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ENZYMATIC POLYMERIZATION
Introduction
Enzymes catalyze not only all in vivo biosynthetic reactions in living cells for main-
taining life but also many in vitro reactions of natural and unnatural substrates
under selected reaction conditions. Enzymatic catalysis for organic synthesis pos-
sesses advantages such as much acceleration of reaction rate, operation under
mild conditions, and high stereo-, regio-, and chemoselectivities of reactions in
comparison with those of chemical catalysts. Such characteristic properties have
brought about an extraordinarily rapid increase in interest in the area of biotrans-
formations (15).
All naturally occurring polymers are produced in vivo by enzymatic catalysis.
Recently, in vitro synthesis of polymers through enzymatic catalysis (enzymatic
polymerization) has been extensively studied (614); highly selective polymer-
izations catalyzed by enzymes have been developed to produce various functional
polymers in response to increasing demands of structural variation of synthetic
targets for polymers in material science.
This article deals with recent advances in enzymatic polymerizations. We
dene enzymatic polymerization as chemical polymer synthesis in vitro (in test
tubes) via nonbiosynthetic (nonmetabolic) pathways catalyzed by an isolated en-
zyme. Enzymes are generally classied into six groups. Table 1 shows typical poly-
mers produced with catalysis by respective enzymes. The target macromolecules
for the enzymatic polymerization have been polysaccharides, poly(amino acid)s,
polyesters, polycarbonates, polyaromatics, vinyl polymers, etc. Here, enzymatic
polymerizations are described according to the polymer structure. In many cases,
enzymatic polymerization enables the synthesis of polymers, which otherwise are
difcult to prepare. Enzymatic polymerization often provides an environmentally
Encyclopedia of Polymer Science and Technology. Copyright John Wiley & Sons, Inc. All rights reserved.
Vol. 2 ENZYMATIC POLYMERIZATION 329
benign process, where starting materials and products are within the natural
material cycle; this is in the context of green polymer chemistry (13,14).
Polysaccharides
Polysaccharides are among the most important biopolymers as are proteins and
nucleic acids in nature. They are regarded as three important families of natu-
ral biomacromolecules. As to the enzymatic polymerization for polysaccharides,
hydrolases and transferases are reported to catalyze their synthetic reactions.
Hydrolases. It is generally accepted that an enzymatic reaction is vir-
tually reversible, and hence, the equilibrium can be controlled by selecting the
reaction conditions. Based on this view, hydrolases, enzymes catalyzing a bond-
cleavage reaction by hydrolysis, have been developed as catalyst for the reverse
reaction of hydrolysis, leading to polymer production by a bond-forming reaction
(9,12).
It is believed that using a glycosidase for the glycosylation process is one of
the most promising methodologies for selective construction of a glycosidic link-
age under appropriate conditions, since chemical approach requires complicated
procedures including a regioselective blocking and deblocking of a hydroxy group
in the sugar moiety to achieve regioselectivity, and furthermore, complete stere-
ocontrol of the glycoside bond-formation has not often been achieved by chemical
catalysts.
Enzymatic formation of a glycosidic bond is realized by combined use of a
glycosyl donor and a glycosyl acceptor. The former is to be activated by an enzyme
to give a glycosyl-enzyme intermediate which can be attacked by a hydroxy group
of the acceptor, forming a glycosidic bond between the donor and the acceptor. The
repeated glycosylations are expected to produce polysaccharide molecules.
Glycosyl uorides, sugar derivatives whose anomeric hydroxy group is re-
placed by a uorine atom, are known to be recognized by glycosidases. Cellulose
is one of the most important biomacromolecules, which is the most abundant or-
ganic substance on the earth (12). Thus, in 1991, the rst in vitro synthesis of
cellulose via nonbiosynthetic pathway has been achieved by an enzymatic poly-
merization of -cellobiosyl uoride as substrate for Tricoderma viride cellulase,
an extracellular hydrolytic enzyme of cellulose (Fig. 1) (1521). The polymeriza-
tion was performed in an aqueous organic solvent in order to make the desired
330 ENZYMATIC POLYMERIZATION Vol. 2
the size, growth and formation/degradation rate, and number of spherulites could
be controlled.
