Biocatalysis in Polymer Chemistry E-Book

• Herausgeber: Wiley-VCH
• Kategorie: Wissenschaft und neue Technologien
• Sprache: Englisch

Seitenzahl: 761

Veröffentlichungsjahr: 2011

Beschreibung

Searching for green and environmentally friendly polymerization methods by using enzymes? This first handbook on this hot and essential topic contains the whole chain of knowledge of biocatalysis in polymer chemistry in both a comprehensive and compact form. International leading experts cover all important aspects, from enzymatic monomer synthesis to polymer modification and degradation. While the major focus of the book is on enzymatic polymerizations of the polymer classes reported so far, industrial contributions are also included, making this invaluable reading for biochemists and polymer chemists working in academia and industry.

Leseprobe

Contents

Preface

List of Contributors

List of Abbreviations

1: Monomers and Macromonomers from Renewable Resources

1.1 Introduction

1.2 Terpenes

1.3 Rosin

1.4 Sugars

1.5 Glycerol and Monomers Derived Therefrom

1.6 Furans

1.7 Vegetable Oils

1.8 Tannins

1.9 Lignin Fragments

1.10 Suberin Fragments

1.11 Miscellaneous Monomers

1.12 Conclusions

2: Enzyme Immobilization on Layered and Nanostructured Materials

2.1 Introduction

2.2 Enzymes Immobilized on Layered Materials

2.3 Enzymes Immobilized on Carbon Nanotubes

2.4 Enzymes Immobilized on Nanoparticles

2.5 Conclusions

3: Improved Immobilization Supports for Candida Antarctica Lipase B

3.1 Introduction

3.2 Industrial Enzyme Production

3.3 Lipase for Biocatalysis

3.4 Immobilization

3.5 CALB- Catalyzed Polymer Synthesis

3.6 Conclusions

4: Enzymatic Polymerization of Polyester

4.1 Introduction

4.2 Synthesis of Polyesters

4.3 Enzyme-Catalyzed Polycondensations

4.4 Enzyme-Catalyzed Ring-Opening Polymerizations

4.5 Enzymatic Ring-Opening Copolymerizations

4.6 Combination of Condensation and Ring-Opening Polymerization

4.7 Conclusion

5: Enzyme-Catalyzed Synthesis of Polyamides and Polypeptides

5.1 Introduction

5.2 Catalysis via Protease

5.3 Catalysis via Lipase

5.4 Catalysis via Other Enzymes

5.5 Comments

6: Enzymatic Polymerization of Vinyl Polymers

6.1 Introduction

6.2 General Mechanism and Enzyme Kinetics

6.3 Peroxidase-Initiated Polymerizations

6.4 Laccase-Initiated Polymerization

6.5 Miscellaneous Enzyme Systems

6.6 The Current State-of-the-Art and Future Developments

7: Enzymatic Polymerization of Phenolic Monomers

7.1 Introduction

7.2 Peroxidase-Catalyzed Polymerization of Phenolics

7.3 Peroxidase-Catalyzed Synthesis of Functional Phenolic Polymers

7.5 Enzymatic Preparation of Coatings

7.6 Enzymatic Oxidative Polymerization of Flavonoids

7.7 Concluding Remarks

8: Enzymatic Synthesis of Polyaniline and Other Electrically Conductive Polymers

8.1 Introduction

8.2 PANI Synthesis Using Templates

8.3 Synthesis of PANI in Template-Free, Dispersed and Micellar Media

8.4 Biomimetic Synthesis of PANI

8.5 Synthesis of PANI Using Enzymes Different From HRP

8.6 PANI Films and Nanowires Prepared with Enzymatically Synthesized PANI

8.7 Enzymatic and Biocatalytic Synthesis of Other Conductive Polymers

8.8 Conclusions

9: Enzymatic Polymerizations of Polysaccharides

9.1 Introduction

9.2 Glycosyltransferases

9.3 Glycosidases

9.4 Conclusion

10: Polymerases for Biosynthesis of Storage Compounds

10.1 Introduction

10.2 Polyhydroxyalkanoate Synthases

10.3 Cyanophycin Synthetases

10.4 Conclusions

11: Chiral Polymers by Lipase Catalysis

11.1 Introduction

11.2 Reaction Mechanism and Enantioselectivity of Lipases

11.3 Lipase-catalyzed Synthesis and Polymerization of Optically Pure Monomers

11.4 Kinetic Resolution Polymerization of Racemic Monomers

11.5 Dynamic Kinetic Resolution Polymerization of Racemic Monomers

11.6 Tuning Polymer Properties with Chirality

11.7 Conclusions and Outlook

12: Enzymes in the Synthesis of Block and Graft Copolymers

12.1 Introduction

12.2 Synthetic Strategies for Block Copolymer Synthesis Involving Enzymes

12.3 Enzymatic Synthesis of Graft Copolymers

12.4 Summary and Outlook

13: Biocatalytic Polymerization in Exotic Solvents

13.1 Supercritical Fluids

13.2 Biocatalytic Polymerization in Ionic Liquids

13.3 Enzymatic Polymerization under Biphasic Conditions

