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Enzymatic degradation of poly (caprolactone), poly (vinyl acetate) and their

blends by lipases
ARTICLE in CHEMICAL ENGINEERING SCIENCE JULY 2003
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Chemical Engineering Science 58 (2003) 2911 2919

www.elsevier.com/locate/ces

Enzymatic degradation of poly (
-caprolactone), poly (vinyl acetate)

and their blends by lipases
G. Sivalingam, S. Chattopadhyay, G. Madras
Department of Chemical Engineering, Indian Institute of Science, Bangalore-560012, India
Received 22 August 2002; received in revised form 3 March 2003; accepted 13 March 2003

Abstract
Poly (
-caprolactone) (PCL) and poly (vinyl acetate) (PVAc) and their blends were degraded in toluene by two lipases (Novozym 435
and Candida Rugosa) at 60 C. The degradation of PCL and side-chain hydrolysis of PVAc yielded speci4c products of molecular weight
500 and 700, respectively. FTIR analysis of the polymer before and after enzyme treatment and the speci4c products show that there
is large reduction of ester linkages and generation of OH, COO() , COOH groups in the broken chains. The optimal temperature for
the side-chain hydrolysis of PVAc was 60 and 65 C and the optimal temperature for the biodegradation of PCL was 55 and 60 C for
Candida Rugosa and Novozym 435, respectively. Continuous distribution kinetics was proposed for determining the rate coe;cients of
the polymers and deactivation of the enzyme. Enzymatic degradation studies of PCLPVAc blends showed that there is a drastic reduction
in the degradation of PCL in the blends. This was modeled by the interaction between polymers.
? 2003 Elsevier Science Ltd. All rights reserved.
Keywords: Polymers; Kinetics; Enzyme; Population balances; Continuous distribution kinetics; Polymer blends

1. Introduction
The use of biodegradable polymers has been widely
accepted in biomedical applications. Due to the environmental issues with the commercial plastics, biodegradable
polymers have attracted much attention recently (Gan, Yu,
Zhong, Liang, & Jing, 1999). Most of the degradable polymers are ester bonded and have diBerent properties such as
mechanical strength, biodegradation rate, morphology, etc.
Poly (
-caprolactone) (PCL) is a well-known biodegradable polyester used in biomedical applications (Woodward,
Brewer, Moatamed, Schindler, & Pitt, 1985), especially in
controlled drug delivery. Good mechanical strength and
biodegradability are expected of biodegradable polymers for
practical applications. Random and block co-polymerization
have been proposed to increase the mechanical and physical properties of the biodegradable polymers (Pitt, Gratzl,
Kimmet, Surles, & Schindler, 1981). Physical blends of
aliphatic polyesters with these polymers were also shown
to change the morphologies and physical characteristics
of biodegradable polyesters (Tsuji & Ikada, 1992, 1996).
Corresponding author. Tel.: +91-080-309-2321;
fax: +91-080-360-0683.
E-mail address: giridhar@chemeng.iisc.ernet.in (G. Madras).

Most of the biodegradable polymers have hydrolysable

and/or oxidizable linkages along the main chain (Guillet,
1984). Polymers like poly (vinyl acetate) (PVAc) is known
to undergo hydrolysis by side-chain breakage due to their
hydrolysable groups in the side chain (Chattopadhyay &
Madras, 2003). One of the most widely used techniques
to modify the properties of the polymers is to blend them
(Gajria, Dave, Gross, & McCarthy, 1996). Blending of
PVAc and PCL may yield better properties, like higher
mechanical strength. This study investigates the biodegradability of this blend. Studies of the pyrolytic degradation
of polymer mixtures have generated varied results. Some
investigators have observed, during degradation, signi4cant
interaction between polymers, while others observed no
interaction (Karmore & Madras, 2001). The degradation of
homopolymers has been extensively studied. The degradation in solution of a mixture of poly(-methylstyrene) and
polystyrene has been studied (Madras & McCoy, 1999).
In this system, the former polymer degrades by chain end
scission while the latter degrades by random chain scission.
The degradation of a mixture of polystyrene and PVAc,
in which both the polymers degrade by random chain
scission, has also been investigated (Karmore & Madras,
2001). In the current investigation, the degradation of
PCL and hydrolysis of PVAc and their blends have been