-Amylase catalyzed the polycondensation of -D-glucosyl uoride in an
aqueous solution to produce maltooligosaccharides (mainly pentamer) (30). -
D-Maltosyl uoride was also polymerized by -amylase catalyst in an aqueous
methanol, yielding a maltooligosaccharide with degree of polymerization (DP) up
to 7 (31). Enzymatic transglycosylation of -D-maltosyl uoride with a cyclodextrin
using pullulanase or isoamylase as a catalyst produced a branched cyclodextrin,
6-O--maltosylcyclodextrin (32,33).
Synthetic xylan was synthesized by a cellulase-catalyzed polymerization us-
ing -xylobiosyl uoride as a substrate (34). The enzymatic polymerization pro-
ceeded in a perfect regio- and stereoselective manner to produce powdery arti-
cial xylan, which is insoluble in any organic solvent. Xylan, one of the most
important components of hemicellulose in plant cell walls, normally contains 4-
O-methylglucuronic acid or L-arabinose as a minor unit in the side chain. On
the other hand, the articial xylan consists exclusively of a xylopyranose moiety
connected through a (14) glycosidic bond.
The rst synthesis of a cellulosexylan hybrid polymer, a novel polysaccha-
ride having a glucosexylose repeating unit, has been achieved by the xylanase-
catalyzed polymerization of -xylopyranosyl-glucopyranosyl uoride (Fig. 2) (35,
36). Identication of the enzyme fraction promoting the polymerization showed
that endoxylanase was highly efcient for production of the hybrid polymer.
Cellulase-catalyzed polycondensation of 4-thio--cellobiosyl uoride pro-
duced hemithiocellodextrins having 4-thiocellobiosyl repeating units linked by
(14) oxygen linkages (37). A water-soluble oligomer with DP up to 20 was
obtained in an aqueous acetonitrile.
Chitin is the most abundant organic macromolecules in the animal eld
found in invertebrates (12). The in vitro synthesis of this important biomacro-
molecule has been achieved for the rst time by enzymatic ring-opening polyad-
dition of a chitobiose oxazoline monomer (Fig. 3). Chitinase, a hydrolysis enzyme
of chitin, regio- and stereoselectively induced the polymerization of the monomer
in a basic buffer (3841). It is postulated that the monomer is preferable as a
substrate because it can be recognized by the active site of chitinase readily due
to the oxazoline structure resembling that of the transition state of the chitin hy-
drolysis with chitinase as revealed by a later work (12,42). Thus, the monomer
is regarded as a transition state analogue substrate for chitinase. From x-ray
diffraction and nmr analysis, the product was found to show crystal structure of
-chitin. A oxazoline monomer from N-acetyl glucosamine was also polymerized
at high substrate concentration to give chitooligosaccharides.
The visualization of high ordered structure formation during the enzymatic
synthesis of articial chitin has been investigated (43). Plate-like single crystals of
-chitin were rst formed and gradually shaped into ribbons by the rapid growth
along the a axis with the crystalline thickness being ca 10 nm. The -chitin rib-
bons then aggregated to form bundle-like or dendritic assemblies as the ribbon
concentration in solution increased. They grew up to spherulites by splaying and
branching. This articial chitin spherulite, in which a number of -chitin rib-
bons radiated from a common center, is completely different from the helicoidal
textures composed of -chitin microbrils known as a typical three-dimensional
organization of chitin (see CHITIN and CHITOSAN).
A cellulosechitin hybrid polymer, a nonnatural polysaccharide having a
glucose unit and an N-acetyl glucosamine unit alternatingly in the main chain,
was synthesized by chitinase-catalyzed polyaddition of a disaccharide oxazoline
monomer in an aqueous solution (44).
Sugar-chain elongation from di-N-acetylchitobiose as initial substrate to
hexamer and heptamer of chitooligosaccharide was efciently induced through
lysozyme catalysis in an acetate buffer containing 30% ammonium sulfate at 70 C.