13.4 Other ‘Exotic’ Media for Biocatalytic Polymerization

13.5 Conclusion

14: Molecular Modeling Approach to Enzymatic Polymerization

14.1 Introduction

14.2 Enzymatic Polymerization

14.3 Candida antarctica Lipase B - Characterization of a Versatile Biocatalyst

14.4 Lipase Catalyzed Alcoholysis and Aminolysis of Esters

14.5 Lipase-Catalyzed Polyester Formation

14.6 CALB -Catalyzed Polymerization of β-Lactam

14.7 General Remarks

15: Enzymatic Polymer Modification

15.1 Introduction

15.2 Enzymatic Polymer Functionalization: From Natural to Synthetic Materials

15.3 Surface Hydrolysis of Poly(alkyleneterephthalate)s

15.4 Surface Hydrolysis of Polyamides

15.5 Surface Hydrolysis of Polyacrylonitriles

15.6 Future Developments

16: Enzymatic Polysaccharide Degradation

16.1 The Features of the Enzymatic Degradation

16.2 Enzymatic Synthesis and Degradation of Cyclodextrin

16.3 Hyaluronic Acid Enzymatic Degradation

16.4 Alginate Enzymatic Degradation

16.5 Chitin and Chitosan Enzymatic Degradation

16.6 Cellulose Enzymatic Degradation

16.7 Conclusion

Index

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ISBN: 978–3-527-32618-1

Preface

Biocatalytic pathways to polymeric materials are an emerging research area with not only enormous scientific and technological promise, but also a tremendous impact on environmental issues.

Whole cell biocatalysis has been exploited for thousands of years. Historically biotechnology was manifested in skills such as the manufacture of wines, beer, cheese etc., where the techniques were well worked out and reproducible, while the biochemical mechanism was not understood.

While the chemical, economic and social advantages of biocatalysis over traditional chemical approaches were recognized a long time ago, their application to industrial production processes have been largely neglected until recent breakthroughs in modern biotechnology (such as robust protein expression systems, directed evolution etc). Subsequently, in recent years, biotechnology has established itself as an indispensable tool in the synthesis of small molecules in the pharmaceutical sector including antibiotics, recombinant proteins and vaccines and monoclonal antibodies.

Enzymatic polymerizations are a powerful and versatile approach which can compete with chemical and physical techniques to produce known materials such as ‘commodity plastics’ and also to synthesize novel macromolecules so far not accessible via traditional chemical approaches.

Enzymatic polymerizations can prevent waste generation by using catalytic processes with high stereo- and regio-selectivity; prevent or limit the use of hazardous organic reagents by, for instance, using water as a green solvent; design processes with higher energy efficiency and safer chemistry by conducting reactions at room temperature under ambient atmosphere; and increase atom efficiency by avoiding extensive protection and deprotection steps. Because of this enzymatic polymerizations can provide an essential contribution to achieving industrial sustainability in the future.

In addition, nature achieves complete control over the composition and polydispersities of natural polymers - an achievement lacking in modern polymer synthesis even by using living polymerization techniques. Biotechnology therefore holds tremendous opportunities for realizing unique new functional polymeric materials.

In this first textbook on the topic we aim to give a comprehensive overview on the current status of the field of sustainable, eco-efficient and competitive production of (novel) polymeric materials via enzymatic polymerization. Furthermore an outlook on the future trends in this field is given.

Enzyme Systems Discussed

Enzymes are responsible for almost all biosynthetic processes in living cells. These biosynthetic reactions proceed under mild and neutral conditions at a low temperature and in a quantitative conversion. This, together with the high catalytic activity and selectivity, makes enzymes highly dedicated catalysts. The reaction rates of enzyme catalyzed reactions are typically 106 to 1012 times greater than the uncatalyzed reactions but can be as high as 1017. In general, the selectivity is higher than conventional catalysts and side products are rarely formed.