0009-2509/03/$ - see front matter ? 2003 Elsevier Science Ltd. All rights reserved.
doi:10.1016/S0009-2509(03)00155-6

2912

G. Sivalingam et al. / Chemical Engineering Science 58 (2003) 2911 2919

examined. In this case, both the homopolymers undergo

speci4c chain scission. Continuous distribution kinetic models are proposed to determine the degradation coe;cients.
The model includes enzyme deactivation and also explains
the interaction between the polymers.
2. Experimental
5 kg=m3 solution of PCL (Aldrich, USA) and PVAc
(made by bulk polymerization in the laboratory) was dissolved in distilled toluene (SD Fines Chem.). Ten milliliters
of this solution were taken separately in screw cap cultured
tubes and kept at constant temperature baths with maximum
temperature variation of 1 C. 0:01 gm of Candida Rugosa
(CR) (Sigma Aldrich) and Novozym 435 lipase (gifted by
Novo Nordisk, Denmark) was added in the culture tube
and closed tightly. Reaction mixtures were stirred at regular
intervals to avoid axial gradient of reactants and products.
Two hundred microliters of samples were taken for analysis
in gel permeation chromatography (GPC) with tetrahydrofuran (THF) as eluent, to obtain the molecular weight
distribution. The details of the GPC system are provided
elsewhere (Sivalingam & Madras, 2003). The initial number average molecular weights and polydispersities for PCL
and PVAc were 121 000, 1.4 and 212 000, 1.2, respectively.
The solution blends of PCL and PVAc were also degraded
with both the enzymes to determine the interaction of these
polymers.

EnZ
O

OH
PCLn

PCLm

(a) Poly (-caprolactone)

OAc O

EnZ
O=C
O
EnZ

OAc
OAc

OAc

OAc

OAc

OAc

OAc

OAc

O=C
OAc
OAc

(b) Poly (Vinyl Acetate)

Fig. 1. Molecular structure of the polymers used: (a) PCL; (b) PVAc.

173h

104 h

3. Theoretical model
We assume the molecular weight of polymer, x, as a continuous variable. The biodegradation of PCL and PVAc are
assumed to contain four steps. (A) Adsorption of enzyme
on polymer substrate. (B) Formation of transition complex
between polymer and enzyme. (C) Speci4c chain scission
of the polymer. (D) Interaction of the polymer enzyme
adsorbed complex and polymers. Figs. 1a and b show the
chemical structure of PCL and PVAc, respectively, and
the point of attack of the enzyme. Because there are no hydrolysable linkages in the backbone of PVAC, the enzyme
only hydrolyzes the pendant acetate groups in the side chain
of the polymer. The detailed mechanism for the cleavage
was determined by analysis of the products by GC, GCMS
and NMR and are presented elsewhere (Chattopadhyay,
Sivalingam, & Madras, 2003). On the other hand, the lipase
cleaves the ester bonds in the main chain of PCL leading
to speci4c products, as reported elsewhere (Sivalingam,
Chattopadhyay, & Madras, 2003). In both the cases, the
molar concentration of the polymer is unaBected by degradation, as shown in Fig. 2.
Let PA and PB represent the polymer molecules of
species A and B, respectively and E for the enzyme. The
adsorption of enzymes over the polymer is reversible and is

EnZ

54h

23h
0h
900

1000

1100

1200

1300

1400

1500

1600

Time (s)
Fig. 2. Typical molecular weight distribution dynamics for the biodegradation of PCL in toluene by Candida Rugosa at 40 C.