The high concentration of ammonium sulfate resulted in a remarkable increase
of the hexamer and heptamer productions. In this reaction, a sugar-elongation
from the dimer to trimer was the rate-limiting step in the overall process of trans-
glycosylation (45).
Transferases. Phosphorylase catalyzes polymerization of -D-glucose-1-
phosphate in the presence of primer, leading to in vitro synthesis of amylose
(Fig. 4) (46). By utilizing phosphorylase catalysis, various amylose derivatives
such as linear-, star-, and comb-shaped amylose polymers were synthesized (47).
The chain length could be controlled by a simultaneous start for all chains us-
ing a primer with a minimum length of four glucosyl residues. This method was
Vol. 2 ENZYMATIC POLYMERIZATION 333
Poly(amino acid)s
Polyesters
polymerization of cholic acid, in which the hydroxy group at 3-position was regios-
electively acylated to give the oligoester with molecular weight less than 1103
(82). An optically active oligoester was obtained by the enantioselective polymer-
ization of racemic 10-hydroxyundecanoic acid catalyzed by lipase CC. The result-
ing polymer was enriched in the (S) enantiomer with 60% enantiomeric excess (ee)
and the (R)-enriched unreacted monomer with 33% ee was recovered (83). In the
polymerization of racemic lactic acid catalyzed by lipase CA at 50 C (84), nonamer
was detected in the product by MALDI-TOF mass measurement. A hplc analysis
showed that the D-enantiomer possessed higher enzymatic reactivity.
Oxyacid Esters. The polymerization of ethyl glycolate using PEG-modied
esterase from hog liver and lipase from Aspergillus niger (lipase A) gave
oligo(glycolic acid) with DP up to 5 (85). PPL catalyzed the polymerization of
methyl esters of 5-hydroxypentanoic and 6-hydroxyhexanoic acids (86). In the
polymerization of the latter in hexane at 69 C for more than 50 days, the polymer
with DP up to 100 was formed. Relationships between solvent type and polymer-
ization behaviors were systematically investigated; hydrophobic solvents such as
hydrocarbons and diisopropyl ether were suitable for the enzymatic production
of high molecular weight polymer. Polycondensation of various hydroxyesters,
ethyl esters of 3- and 4-hydroxybutyric acids, 5- and 6-hydroxyhexanoic acids,
5-hydroxydodecanoic acid, and 15-hydroxypentadecanoic acid, proceeded by Pseu-
domonas sp. lipase catalyst to give the corresponding polyesters with molecular
weight of several thousands (87).
A symmetrical hydroxy diester, dimethyl -hydroxyglutarate, was enantios-
electively polymerized by lipase catalyst to produce a chiral oligomer (dimer or
trimer) with 3037% ee (88). The enantioselective polymerization of -substituted-
-hydroxy esters took place in the presence of PPL catalyst, yielding optically
active oligomers (DP < 6) (89). The enantioselectivity increased as a function of
bulkiness of the monomer substituent. Optically active polyesters with molecular
weight more than 1103 were obtained by the copolymerization of the racemic
oxyacid esters with methyl 6-hydroxyhexanoate.
Lipase-Catalyzed Polymerization of Dicarboxylic Acids or Their
Derivatives. Enzymatic synthesis has been achieved via various combinations
of dicarboxylic acid derivatives and glycols. As to the diacid monomer, dicarboxylic
acids, activated and nonactivated esters, cyclic acid anhydrides, and polyanhy-
drides were enzymatically reacted with glycols under mild reaction conditions.
Dicarboxylic Acids. Immobilized Mucor miehei lipase (lipase MM) cat-
alyzed polycondensation of adipic acid and 1,4-butanediol by using a horizontal
two-chamber reactor in the presence of molecular sieves as dehydrating agent
(90). A low dispersity polyester with DP=20 was obtained by the two-stage poly-
merization.