According to the first report of the Enzyme Commision from 1961 all enzymes are classified in six enzyme classes, depending on the reaction being catalyzed. Within the scheme of identification each enzyme has an Enzyme Commission number denominated by four numbers after the abbreviation E.C. The first number indicates one of the six possible reaction types that the enzyme can catalyze; the second number defines the chemical structures that are changed in this process; the third defines the properties of the enzyme involved in the catalytic reaction or further characteristics of the catalyzed reaction; the fourth number is a running number.

At present, enzymes from 4 of the 6 E.C. enzyme classes are known to induce or catalyze polymerizations. An overview of the main enzyme and polymer systems discussed in this book is shown in the following table.

Outline of This Book

Biocatalytic approaches in polymer synthesis have to include an optimized combination of biotechnological with classical processes. Therefore, this book starts with a thorough review on the sustainable, ‘green’ synthesis of monomeric materials (Chapter 1). While few of the monomers presented in this chapter have been used in enzymatic polymerizations so far, the examples given could provide inspiration to use sustainable monomers more often in the future for enzymatic polymerizations and also for classical approaches.

Many of the polymerizations presented in this book proceed in organic solvents. To enhance the stability of enzymes in these solvent systems and to ensure efficient recovery of the biocatalysts the enzymes are commonly immobilized. Chapter 2 reviews some of the new trends of enzyme immobilization on nanoscale materials, while Chapter 3 sheds light on some new approaches to improve the commercial immobilization of Candida antarctica lipase B - the biocatalyst most often employed in enzymatic polymer synthesis.

The most extensively studied enzymatic polymerization system is that of polyesters via polycondensations or ring-opening polymerizations. The state of the art of in vitro enzymatic polyester synthesis is reviewed in Chapter 4.

Polyamides are important engineering plastics and excellent fiber materials and their worldwide production amounts to a few million tons annually. Therefore, it is astonishing that not many approaches to synthesize polyamides via enzymatic polymerization have been reported so far. Chapter 5 reviews these approaches and hopefully inspires future research in this direction.

In Chapter 6 the enzymatic polymerization of vinyl monomers is presented. Polymers, such as polystyrene and poly(meth)acrylates can be readily polymerized under catalysis of oxidoreductases like peroxidases, oxidases, etc. In addition oxidoreductases can be used to polymerize phenolic monomers (Chapter 7) and even to synthesize conducting polymers such as polyaniline (Chapter 8).

Well-defined polysaccharides are extremely difficult to synthesize via conventional organic chemistry pathways due to the diverse stereochemistry of the monosaccharide building blocks and the enormous number of intersugar linkages that can be formed. Chapter 9 shows that enzymatic polymerizations are superior alternatives to traditional approaches to synthesize polysaccharides.

The synthesis of bacterial storage compounds is reviewed in Chapter 10, focusing on two systems, namely polyhydroxyalkanoic acids and cyanophycin. Bacterial storage compounds are very interesting biopolymers having attractive material properties, sometimes similar to those of the petrochemical-based polymers.

Chapter 11 draws our attention towards the possibility of synthesizing chiral polymers via biocatalytic pathways. It becomes obvious in that chapter that chiral macromolecules can be achieved by enzymatic polymerizations that would not be synthesizable via traditional methods.

At present not many block copolymer systems using enzymatic polymerizations are reported. Chapter 12 reviews the current status of this field and shows the potential of future research in this direction.

Many enzymatic polymerizations suffer from low solubility of the synthesized polymers limiting the obtained degree of polymerization (e.g. polyamides, cellulose etc.). Chapter 13 illustrates several solutions by reviewing ‘exotic’ solvents and the possibilities of using them in biocatalysis. Not many reports on using such solvent systems for enzymatic polymerizations have yet been reported but the potential of such solvent systems becomes obvious immediately.

Chapter 14 introduces an interesting way to establish/solve the mechanism of enzymatic polymerizations via computer simulation. This method is quite wellestablished in other fields of chemistry but has only been used for solving the reaction mechanism of one enzymatic polymerization (the enzymatic ring opening polymerization of β-lactam). The outline of the technique in this chapter proves the power of this method and hopefully inspires future research on other enzymatic polymerization mechanisms.