given by
kaA

PA (x) + E
PAE (x);

kdA
kaB

PB (x) + E
PBE (x);

kdB

(A)
(B)

where PAE (x) and PBE (x) are the adsorbed polymer substrate
of individual species A and B, respectively. The adsorbed
polymer substrate undergoes reversible reaction to form the
transition complex by the following reactions:
ktfA

PAE (x)
PAE (x);

ktbA

(C)

G. Sivalingam et al. / Chemical Engineering Science 58 (2003) 2911 2919

ktfB

PBE (x)
PBE (x):

(D)

ktbB

PAE

and PBE are the activated (adjunct) complex formed

in the above step of polymer A and B, respectively. They
undergo irreversible speci4c chain scission as follows:

ksA

PAE (x) QsA (xsA ) + PAE (x xsA );

ksB

PBE (x) QsB (xsB )

PBE (x

xsB );

where QsA and QsB represent speci4c products of A and B

formed with molecular weights xsA and xsB , respectively.
Because the enzyme activity reduces with time, the above
rate coe;cients are multiplied by the activity of the enzyme,
given by a, which decreases with time as enzyme deactivates. The interaction of the two degrading polymers is due
to the multiple active site of the enzyme represented as reversible exchange reaction. The adsorbed enzymepolymer
B intermediate, PBE (x), combines with polymer A to form
an intermediate complex that undergoes transformation to
polymer B and, PAE (x), intermediate.
kd

kD

kD

kd

PBE (x) + PA (x )
P E (x + x )
PB (x) + PAE (x ):

(G)

Including the intermediate complex, P E (x + x ), facilitates the formulation of population balance equations of the
reversible interaction of adsorbed species with the polymer.
If P E (x + x ) is ignored in reaction (G), the forward and reverse rate coe;cients will be kd and kD , respectively. Representing the concentration of the individual species with
small case letters, the population balances are
@pA
= kaA pA e + kdA pAE kd pA pBE; (0)
@t


+ kD
pE (x )(1=x ) d x ;
(1)
x

@pB
= kaB pB e + kdB pBE kd pB pAE; (0)
@t


+ kD
pE (x )(1=x ) d x ;
x

@qsA
= ksA a
pAE (x )(x xs ) d x ;
@t

x

@qsB
pBE (x )(x xs ) d x ;
= ksB a
@t
x

@pAE
= ktfA pAE ktbA pAE ksA apAE ;
@t

@pBE
= ktfB pBE ktbB pBE ksB apBE ;
@t

@pAE
= kaA pA e kdA pAE ktfA pAE + ktbA pAE
@t

+ ksA a
pAE (x )(x (x xs )) d x
x

kd pB(0) pAE + kD

x

pE (x )(1=x ) d x ;

@pBE
= kaB pB e kdB pBE ktfB pBE + ktbB pBE
@t

+ ksB a
pBE (x )(x (x xs )) d x

kd pA(0) pBE + kD

(E)
(F)

2913

@p
= kd
@t

+ kd

x

pE (x )(1=x ) d x ;

(8)

pA (x )pBE (x x ) d x

0

pB (x )pAE (x x ) d x 2kD pE :



Applying the moment operation, p(j) (t)=

on Eqs. (1)(9) yields

(9)
xj p(x; t) d x,

dpA( j)
= kaA pA( j) e + kdA pAE; ( j) kd pA( j) pBE; (0)
dt
+

kD pE; ( j)
;
j+1

(10)

dpB( j)
= kaB pB( j) e + kdB pBE; ( j) kd pB( j) pAE; (0)
dt
+

kD pE; ( j)
;
j+1

(11)

( j)

dqsA
j
= ksA axsA
pAE ;(0) ;
dt

(12)