The polymerization of dicarboxylic acids and glycols proceeded by using li-
pase CA catalyst in a solvent-free system, despite the initial heterogeneous mix-
ture of the substrates (9194). The polymerization behaviors strongly depended
on the chain length of both monomers (93). The polymerization under reduced
pressure increased the molecular weight of polyesters. The detailed studies in the
combination of adipic acid (A) and 1,4-butanediol (B) showed that the propaga-
tion took place by the reaction of the preliminary adduct (AB) with a hydroxy-
terminated species (92).
Vol. 2 ENZYMATIC POLYMERIZATION 337
room temperature produced PHB with molecular weight around 1103 (142). In
the polymerization at high temperature (80 or 100 C), PHB with higher molecu-
lar weight was obtained by lipase CC, PF, or PPL catalyst (143,144). A signicant
amount of the cyclic PHB fraction was formed and the content of the cycles in-
creased with increasing the monomer conversion. Enantioselective polymerization
of -BL was achieved by using thermophilic lipase to give (R)-enriched PHB with
2037% ee (145).
PHB depolymerase is an enzyme catalyzing hydrolysis of PHB and its cat-
alytic site is a serine residue, the same as lipase. The polymerization of -BL pro-
ceeded using two types of PHB depolymerase with or without substrate-binding
domains (SBD) as catalyst (146). The SBD-lacking PHB depolymerase showed
higher catalytic activity.
Chemoenzymatic synthesis of biodegradable poly(malic acid) was demon-
strated by lipase-catalyzed polymerization of benzyl -malolactone, followed by
the debenzylation (147). The molecular weight of poly(benzyl -malolactone) in-
creased by the copolymerization with a small amount of -PL (17 mol% for the
monomer) (148).
Five-membered unsubstituted lactone, -butyrolactone, is not polymer-
ized by conventional chemical catalysts. However, oligomer formation from -
butyrolactone was observed by using PPL or Pseudomonas sp. lipase as catalyst
(87,142).
Medium size lactones, -valerolactone (-VL, six-membered) and -
caprolactone (-CL, seven-membered), were subjected to lipase-catalyzed poly-
merizations. Lipases CC, PF, and PPL showed high catalytic activity for the poly-
merization of -VL (149,150). The molecular weight of enzymatically obtained
poly(-VL) was relatively low (less than 2103 ).
-CL was enzymatically polymerized by various lipases of different origin,
lipases CA, CC, PC, PF, and PPL (86,149157). Among them, lipase CA was the
most active toward the -CL polymerization; a very small amount of lipase CA (less
than 1 wt% for -CL) was enough to induce the polymerization (151). Under appro-
priate reaction conditions, the molecular weight reached more than 4104 (157).
In the lipase CA-catalyzed polymerization in organic solvents, cyclic oligomers
were mainly formed, whereas the main product in the bulk polymerization was of
linear structure (155).
The detailed kinetics of the -CL polymerization showed that termination
and chain transfer did not occur and the monomer consumption followed a rst-
order rate law under appropriate conditions, indicating that the system provided
controlled polymerizations where the molecular weight was a function of the
monomer to initiator stoichiometry (152,153,156).
Effect of reaction medium has been systematically investigated in the lipase
CA-catalyzed polymerization of -CL (157). Solvents having log P values from 1.1
to 0.49 showed low propagation rates; on the other hand, solvents with log P values
from 1.9 to 4.5 efciently induced the polymerization, leading to high molecular
weight polymer. The monomer-to-solvent ratio also affected the polymerization
behaviors.
Enzymatic hydrolytic degradation of poly(-CL) in toluene also took place
using lipase CA catalyst to give oligomers with molecular weight of less than 500
(158). After the removal of the solvent from the reaction mixture, the residual
Vol. 2 ENZYMATIC POLYMERIZATION 343
oligomer was polymerized in the presence of the same catalyst of lipase. From
these data is proposed a basic concept that the degradationpolymerization could
be controlled by presence or absence of the solvent, providing a new methodology
of plastics recycling.
Substituted medium size lactones were polymerized by lipase catalyst.
Ring-opening polymerization of -methyl-substituted six- and seven-membered
lactones (-methyl--valerolactone and -methyl--caprolactone, respectively)
proceeded using lipase CA catalyst in bulk (159). As to (R)- and (S)-3-methyl-4-oxa-
6-hexanolides (MOHELs), lipase PC induced the polymerization of both isomers.