In Chapters 15 and 16 the modification and degradation of respectively synthetic (e.g. PET, polyamides) and natural polymers (e.g. polysaccharides) are reviewed. It becomes obvious that biocatalytic modifications can offer advantages over chemical modifications therefore building a bridge between ‘traditional’ polymerization techniques and enzymatic polymerizations.

On most topics described in these chapters an increase in publications in recent years can be observed. This is a very promising trend showing that more and more researchers realize the importance of enzymatic polymerizations. We hope that with this book we can attract more researchers worldwide to this field and thus to tremendously extend the range of polymer classes synthesized by enzymes so far.

Acknowledgement

First of all I would like to acknowledge all authors of this book for their contribution to the book content. Each author is a leading authority in her/his field and generously offered effort and time to make this book a success.

Many thanks go to Iris Baum and Lars Haller for designing the cover and creating the lipase structure shown on the cover. Frank Brouwer is acknowledged for providing the photo on the book cover.

In addition, I would like to thank the Wiley team - especially Heike Nöthe, Elke Maase, Claudia Nussbeck, Hans-Jochen Schmitt, Rebecca Hübner und Mary Korndorffer - for their professional support, assistance and encouragement to make this book a reality.

Katja LoosGroningen, August 2010

Enzymatic Polymerizations

Book Series

Palmans, A., and K. Hult, eds. Enzymatic Polymerizations. Advances in Polymer Science Vol. 237. 2010, Springer.

Cheng, H.N., and R.A. Gross, eds. Green Polymer Chemistry: Biocatalysis and Biomaterials. ACS Symposium Series. Vol. 1043. 2010, American Chemical Society.

Cheng, H.N., and R.A. Gross, eds. Polymer Biocatalysis and Biomaterials II. ACS Symposium Series. Vol. 999. 2008, American Chemical Society.

Kobayashi, S., H. Ritter, and D. Kaplan, eds. Enzyme-Catalyzed Synthesis of Polymers. Advances in Polymer Science. Vol. 194. 2006, Springer.

Cheng, H.N., and R.A. Gross, eds. Polymer Biocatalysis and Biomaterials. ACS Symposium Series. Vol. 900. 2005, American Chemical Society.

Gross, R.A., and H.N. Cheng, eds. Biocatalysis in Polymer Science. ACS Symposium Series. Vol. 840. 2002, American Chemical Society.

Scholz, C., and R.A. Gross, eds. Polymers from Renewable Resources: Biopolyesters and Biocatalysis. ACS Symposium Series. Vol. 764. 2000, American Chemical Society.

Gross, R.A., D.L. Kaplan, and G. Swift, eds. Enzymes in Polymer Synthesis. ACS Symposium Series. Vol. 684. 1998, American Chemical Society.

Review Articles

Kobayashi, S., Makino, A., Chemical Reviews 2009, 109, 5288.

Kobayashi, S., Uyama, H., Kimura, S., Chemical Reviews 2001, 101, 3793.

Gross, R.A., Kumar, A., Kalra, B., Chemical Reviews 2001, 101, 2097.

Kobayashi, S., Journal of Polymer Science Part A-Polymer Chemistry 1999, 37, 3041.

Kobayashi, S., Shoda, S.-i., Uyama, H., in Advances in Polymer Science, Vol. 121, 1995, pp. 1.

Biocatalysis

Books

Fessner, W.-D., Anthonsen, T., Modern Biocatalysis: Stereoselective and Environmentally Friendly Reactions, Wiley-VCH 2009.

Tao, J., Lin, G.-Q., Liese, A., Biocatalysis for the Pharmaceutical Industry–Discovery, Development, and Manufacturing, John Wiley & Sons, 2009.

Grunwald, P., Biocatalysis: Biochemical Fundamentals and Applications, Imperial College Press 2009.

Liese, A., Seelbach, K., Wandrey, C., Industrial Biotransformations, Wiley-VCH, 2006.

Faber, K., Biotransformations in Organic Chemistry: A Textbook, Springer, 2004.

Bommarius, A.S., Riebel, B.R., Biocatalysis – Fundamentals and Applications, Wiley-VCH, 2004.

Drauz, K., Waldmann, H., Enzyme Catalysis in Organic Synthesis: A Comprehensive Handbook, Wiley-VCH, 2002.

