-同舟云学术

Enlarging the tools for efficient enzymatic polycondensation: structural and catalytic features of cutinase 1 from Thermobifida cellulosilytica

Published:2016 Issue:10 Volume:6 Page:3430-3442
ISSN:2044-4753
Container-title:Catalysis Science & Technology
language:en
Short-container-title:Catal. Sci. Technol.

Author:

Pellis A.¹²³⁴,Ferrario V.⁵⁶⁷⁸⁹,Zartl B.¹²³⁴,Brandauer M.¹⁰¹¹³⁴,Gamerith C.¹⁰¹¹³⁴,Herrero Acero E.¹⁰¹¹³⁴,Ebert C.⁵⁶⁷⁸⁹,Gardossi L.⁵⁶⁷⁸⁹,Guebitz G. M.¹²³⁴¹⁰

Affiliation:

1. University of Natural Resources and Life Sciences

2. Institute for Environmental Biotechnology

3. 3430 Tulln an der Donau

4. Austria

5. Laboratory of Applied and Computational Biocatalysis

6. Dipartimento di Scienze Chimiche e Farmaceutiche

7. Università degli Studi di Trieste

8. Trieste

9. Italy

10. Austrian Centre of Industrial Biotechnology GmbH

11. Division Enzymes and Polymers

Abstract

Catalytic and structural properties make cutinase 1 from Thermobifida cellulosilytica a more efficient biocatalyst for polycondensations, also of short-chain monomers.

Funder

Seventh Framework Programme

European Cooperation in Science and Technology

Publisher

Royal Society of Chemistry (RSC)

Subject

Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CY/C5CY01746G

Reference64 articles.

1. Enzyme-catalysis breathes new life into polyester condensation polymerizations

2. One-Step Syntheses of Photocurable Polyesters Based on a Renewable Resource