Designer enzyme for green materials innovation: Lactate-polymerizing enzyme as a key catalyst

Seiichi Taguchi

Front. Chem. Sci. Eng. ›› 2017, Vol. 11 ›› Issue (1) : 139 -142.

PDF (191KB)
Front. Chem. Sci. Eng. ›› 2017, Vol. 11 ›› Issue (1) : 139 -142. DOI: 10.1007/s11705-017-1636-0
VIEWS & COMMENTS
VIEWS & COMMENTS

Designer enzyme for green materials innovation: Lactate-polymerizing enzyme as a key catalyst

Author information +
History +
PDF (191KB)

Abstract

Establishment of the regeneratable whole-cell catalyst platform for the production of biobased polymeric materials is a typical topic of synthetic biology. In this commentary, discovery story of a “lactate-polymerizing enzyme” (LPE) and LPE-based achievements for creating a new variety of polyesters with incorporated unnatural monomers are presented. Besides the importance of microbial platform itself is discussed referring to the “ballooning”-Escherichia coli.

Graphical abstract

Keywords

synthetic biology / enzyme evolutionary engineering / polyhydroxyalkanoate

Cite this article

Download citation ▾
Seiichi Taguchi. Designer enzyme for green materials innovation: Lactate-polymerizing enzyme as a key catalyst. Front. Chem. Sci. Eng., 2017, 11(1): 139-142 DOI:10.1007/s11705-017-1636-0

登录浏览全文

4963

注册一个新账户 忘记密码

References

[1]

Lemoignei M. Produits dedehydration et de polymerisation delacideßoxobutyrique. Bulletin de la Société de Chimie Biologique, 1926, 8: 770–782

[2]

Doi Y, Steinbühel A.Methabolic Pathways and Engineering of PHA Biosynthesis. Weinheim: Wiley-VCH Verlag GmbH, 2002, 217–247

[3]

Lenz R W, Marchessault R H. Bacterial polyesters: Biosynthesis, biodegradable plastics and biotechnology. Biomacromolecules, 2005, 6(1): 1–8

[4]

Anderson A J, Dawes E A. Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates. Microbiological Reviews, 1990, 54(4): 450–472

[5]

Ryner M, Stridsberg K, Albertsson A N, von Schenck H, Svensson M. Mechanism of ring-opening polymerization of 1,5-dioxepan-2-one and L-lactide with stannous 2-ethylhexanoate. A theoretical study. Macromolecules, 2001, 34(12): 3877–3881

[6]

Rehm B H. Polyester synthases: Natural catalysts for plastics. Biochemical Journal, 2003, 376(1): 15–33

[7]

Taguchi S, Doi Y. Evolution of polyhydroxyalkanoate (PHA) production system by “enzyme evolution”: Successful case studies of directed evolution. Macromolecular Bioscience, 2004, 4(3): 146–156

[8]

Nomura C T, Taguchi S. PHA synthase engineering toward superbiocatalysts for custom-made biopolymers. Applied Microbiology and Biotechnology, 2006, 73(5): 969–979

[9]

Taguchi S, Yamada M, Matsumoto K, Tajima K, Satoh Y, Munekata M, Ohno K, Kohda K, Shimamura T, Kambe H, . A microbial factory for lactate-based polyesters using a lactate-polymerizing enzyme. Proceedings of the National Academy of Sciences of the United States of America, 2008, 105(45): 17323–17327

[10]

Tajima K, Satoh Y, Satoh T, Itoh R, Han X, Taguchi S, Kakuchi T, Munekata M. Chemo-enzymatic synthesis of poly(lactate-co-(3-hydroxybutyrate)) by a lactate-polymerizing enzyme. Macromolecules, 2009, 42(6): 1985–1989

[11]

Taguchi S. Current advances in microbial cell factories for lactate-based polyesters driven by lactate-polymerizing enzymes: Toward further creation of new LA-based polyesters. Polymer Degradation & Stability, 2010, 95(8): 1421–1428

[12]

Park S J, Kim T W, Kim M K, Lee S Y, Lim S C. Advanced bacterial polyhydroxyalkanoates: Towards a versatile and sustainable platform for unnatural tailor-made polyesters. Biotechnology Advances, 2012, 30(6): 1196–1206

[13]

Matsumoto K, Taguchi S. Enzyme and metabolic engineering for the production of novel polymers: Crossover of biological and chemical processes. Current Opinion in Biotechnology, 2013, 24(6): 1054–1060

[14]

Matsumoto K, Taguchi S. Biosynthetic polyesters consisting of 2-hydroxyalkanoic acids: Current challenges and unresolved questions. Applied Microbiology and Biotechnology, 2013, 97(18): 8011–8021

[15]

Volodina E, Schürmann M, Lindenkamp N, Steinbüchel A. Characterization of propionate CoA-transferase from Ralstoniaeutropha H16. Applied Microbiology and Biotechnology, 2014, 98(8): 3579–3589

[16]

Wittenborn E C, Jost M, Wei Y, Stubbe J A, Drennan C L. Structure of the catalytic domain of the class I polyhydroxybutyrate synthase from Cupriavidusnecator. Journal of Biological Chemistry, 2016, 291(48): 25264–25277

[17]

Yamada M, Matsumoto K, Uramoto S, Motohashi R, Abe H, Taguchi S. Lactate fraction dependent mechanical properties of semitransparent poly(lactate-co-3-hydroxybutyrate)s produced by control of lactyl-CoA monomer fluxes in recombinant Escherichia coli. Journal of Biotechnology, 2011, 154(4): 255–260

[18]

Utsunomia C, Matsumoto M, Taguchi S. Micobial secretion of D-lactate-based oligomers. ACS Sustainable Chemistry & Engineering, in press

[19]

Kadoya R, Matsumoto K, Ooi T, Taguchi S. MtgA deletion-triggered cell enlargement of Escherichia coli for enhanced intracellular polyester accumulation. PLoS One, 2015, 10(6): e0125163

[20]

Wu H, Chen J, Chen G Q. Engineering the growth pattern and cell morphology for enhanced PHB production by Escherichia coli. Applied Microbiology and Biotechnology, 2016, 100(23): 9907–9916

RIGHTS & PERMISSIONS

Higher Education Press and Springer-Verlag Berlin Heidelberg

AI Summary AI Mindmap
PDF (191KB)

2182

Accesses

0

Citation

Detail

Sections
Recommended

AI思维导图

/