List of Contributors

Iris Baum

University of Paderborn Department of Chemistry Warburger Straße 100 33098 Paderborn Germany

Jesper Brask

Novozymes A/S Krogshoejvej 36 2880 Bagsvaerd Denmark

Anna Bröker

Westfälische Wilhelms-Universität Münster Institut für Molekulare Mikrobiologie und Biotechnologie Corrensstrasse 3 48149 Münster Germany

H. N. Cheng

USDA Agricultural Research Service Southern Regional Research Center 1100 Robert E. Lee Blvd. New Orleans, LA 70124 USA

Rodolfo Cruz-Silva

Universidad Autonoma del Estado de Morelos Centro de Investigacion en Ingenieria y Ciencias Aplicadas Ave. Universidad 1001 Col. Chamilpa Cuernavaca, Morelos, CP62209 Mexico

Apostolos Enotiadis

University of Ioannina Department of Materials Science and Engineering 45110 Ioannina Greece

Gregor Fels

University of Paderborn Department of Chemistry Warburger Straße 100 33098 Paderborn Germany

Alessandro Gandini

University of Aveiro CICECO and Chemistry Department 3810–193 Aveiro Portugal

Dimitrios Gournis

University of Ioannina Department of Materials Science and Engineering 45110 Ioannina Greece

Richard A. Gross

Fruit Research Institute Kralja Petra I no 9 32000 Čačak Serbia

Georg M. Guebitz

Graz University of Technology Department of Environmental Biotechnology Petersgasse 12 8010 Graz Austria

Andreas Heise

Dublin City University School of Chemical Sciences Glasnevin Dublin 9 Ireland

Frank Hollmann

Delft University of Technology Department of Biotechnology Biocatalysis and Organic Chemistry Julianalaan 136 2628BL Delft The Netherlands

Steven Howdle

University of Nottingham School of Chemistry University Park Nottingham NG7 2RD UK

Katja Loos

University of Groningen Zernike Institute for Advanced Materials Department of Polymer Chemistry Nijenborgh 4 9747 AG Groningen The Netherlands

Nemanja Miletic

Fruit Research Institute Kralja Petra I no 9 32000 Čačak Serbia

Maricica Munteanu

Heinrich-Heine-Universität Düsseldorf Institute für Organische Chemie und Makromolekulare Chemie Lehrstuhl II Universitätsstraße 1 40225 Düsseldorf Germany

Anja Palmans

Eindhoven University of Technology Department of Chemical Engineering and Chemistry Molecular Science and Technology PO Box 513 5600 MB Eindhoven The Netherlands

Ioannis V. Pavlidis

University of Ioannina Department of Biological Applications and Technologies 45110 Ioannina Greece

Helmut Ritter

Heinrich-Heine-Universität Düsseldorf Institute für Organische Chemie und Makromolekulare Chemie Lehrstuhl II Universitätsstraße 1 40225 Düsseldorf Germany

Paulina Roman

Universidad Autonoma del Estado de Morelos Centro de Investigacion en Ingenieria y Ciencias Aplicadas Ave. Universidad 1001 Col. Chamilpa Cuernavaca, Morelos, CP62209 Mexico

Jorge Romero

Centro de Investigacion en Quimica Aplicada Blvd. Enrique Reyna 120 Col. Los Pinos Saltillo, Coahuila, CP 25250 Mexico

Paria Saunders

Novozymes North America Inc. 77 Perry Chapel Church Road Franklinton, NC 27525 USA

Haralambos Stamatis

University of Ioannina Department of Biological Applications and Technologies 45110 Ioannina Greece

Alexander Steinbüchel

Westfälische Wilhelms-Universität Münster Institut für Molekulare Mikrobiologie und Biotechnologie Corrensstrasse 3 48149 Münster Germany

Kristofer J. Thurecht

The University of Queensland Australian Institute for Bioengineering and Nanotechnology and Centre for Advanced Imaging St Lucia, Queensland, 4072 Australia

Aikaterini A. Tzialla

University of Ioannina Department of Biological Applications and Technologies 45110 Ioannina Greece

Hiroshi Uyama

Osaka University Graduate School of Engineering Department of Applied Chemistry Suita 565–0871 Japan

Martijn Veld

Eindhoven University of Technology Department of Chemical Engineering and Chemistry Molecular Science and Technology PO Box 513 5600 MB Eindhoven The Netherlands