The apparent initial rate of the S isomer was seven times larger than that of the R
isomer, suggesting that the enantioselective polymerization of MOHEL took place
through lipase catalysis (160).
Poly(1,4-dioxane-2-one) is a biocompatible polymer with good exibility and
tensile strength for medical applications. Metal-free poly(1,4-dioxane-2-one) with
M w up to 4.1104 was synthesized by lipase CA-catalyzed ring-opening polymer-
ization of 1,4-dioxan-2-one (161).
Lipase-catalyzed ring-opening polymerization of nine-membered lactone, 8-
octanolide (OL), has been reported (162). Lipases CA and PC showed the high
catalytic activity for the polymerization.
Four unsubstituted macrolides, 11-undecanolide (12-membered, UDL) (163,
164), 12-dodecanolide (13-membered, DDL) (164,165), 15-pentadecanolide (16-
membered, PDL) (163,164,166,167), and 16-hexadecanolide (17-membered) (168),
were subjected to the lipase-catalyzed polymerization. An nmr analysis showed
that the terminal structure of the polymer obtained in bulk was of carboxylic acid
at one end and of alcohol at the other terminal.
The bulk polymerization of PDL using lipase CA or MM as catalyst produced
the corresponding polyester with high molecular weight up to 3.4104 (167). The
polymerization behaviors (rate of the monomer consumption and molecular weight
of the polymer) depended on the water content in the reaction system. Enzymatic
ring-opening polymerization of macrolides (UDL, DDL, and PDL) proceeded even
in an aqueous medium (169).
The enzymatic polymerization of lactones is explained by considering the fol-
lowing reactions as the principal reaction course (Fig. 10) (160,163,170,171). The
key step is the reaction of the lactone with lipase involving the ring-opening of the
lactone to give the acyl-enzyme intermediate (enzyme-activated monomer, EM).
The initiation is a nucleophilic attack of water, which is probably contained in the
enzyme, onto the acyl carbon of the intermediate to produce -hydroxycarboxylic
acid (n = 1, the shortest propagating species). In the propagation stage, the in-
termediate is nucleophilically attacked by the terminal hydroxyl group of a prop-
agating polymer to produce a one-unit-more elongated polymer chain. This is a
monomer-activated mechanism in contrast to an active chain-end mechanism, the
widely known polymerization mechanism.
Macrolides have virtually no ring strain, and hence, show similar reactivi-
ties with acyclic fatty acid alkyl esters in the alkaline hydrolysis and lower an-
ionic ring-opening polymerizability than -CL. However, polymerization of the
macrolides using lipase PF catalyst proceeded much faster than that of -CL.
This specic polymerizability by lipase catalyst was quantitatively evaluated by
MichaelisMenten kinetics (160,168,170172). For unsubstituted lactones in the
344 ENZYMATIC POLYMERIZATION Vol. 2
range of ring-size from 7 to 17, linearity was observed in the HanesWoolf plot
for the formation of the acyl-lipase intermediate, indicating that the polymer-
ization followed MichaelisMenten kinetics. V max(lactone) /K m(lactone) and V max(lactone)
values increased as a function of the ring-size; on the other hand, K m(lactone) values
were not so different from each other. These data imply that the enzymatic poly-
merizability increased as the ring-size increased, and the large polymerizability
of macrolides through lipase catalysis is mainly due to the large reaction rate
(V max ), but not to the binding abilities, ie, the ring-opening reaction process of
the lipaselactone complex to the acyl-enzyme intermediate is the key step of the
polymerization.
Fluorinated lactones in the ring-size from 10 to 14 were enantioselectively
polymerized using lipase catalyst (173). The lipase CA-catalyzed polymerization
of 10-uorodecan-9-olide (10-membered) produced the optically active polymer
with positive rotation. Interestingly, the corresponding oxyacid gave an optically
inactive polyester.