( j)

dqsB
j
= ksB axsB
pBE ;(0) ;
dt

(13)

dpAE ;( j)
= ktfA pAE; ( j) ktbA pAE ;( j) ksA apAE ;( j) ;
dt

(14)

dpBE ;( j)
= ktfB pBE; ( j) ktbB pBE ;( j) ksB apBE ;( j) ;
dt

(2)
(3)

dpAE; ( j)
= kaA pA( j) e kdA pAE; ( j) ktfA pAE; ( j) + kibA pAE ;( j)
dt

j


Ci (xsB )i pAE

(4)

+ ksA a

(5)

kd pB(0) pAE; ( j) +

(6)

(15)

i=0

;( ji)

kD pE; ( j)
;
j+1

(16)

dpBE; ( j)
= kaB pB( j) e kdB pBE; ( j) ktfB pBE; ( j) + ktbB pBE ;( j)
dt

+ ksB a

j


Ci (xsA )i pBE

;( ji)

i=0

(7)

kd pA(0) pBE; ( j) +

kD pE; ( j)
;
j+1

(17)

2914

G. Sivalingam et al. / Chemical Engineering Science 58 (2003) 2911 2919

equations yield


dpE; ( j)
j
= kd
Ci pAE; (i) pB( ji)
dt

(0)
dqsA
= KA apA(0) ;
dt

i=0

+ kd

i=0

Ci pBE; (i) pA( ji) 2kD pE; ( j) :

(18)

Expressions for the intermediates can be obtained by

equating the expressions of their zeroth moments (j = 0) to
zero. Eqs. (14) to (17) yield
pAE

;(0)

ktfA
pE; (0) ;
ksA + ktbA A

(19)

pBE

;(0)

ktfB
pE; (0) :
ksB + ktbB B

(20)

pAE; (0) =
pBE; (0) =

kD p

kd pB(0)

kaA pA(0) e

+ kdA

kD pE; (0) + kaB pB(0) e

kd pA(0) + kdB

(21)

(22)

Eq. (18) gives

p

E; (0)

kd
=
(pE; (0) pB(0) + pBE; (0) pA(0) ):
2kD A

where KA = ksA kaA =kdA ktfA =(ksA + ktbA )e. The mass concentration of the speci4c product can be obtained using the 4rst
moment. The mass balance is given by
(1)
dqsA
= KA axsA pA(0) :
dt

(27)

With the simpli4ed exponential model to account for the

deactivation, a(t) = a0 exp(kenz t), where a0 is the initial
activity of the enzyme and kd is the speci4c deactivation
rate, Eq. (27) can be deduced to
(1)
dqsA
= KA a0 exp(kenz t)xsA pA(0) :
dt

Equating Eqs. (16) and (17) to zero gives

E; (0)

(26)

(23)

Using these expressions in Eqs. (10) and (11) yields

dpA(0)
= 0;
dt

(24)

dpB(0)
= 0:
dt

(25)

Eqs. (24) and (25) indicates that the molar concentration

of the polymer remains constant. This is consistent with the
derivation of Madras, Smith, and McCoy (1996), who used
an overall mechanism.
4. Result and discussions
The hypothesized interaction of the polymer and
enzymepolymer species can be checked with limiting
cases. When kd = kD = 0, the two polymers undergo degradation independently. Eqs. (12) and (13) show the variation
of the zeroth moment of polymers in the mixture. The degradation rates for the binary mixture show that (Karmore &
Madras, 2001), depending on the particular polymer, the
presence of another polymer in the mixture can increase,
decrease, or have no eBect. Thus, the rate coe;cient for the
speci4c chain scission of PCL is a function of the concentration of PVAc in the mixture based on the experimental
conditions. The degradation rate of individual polymer can
be obtained by setting the other intermediates and species
to zero. For example, to get the degradation kinetics of
polymer A (PCL), setting pB(0) = pBE; (0) = 0 in the governing

(28)

(1)
Solving Eq. (28) with the initial condition, qsA
(t =0)=0,
yields
(1)
qsA
=

(1)
KA a0 xsA pA0
(1 exp(kenz t)):
kenz MnA0

(29)