Silvia Villarroya

G24 Innovations Limited Wentloog Environmental Centre Cardiff CF3 2EE United Kingdom

Jeroen van der Vlist

University of Groningen Faculty of Mathematics and Natural Sciences Department of Polymer Chemistry Zernike Institute for Advanced Materials Nijenborgh 4 9747 AG Groningen The Netherlands

List of Abbreviations

3D

three-dimensional

3-MePL

α-methyl-β-propiolactone

3MP

3-mercaptopropionic acid

4MCL

4-methyl caprolactone

4-MeBL

α-methyl-γ-butyrolactone

5-MeVL

α-methyl-δ-valerolactone

6-MeCL

α-methyl-ε-caprolactone

7-MeHL

α-methyl-ζ-heptalactone

8-MeOL

α-methyl-8-octanolide

8-OL

8-octanolide

10-HA

10-hydroxydecanoic acid

11MU

11-mercaptoundecanoic acid

12-MeDDL

α-methyl-dodecanolactone

ABTS

2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) diammonium salt

Acac

acetylacetone

ADM

Archer Daniels Midland

ADP

adenosine diphosphate

AM

amylose

AP

Amylopectin

ATP

adenosine triphosphate

ATRP

atom transfer radical polymerization

BCL

Burkholderia cepacia lipase

BG

benzyl glycidate

BHET

bis(2-hydroxyethyl) terephthalate

BMIM BF4

1-butyl-3-methylimidazolium tetrafluoroborate

BMIM DCA

1-butyl-3-methylimidazolium dicyanamide

BMIM FeCl4

1-butyl-3-methylimidazolium tetrachloroferrate

BMIM NTf2

1-butyl-3-methylimidazolium bistriflamide

BMIM PF6

1-butyl-3-methylimidazolium hexafluorophosphate

BMPy BF4

1-butyl-1-methylpyrrolidinium tetrafluoroborate

BMPy DCA

1-butyl-1-methylpyrrolidinium dicyanamide

BOD

bilirubin oxidase

BPAA

Biphenyl acetic acid

BrNP

2-(bromonethyl)naphthalene

BSA

bovine serum albumin

BTMC

5-benzyloxytrimethylene carbonate

Buk

butyrate kinase

CA

Candida antarctica

CAL

Candida antarctica lipase

CALB

Candida antarctica lipase B

CCK

cholecystokinin

CCVD

catalytical chemical vapor deposition

CD

circular dichroism (Chapter 2)

CD

cyclodextrin (Chapter 7, 16)

CDase

cyclomaltodextrinase

CGP

cyanophycin granule polypeptide, cyanophycin

CGTase

cyclodextrin glycosyltransferase

CL

caprolactone

CMC

critical micellar concentration

CMD

cyclomaltodextrinase

CNSL

cashew nut shell liquid

CNT

carbon nanotube

CphA

cyanophycin synthetase

CphB

cyanophycinase

CPO

chloroperoxidase

CRL

Candida rugosa lipase

CS

chondroitin sulfate

CSA

camphor sulfonic acid

CSD

Cambridge structural database

CTAB

cetyltrimethylammonium bromide

CVL

Chromobacterium viscosum lipase

DA

degree of acetylation

DA

Diels–Alder

DB

degrees of branching

DBSA

dodecylbenzensulfonic acid

DDL

ω-dodecanolactone

DFT

density function theory

DKR

dynamic kinetic resolution

DKRP

dynamic kinetic resolution polymerization

DLLA

D,L-lactide

DMA

dimethyl adipate

DMP

2,4-dimethyl-3-pentanol

DMSO

dimethyl sulfoxide

DM-β-CD

2,6-di-O-methyl-β-cyclodextrin

DM-α-CD

2,6-di-O-methyl-α-cyclodextrin

DNA

deoxyribonucleic acid

DO

p-dioxanone

DODD

dodecyl diphenyloxide disulfonate

DON

1,4-dioxan-2-one

DP

degree of polymerization

DSC

differential scanning calorimetry

DTA

differential thermal analysis

DTC

5,5-dimethyl-trimethylene carbonate

DTNB

5,5′-dithiobis-(2-nitrobenzoic acid)

DWCNT

double-wall carbon nanotube

DXO

1,5-dioxepan-2-one

EACS

enzyme activated chain segment

EAM

enzyme activated monomer

EC

(−)-epicatechin (Chapter 7)