Enzymatic synthesis of aliphatic ester copolymers was achieved by lipase-
catalyzed polymerization of two lactones. The copolymerization of -VL and -
CL catalyzed by lipase PF produced the corresponding copolymer having random
structure of both units (174). In the copolymerization of OL with -CL or DDL,
random copolyesters were also formed (162), suggesting the frequent occurrence
of transesterications between the polyesters. On the other hand, the copolymer
from -CL and PDL was not statistically random (166).
Polyesters with high optical purity were synthesized by the lipase CA-
catalyzed copolymerization of racemic -BL with -CL or DDL (175). (S)--BL was
preferentially reacted with DDL to give the (S)-enriched optically active copoly-
mer with ee of -BL unit = 69%. -CL was also enantioselectively copolymerized
by the lipase catalyst to give the (R)-enriched optically active polyester with ee up
to 76%.
Frequent occurrence of transesterication between polyesters chains was
expanded to synthesis of random ester copolymers by the lipase-catalyzed
Vol. 2 ENZYMATIC POLYMERIZATION 345
Polycarbonates
ve-membered cyclic phosphate, took place at 40100 C to give the polymer with
molecular weight of ca 1103 .
Polyaromatics
the expense of aromatic proton donors in living cells. In some cases, the peroxidase-
catalyzed oxidation of these donors, eg, phenols, yields water-insoluble polymeric
materials, which had not been characterized yet.
In 1987, enzymatic synthesis of a new class of polyphenols has been rst
reported. An oxidative polymerization of p-phenylphenol using horseradish per-
oxidase (HRP) as catalyst was carried out in a mixture of water and water-miscible
solvents such as 1,4-dioxane, acetone, DMF, and methyl formate to give powdery
polymeric materials (219). The reaction medium composition greatly affected the
molecular weight, and the highest molecular weight (2.6104 ) was achieved in
85% 1,4-dioxane.
In the case of phenol, the simplest and most important phenolic compound in
industrial elds, conventional polymerization catalysts afford an insoluble prod-
uct with noncontrolled structure since phenol is a multifunctional monomer for
oxidative polymerization. On the other hand, the peroxidase catalysis induced the
polymerization in an aqueous organic solvent to give a powdery polymer consist-
ing of phenylene and oxyphenylene units showing relatively high thermal stability
(Fig. 12) (220224). HRP and soybean peroxidase (SBP) were active as catalyst
for the polymerization in the aqueous 1,4-dioxane (220222). However, the result-
ing polymer showed low solubility; the polymer was partly soluble in DMF and
dimethyl sulfoxide, and insoluble in other common organic solvents. The solubility
was much improved by using a mixed solvent of buffer and methanol, producing
the DMF-soluble polymer with molecular weight of 21006000 in good yields.
Furthermore, the unit ratio (regioselectivity) could be controlled by changing the
solvent composition; the polymer in the range of the phenylene unit from 32 to
66% was obtained (223,224).
So far, various phenol derivatives have been polymerized through peroxidase
catalysis in the aqueous organic solvent (225227). For the case of a combination
of p-n-alkylphenols and HRP, the polymer yield increased as the chain length of
the alkyl group increased from 1 to 5 (228,229). Polymer formation was observed
in using all cresol isomers by HRP catalyst (230). The polymer was obtained in a
high yield from p-i-propylphenol, whereas ortho and metaisomers were not poly-
merized under the similar reaction conditions. Poly(p-n-alkylphenol)s prepared in
the aqueous 1,4-dioxane showed low solubility toward common organic solvents,
and the molecular weight was in the range of several thousands. On the other
hand, soluble oligomers with molecular weight less than 1000 were formed in
using an aqueous DMF as solvent (231).
Enzymatically synthesized polyphenols showed biodegradability (232), al-
though the degradation rate was not high. Antioxidant effects of the polymers ob-
tained from various phenols through the enzyme catalysis were evaluated (233).
Pronounced improvement for the autooxidation of tetralin was observed.
350 ENZYMATIC POLYMERIZATION Vol. 2
Vinyl Polymers
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364 ENZYMATIC POLYMERIZATION Vol. 2
SHIRO KOBAYASHI
HIROSHI UYAMA
Kyoto University