Eq. (29) represents the evolution of the mass of the speci4c products of polymer A when B is not present. As t ,
the degradation reaches a saturation value, by Eq. (29) it
becomes
(1)
qssA = qsA
(t ) =

KA a0 xsA pA(1)
:
kenz MnA0

(30)

The rationalized mass fraction of speci4c product formed

can be obtained, by omitting the moment indicator, from
Eqs. (29) and (30).
qr (t) =

qsA (t)
= 1 exp(kenz t):
qssA (t )

(31)

Eq. (31) indicates that a semi-logarithmic plot of 1qr (t)

with time will be linear with a slope of kenz . Eq. (30)
can then employed to get KA , assuming a0 to be unity.
Fig. 2 shows representative time evolution of molecular
weight distributions for the degradation of PCL in toluene by
Candida Rugosa at 40 C. The peaks at the elution times
of 1000 and 1500 s represent the peaks of the polymer and
the speci4c product, respectively. As the reaction time increases, the speci4c product peak increases. The number
average molecular weight of the oligomer formed by the
degradation of PCL and PVAC were 500 (with polydispersity 1.4) and 700 (with polydispersity 1.32), respectively.
The structure of the degradation products was veri4ed by
FTIR (Perkin-Elmer) and the functional groups remained
unchanged for polymers and the degraded products con4rming that they are oligomers. The eluent of GPC for
the oligomeric fraction (around 1500 s in Fig. 2) was collected and analyzed in MS (micromass Q-TOF spectrometer) and the molecular weight was 300 700 and 470 920
for the degradation of PCL and PVAC, respectively. Control

G. Sivalingam et al. / Chemical Engineering Science 58 (2003) 2911 2919

0.08
0.07
0.06

0.04

(1)

q (t)/p0

(1)

0.05

0.03
0.02
0.01
0.00
0

25

50

75

100

125

150

175

200

225

250

275

time, hr

(a)
0.045
0.040
0.035

(1)

0.020

q (t)/p0

0.025

(1)

0.030

0.015
0.010
0.005
0.000
0

(b)

25

50

75

100

125

150

175

200

225

250

275

time, hr

Fig. 3. EBect of temperature on the degradation of PCL catalyzed by (a)

Novozym-435. Legend: (5), 45 C; (), 50 C; (4), 55 C; (), 60 C;
(), 65 C. (b) Candida Rugosa. Legend: (), 40 C; (), 50 C; (4),
55 C; (5), 60 C; (), 65 C; (J), 70 C. Solids lines: model 4ts.

experiments were done at identical conditions without enzyme and no degradation of the polymer was observed.
The eBect of temperature on degradation of PCL by

iments were conducted using these spent enzymes to degrade

the initial polymer in solution. The polymer did not degrade
indicating that the spent enzyme was completely inactive.
The model assumes that the activity of enzyme decreases
exponentially and that the enzyme forms a complex with the
polymer. Many enzymatic reactions occur after a enzyme
substrate complex formation (Bailey & Ollis, 1986). In the
present study, the formation of the enzymesubstrate complex is assumed. No radicals were found to form during the
reaction. This was con4rmed by adding a radical trapping
agent (2,2, diphenyl-1-picrlhydrazyl (DPPH)) to the reaction mixture and monitoring the concentration of DPPH by
a spectrophotometer (Shimadzu UV 2100) (Price, Norris,
& West, 1992). There was no change in the UV absorption,
indicating no radical formation during reaction. The overall
rate constant (KA ) of PCL and enzyme deactivation constant
(kenz ) of Novozym 435 and Candida Rugosa are listed in
Table 1. Figs. 4a and b show the degradation by hydrolysis of side chains of PVAc by Novozym 435 and Candida
Rugosa. The kinetic parameters are given in Table 1. Several experiments were conducted in triplicate and the standard deviation of the rate coe;cients was less than 3%. The
solid lines shown are model prediction by Eq. (29) obtained
by evaluating the enzyme deactivation coe;cient and KA .
The eBect of temperature on the degradation rate coe;cients
of polymers can be determined from the plot of KA =kenz vs.
temperature. Figs. 5 and 6 show the temperature pro4les
for the degradation of PCL and PVAc by Novozym 435
and Candida Rugosa. The optimal temperature of the PCL
degradation is 55 C with Candida Rugosa and 60 C with
Novozym 435. The optimal temperature for the side-chain
hydrolysis of PVAc by Novozym and Candida Rugosa is 60
and 65 C.
To support the hypothesis of reduction in enzyme activity,
enzymes after experiments were reused in a new experiment
with a fresh batch of polymer solution without any treatment
and the degradation rate was drastically reduced compared
to the rate with fresh enzyme in Fig. 7.
The concentration of the complex formed by the interaction of the polymers in blend can be determined by simultaneously solving Eqs. (21)(23).