EC

Enzyme Commission (Chapter 9)

ECG

(−)-epicatechin gallate

ECM

extracellular matrix

EDC

1-ethyl-3-(3-dimethylaminopropyl) carbodiimide

EDOT

(3,4-ethylendioxythiophene)

ee

enantiomeric excess

EG

ethylene glycol

EGC

(−)-epigallocatechin

EGCG

(−)-epigallocatechin gallate

EGP

ethyl glucopyranoside

eROP

enzymatic ring-opening polymerization

eROP

enzyme-catalyzed ring-opening polymerization

ESI-MS

electrospray ionization mass spectrometry

F

furfural

FA

furfuryl alcohol

f-CNT

functionalized CNT

FED

flexible electronic device

FOMA

perfluorooctyl methacrylate

FT-IR

Fourier transform infrared

GA

glutaraldehyde

GAG

glycosaminoglycan

GAP

granule-associated protein

GCE

glassy carbon electrode

GlcA

d-glucuronic acid

GMA

glycidyl methacrylate

GME

glycidyl methyl ether

GPC

gel permeation chromatography

GPE

glycidyl phenyl ether

GPEC

gradient polymer elution chromatography

GT

glycosyltransferase

GTFR

glycosyltransferase R

HA

hyaluronan

HAS

hyaluronan synthase

HDL

hexadecanolactone

HEMA

hydroxyethyl methacrylate

HiC

Humicola insolens cutinase

HiC-AO

Humicola insolens cutinase immobilized on Amberzyme oxiranes

HMF

hydroxymethylfuraldehyde

HMWHA

high-molecular-weight HA

HPLC

high performance liquid chromatography

HRP

horseradish peroxidase

ICP

intrinsically conducting polymer

IL

ionic liquid

IPDM

3(S)-isopropylmorpholine-2,5-dione

IPPL

immobilized porcine pancreas lipase

ITC

iterative tandem catalysis

ITO

indium tin oxide

KRP

kinetic resolution polymerization

L

large

lacOCA

pure lactic acid derived O-carboxy anhydride

LCCC

liquid chromatography under critical condition

LDL

low-density lipoprotein

LLA

lactide

LMS

laccase-mediator-system

LMWC

low-molecular-weight chitosan

LMWHA

low-molecular-weight HA

LS

light scattering

M

medium

MA

malic acid

MALS

multi-angle light scattering

MBC

5-methyl-5-benzyloxycarbonyl-1,3-dioxan-2-one

MBS

maltose-binding site

MCL

4-methyl caprolactone (Chapter 12)

MCL

medium-carbon-chain length (Chapter 10)

MD

molecular dynamics

MDI

methylene-diphenyl diisocyanate

MF

5-methylfurfural

MHET

mono(2-hydroxyethyl) terephthalate

ML

laccase derived from Myceliophthore

MM

molecular mechanics

MMA

methyl methacrylate

MML

Mucor miehei lipase

MNP

Magnetic nanoparticle

MOHEL

3-methyl-4-oxa-6-hexanolide

MPEG

methoxy-PEG

MRI

magnetic resonance imaging

mRNA

messenger ribonucleic acid

MW

molecular weight

MWCNT

multi-wall carbon nanotube

NAG

N-acetylglucosamine

NMP

nitroxide-mediated polymerization (Chapter 11, 12)

NMP

N-methyl-2-pyrrolidinone (Chapter 8)

NMR

nuclear magnetic resonance

NP

nanoparticle

NRPS

nonribosomal peptide synthetases

O/W

oil-in-water

OC

2-oxo-12-crown-4-ether

OCP

open circuit potential

OMIM DCA

1-octyl-3-methylimidazolium dicyanamide

PA

phthalic anhydride

PA

polyamide

Pam

peptide amidase

PAMPS

poly(2-acrylamido-3-methyl-1-propanesulfonic acid)

PAN

polyacrylonitrile

PANI

polyaniline

PAT

poly(alkylene terephthalate)

PBS

poly(butylene succinate)

PCL

Laccase derived from Pycnoporus coccineus

PCL

polycaprolactone (Chapter 3, 4)

PCL

proceeded using laccase (Chapter 7)

PCL

Pseudomonas cepacia lipase (Chapter 11, 12, 13)

PDADMAC

poly(diallyldimethyl ammonium chloride)

PDB

protein database

PDDA

poly(dimethyl diallylammonium chloride)