pE; (0) = kd pA(0) pB(0) e

Novozym 435 and Candida Rugosa is shown in Figs. 3a and

b. The degradation of the polymer ceases and attains the saturation value after 20 days. This is because the enzyme becomes inactive. To prove that the saturation value is not due
to the polymer, further experimentation was carried out. After 20 days, the enzymes were 4ltered out of the solution and
a same amount of fresh enzyme was added to the solution.
The polymer continued to degrade in this case indicating that
the saturation was due to the inactivity of the enzyme. To
further prove that the spent enzyme was inactive, new exper-

2915

kaB kdA k1 + kaA kdB k2

kD (2kdA kdB k1 k2 kd kdB k2 pB(0) kd kdA k1 pA(0) )

(32)

where k1 =1+kd pB(0) =kdA and k2 =1+kd pA(0) =kdB . Substituting

the expressions for p(0) in Eq. (21) yields
pAE; (0) =

kaA pA(0) e
(1 + k3 pB(0) ):
k1 kdA

(33)

Substituting Eq. (33) into Eq. (19) gives

pAE

;(0)

ktfA
kaA pA(0) e
(1 + k3 pB(0) ):
ksA + ktbA k1 kdA

(34)

2916

G. Sivalingam et al. / Chemical Engineering Science 58 (2003) 2911 2919

Table 1
Rate coe;cients for the degradation of PCL and PVAc and their blends

Polymer

Speci4cation

Novozym 435

Candida Rugosa

qs(1) =p0(1)

kenz (h1 )

KA (h1 )

qs(1) =p0(1)

kenz (h1 )

KA (h1 )

PCL

45 C
50 C
55 C
60 C
65 C

0.0234
0.0600
0.0700
0.0776
0.0722

0.0049
0.0053
0.0073
0.0133
0.0072

0.0282
0.0764
0.1237
0.2497
0.1264

0.0259a
0.0320
0.0423
0.0342
0.0312

0.0063a
0.0096
0.0181
0.0107
0.0094

0.0395a
0.0743
0.1853
0.0886
0.0710

PVAc

50 C
55 C
60 C
65 C
70 C

0.0029
0.0032
0.0039
0.0037

0.0069
0.0074
0.0112
0.0099

0.0060
0.0071
0.0133
0.0111

0.0004
0.0009
0.0026
0.0029
0.0012

0.0058
0.0087
0.0142
0.0182
0.0102

0.0007
0.0024
0.0111
0.0162
0.0029

BLENDS

10%
30%
50%
70%
90%

0.0058
0.0054
0.0047
0.0044
0.0043

0.0144
0.0136
0.0121
0.0103
0.0099

0.0201
0.0177
0.0137
0.0109
0.0102

0.0042
0.0040

0.0033
0.0031

0.0125
0.0110

0.0114
0.0106

0.0126
0.0107

0.0091
0.0080

a Corresponds

PVAc
PVAc
PVAc
PVAc
PVAc

to 40 C for the degradation of PCL by Candida Rugosa.

0.0040

20.0

0.0035

17.5
0.0030

15.0

KA/kenz

q(1)(t)/p0

(1)

0.0025
0.0020

12.5

0.0015

10.0
0.0010

7.5

0.0005
0.0000

5.0
0

25

50

75

(a)

100

125

150

175

200

225

250

275

300

time, h

40

45

50

55

60

65

70

Temperature, K
0.0030

Fig. 5. Optimal temperature for enzymatic degradation of PCL. Legend:

(), Novozym-435; (), Candida Rugosa.

0.0025

Using Eq. (34), the molar rate of formation of speci4c

product is

0.0015

(0)
ktfA
dqsA
p(0)
ksA kaA e
a A (1 + k3 pB(0) );
=
dt
kdA ksA + ktbA
k1

(1)

q (t)/p0

(1)

0.0020

0.0010

where


kd
kaB kdA k1 + kaA kdB k2
:
k3 =
kdA kdB (k1 + k2 )
kaA e

0.0005

0.0000
0

(b)

(35)

25

50

75

100 125 150 175 200 225 250 275 300 325

time, hr

Fig. 4. EBect of temperature on the degradation of PVAc catalyzed by (a)

Novozym 435. Legend: (), 50 C; (), 55 C; (4), 60 C; (5), 65 C.
(b) Candida Rugosa. Legend: (), 50 C; (), 55 C; (4), 60 C; (5),
65 C; (), 70 C. Solid lines: model 4ts.

In the present work, the eBect of PVAc on the degradation

of PCL is investigated. PVAc undergoes side-chain hydrolysis and it was experimentally observed that the rate of speci4c product formation from PVAc is one order less than
PCL, as shown in Figs. 36. The degraded products from the
blends have been analyzed for functional groups in FTIR.

G. Sivalingam et al. / Chemical Engineering Science 58 (2003) 2911 2919

2917

0.08

1.50

0.07
0.06

1.25

0.05
0.04

1.00
(1)

0.02

(1)

0.005

q (t)/p0

KB/kenz

0.03

0.75

0.004

0.50

0.003
0.002

0.25

0.001
0.000

0.00
48

50

52

54

56

58

60

62

64

66

68

70

72

25

50

75

100

125

150

175

200

225

250

275

300

time, hr

Temperature, K

Fig. 6. Optimal temperature for enzymatic degradation of PVAc. See Fig.

3 for legend.

Fig. 8. EBect of wt% PVAc on the degradation of blends by Novozym.

Legends: (I), 100% PVAc; (), 90% PVAc; (), 70% PVAc; (4),
50% PVAc; (5), 30% PVAc; (), 90% PVAc; (J), 0% PVAc. Solid
lines: model 4ts.

0.030

Eq. (37) can be solved with initial condition to get the dynamics of the speci4c product formed in the polymer blend,
KA a0 xsA
(1)
(1)
qsA
=
kint pA0
(1 exp(kenz t));
(38)
MnA0 kenz

0.025

(1)

qt /p0

(1)

0.020

0.015

0.010

0.005

0.000
0

50

100

150

200

250

Time (hrs)

Fig. 7. Speci4c products generated at 60 C by using used (PCL (),

PVAc ()) and new (PCL (4), PVAc (5)) Candida Rugosa.

It showed that the majority of the products are of PCL origin. Therefore, it is reasonable to neglect the degradation
rate of PVAc compared to PCL in the polymer blend, i.e.,

dpB(0) =dt = ksB pAE ;(0) = 0. Solving with the initial conditions,
(0)
. This simplifying assumptions lead to
we have pB(0) = pB0
the following expression for the speci4c products:
(0)
(0)
) (0)
(1 + k3 pB0
dqsA
pA :
= KA a
dt
k1

(36)

The mass concentration of the speci4c products can be

written as
(0)
(1)
(1 + k3 pB0
) (0)
dqsA
= KA axsA
pA :
dt
k1

(37)