PDI

polydispersity index

PDL

pentadecalactone

PDMS

poly(dimethylsiloxane)

PEDOT

poly(3,4-ethylendioxythiophene)

PEF

poly(2,5-ethylene furancarboxylate)

PEG

poly(ethylene glycol)

PEGMA

poly(ethylene glycol) methacrylate

PEI

polyethyleneimine

PET

poly(ethylene terephthalate)

PFL

Pseudomonas fluorescens lipase

PGA

poly-(γ-glutamate)

PHA

polyhydroxyalkanoic acid (Chapter 10)

PhaC

PHA synthase

PhaG

3-hydroxyacyl-ACP:CoA transferase

PHB

poly(3-hydroxybutyrate) (Chapter 10)

PHB

poly[(R)-3-hydroxybutyrate] (Chapter 11, 12)

Pi

inorganic phosphate

pI

isoelectric point

PL

poly-(ε-lysine)

PLA

polylactic acid

PLP

pyridoxal-5′-phosphate

PLU

propyl laurate units

POA

poly(octamethylene adipate)

poly(ε-CL)

poly(ε-caprolactone)

PPG

PEG-poly(propylene glycol)

PPL

porcine pancreatic lipase

PPO

poly(phenylene oxide)

PPP

pentose phosphate pathway

PPy

polypyrrole

PS

Polystyrene

PSorA

poly(sorbitol adipate)

Ptb

phosphotransbutyrylase

PTE

polythioester

PTHF

poly(tetrahydrofuran)

PTP

palm tree peroxidase

PTT

poly(trimethyleneterephthalate)

PVA

poly(vinyl alcohol)

PVP-OH

mono-hydroxyl poly(vinyl pyrolidone)

QCM

quartz crystal microbalance

QM

quantum mechanical

RAFT

reversible addition fragmentation chain-transfer

RI

refractive index

ROP

ring opening polymerization

ROS

reactive oxygen species

RTIL

room temperature ionic liquid

SA

succinic anhydride

SBE

starch branching enzyme

SBP

soybean peroxidase

scCO2

supercritical CO2

SCL

short-carbon-chain length

SDBS

sodium dodecylbenzensulfonate

SDS

sodium dodecyl sulfate

SEC

size exclusion chromatography

SEM

scanning electron microscopy

SET

single electron transfer

SO

styrene oxide

SP

starch-urea phosphate

SPS

sulfonated polystyrene

SWCNT

single-wall carbon nanotube

TA

terephthalic acid

TGA

thermogravimetric analysis

THF

tetrahydrofuran

TMC

trimethylene carbonate

TMP

trimethylolpropane

TSA

toluene sulfonic acid

TVL

laccase from Trametes versicolor

UDL

undecanolactone

UV-Vis

ultraviolet-visible

VOC

volatile organic compound

w/c

water-in-CO2

WCA

water contact angle

XO

xanthine oxidase

XPS

X-ray photoelectron spectroscopy

XRD

X-ray diffraction

β-PL

β-propiolactone

δ-VL

δ-valerolactone

ε-CL

ε-caprolactone

ωHA

ω-hydroxyalkanoic acids

1

Monomers and Macromonomers from Renewable Resources

Alessandro Gandini

1.1 Introduction

Renewable resources constitute an extremely rich and varied array of molecules and macromolecules incessantly produced by natural biological activities thanks to solar energy. Their exploitation by mankind has always been at the heart of its survival as sources of food, remedies, clothing, shelter, energy, etc., and of its leisure as sources of flowers, dyes, fragrances, and other amenities. In the specific context of materials, good use has always been made of cotton, paper, starch products, wool, silk, gelatin, leather, natural rubber, vegetable oils and terpenes, among others, through progressively more sophisticated and scaled-up technologies.

The meteoric ascension of coal and petroleum chemistry throughout the twentieth century gave rise to the extraordinary surge of a wide variety of original macromolecules derived from the rich diversity of monomers available through these novel synthetic routes. This technical revolution is still very much alive today, but the dwindling of fossil resources and their unpredictable price oscillations, mostly on the increase, is generating a growing concern about finding alternative sources of chemicals, and hence of organic materials, in a similar vein as the pressing need for more ecological and perennial sources of energy. The new paradigm of the biorefinery [1] represents the global strategic formulation of such an alternative in both the chemical and the energy fields, with progressive implementations, albeit with different approaches, throughout the planet.