(1)
where kint = (1 + k3 pB0
=MnB0 )=k1 . Eqs. (29) and (38) represent the evolution of the speci4c products of A in the
absence and presence of polymer B, respectively. The ratio of Eqs. (38) and (29) is the interaction rate coe;cient,
kint . This indicates that when kint is unity, there is no interaction between the polymers or polymer B is not present.
The interaction coe;cient kint can either be greater or less
than unity based on the positive or negative interaction between the polymers, respectively. It is also seen from the
above equation that the interaction term is dependent on the
amount of enzyme. The saturation value of speci4c products
formed can be obtained by setting time to in4nity.
KA a0 xsA
(1)
qssA
(t ) =
kint pA(0) = KAB :
(39)
MnA0 kenz

The rationalized fraction of speci4c products formed can

be obtained from Eqs. (38) and (39) as
qrA =

(1)
qsA

(1)
qssA

= 1 exp(kenz t):

(40)

A semi-logarithmic plot of (1 qrA ) with time t yields

the enzyme deactivation coe;cient (kenz ). The combined
degradation coe;cient was obtained using Eq. (39). The
interaction coe;cient kint was obtained from the pure PCL
degradation rate from Eqs. (30) and (31). Fig. 8 shows the
eBect of PVAc on the biodegradation of PCL catalyzed by
Novozym 435. Even the addition of 10 wt% PVAc showed
drastic reduction in degradability of PCL. The degradation of the blends was between the pure polymer species
degradation rates, with the addition of PVAc reducing the

2918

G. Sivalingam et al. / Chemical Engineering Science 58 (2003) 2911 2919

0.12
0.030

0.11
0.025

0.10
0.020

(1)

kint

q (t)/p0

(1)

0.09
0.015

0.08
0.004

0.07
0.003
0.002

0.06

0.001

0.05

0.000
0

25

50

75

100

125

150

175

200

225

250

275

20

40

60

80

100

Wt% PVAC

time, hr

Fig. 9. EBect of wt% PVAc on the degradation of blends by Candida

Rugosa. See Fig. 6 for legend. Solid lines: model 4ts.

Fig. 11. Plot between the interaction parameter and wt% of PVAc in the
blend. See Fig. 8 for legend.

Acknowledgements

20.0
17.5

The authors thank the department of Science and Technology for 4nancial support.

15.0
12.5

KAkint/kenz

10.0

5. Conclusions

7.5
1.50
1.25
1.00
0.75
0.50
0.25
0.00
0

20

40

60

80

100

wt % PVAc

Fig. 10. EBect of wt% PVAc on the rate coe;cients for the degradation
of PCL. Legend: (), Candida Rugosa; (), Novozym 435.

degradation of PCL signi4cantly. This is similar to the

4lm degradation behavior of poly lactic acid/PVAc blends
(Gajria et al., 1996), where the degradation of PLA changes
drastically even with 5 wt% addition of PVAc. This has
been attributed to change in the surface tension of the 4lm.
The solution degradation behavior may be due to change
in the conformation of PCL molecule in the presence of
PVAc. A similar behavior is observed when the blends
were degraded by Candida Rugosa as shown in Fig. 9. Fig.
10 shows that the interaction coe;cient (kint ) varies linearly with the percentage PVAc (10 100%) in the blend.
Because the variation of the rate coe;cients as shown in
Figs. 10 and 11 are linear with the amount of homopolymer
in the blend, the model can predict the rate coe;cients for
any intermediate composition of the polymer in the blend.

The degradation of two polymers, PVAc and PCL, and

their blends was studied with two lipases: Novozym 435 and
Candida Rugosa. The optimum temperature for the degradation of the pure polymers was determined. The investigation
of the degradation of the blend showed a rapid reduction
in the degradation of PCL with the addition of PVAc. A
model based on continuous distribution kinetics accounting
the enzyme deactivation and the interaction of polymers in
the solution was proposed. This model was able to predict
the experimental data satisfactorily.

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