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Summary
Wider use of chrome-tanned leather waste hydrolysate as a secondary industrial raw material is impeded by the
unclear economic effect of most proposed practical applications. More attention should deservedly go to
hydrolysate utilised as a biodegradable packing material (packing for agricultural chemicals including herbicides,
insecticides, pesticides, fertilizers etc.) The appropriate cross-link density enables us to control the water
solubility of hydrolysate, its biodegradation and the rate at which active substances are released from such
packing. The properties may significantly influence the economic effect of such an application. Increasing the
cross-link density of hydrolysate by reacting it with dialdehydes easily leads to the formation of thermoirreversible gels which are difficult to process. The main attention, therefore, is aimed at cross-linking hydrolysate
with epichlorhydrin.
In an aqueous environment, epichlorhydrin reacts with the primary amino groups of hydrolysate as a
monofunctional agent through its chlorine atom. At temperatures around 60C an equilibrium is attained in about
60 min. characterised by approx. 80% of the primary amino groups present having reacted. Reaction of the
oxirane ring of epichlorhydrin proceeds at considerably higher temperatures (~200C). Cross-linking of
hydrolysate with epichlorhydrin is thus a two-stage reaction, which may be regarded as an advantage for some
applications.
Introduction
Glues
The mean molecular mass of hydrolysates obtained
through enzymatic procedures usually ranges within limits
of 15-50kDa.5 These are capable, in a similar fashion to
gelatine or glues, of producing thermo-reversible gels
although, of course, at considerably higher concentrations
of dry matter. The rigidity of such gels (similarly to glues)
depends on their mean molecular mass (weighted mean
Mw) and dry matter concentration. At dry matter
concentrations of 20-35 % (w/w), gels of enzymatic
hydrolysates usually exhibit rigidities of 150-350g -1
(Bloom).6 Their quality, assessed in a standard manner, is
thus not too high and makes it impossible to consider their
application as adhesives for functional bonds with the
exception, maybe, for sticking labels (e.g., on glass bottles
and such) that should be removable with water. The
economic advantage of such applications, when compared
with lower quality glues or even starch adhesives, is hardly
appreciable.
In aqueous solutions, collagen hydrolysates behave like
substances with positive sorption, but do not display
stronger surface activity if not further processed. This is the
basis for contemplating their use in the form of additives
for retarding concrete setting in building. Nevertheless, the
necessity to concentrate hydrolysate solutions (for storage)
is a factor limiting the economy of these applications even
in such considerations.
The environmental necessity to process leather waste
and the benefits of processing it through enzymatic
hydrolysis are not, then, sufficiently supported by the
above mentioned applications as having any economic
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Surfactants
One of the more realistic possibilities consists in using
leather waste hydrolysates for manufacturing surfactants of
Lamepon type - through acylation of primary amino
groups of hydrolysates with acyl chlorides of fatty acids
(anionic surfactant types), or through their quaternation,
which is best with benzyl chloride (various types of
amphoteric surfactants).7 The relatively high mean
molecular mass of enzymatic hydrolysates results in
reduced solubility of surfactant derivatives made from them
in water, which leads to a lower production yield.
Acceptable yields can be attained if the mean molecular
mass of enzymatic hydrolysates is reduced to below
approx. 1.0kDa. That is more readily achieved through acid
hydrolysis (e.g. in HCl) than through alkaline hydrolysis or
through prolonged enzymatic hydrolysis.8 Subsequent
acylation or quaternation has to be performed in an alkaline
medium (pH>10.5 ),which somewhat complicates this
industrial application.
Experimental procedures
Starting materials:
Collagen hydrolysate (H) in powder form was prepared
by enzymatic hydrolysis of chrome-tanned leather waste by
a procedure according to reference 16 and drying in
pulverising drier. Its characteristics are shown in Table I.
TABLE I
Characteristics of the collagen hydrolysate used in the work
Dry substance %
92.99
Amide nitrogen in dry substance %
14.85
Ash in dry substance %
4.94
Cr content in dry substance ppm
28.15
Ca content in dry substance ppm
2746.62
Mg content in dry substance ppm
4798.00
0.216
Primary amino groups in dry substance mmol-NH2.g-1
17.75
Average molecular weight (numerical mean MN), kDa
Adhesives
On closer study of the properties of hydrolysate, it was
found that its addition to aminoplast type adhesives, at
approx. 5% (w/w) level, may considerably limit emissions
of formaldehyde gas from their cured adhesive films. The
effect is more pronounced if addition of hydrolysate is
accompanied with adapted, optimised conditions for curing
adhesive bonds.9-11 Results evaluating formaldehyde
emissions from cured films by the official bottle
method 12-13 confirmed that added hydrolysate may reduce
formaldehyde emissions from free adhesive films by as
much as 70%.
Working procedure
Packaging materials
A topic much discussed lately, concerns problems of
biodegradable polymers based on renewable raw material
sources, due to their employment in packing technology.
Besides renewability of raw material sources, the property
they are appreciated for is degradation rate, on termination
of package life. That, (degradation rate) when compared
with hitherto most widespread synthetic polymers based on
non-renewable crude oil, is several times greater and poses
virtually no environmental hazards. Among biodegradable
materials, proteins of both animal and vegetable origin
occupy a prominent position. It was proved that treating
hydrolysates of chrome-tanned leather waste with
glutaraldehyde allowed the production of biodegradable
materials14 applicable to packing of chemicals in farming
technology (herbicides, insecticides, fertilisers, etc.). In
addition, the degree of hydrolysate cross-linking with
glutaraldehyde allows efficient control of the rate at which
active substances are released from such packing into
surroundings, which is a very interesting effect from the
practical point of view.
Similar results may be probably also attained by reacting
hydrolysates with other cross-linking agents. One of them,
easily and economically available, is epichlorhydrin, which
was more applied in the past to grafting cellulose materials
(e.g., for immobilising various enzymes, etc). It is known
that under favourable conditions epichlorhydrin can
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Temperature (C)
Relative absorbance
Reaction time, H
Figure 2. Time dependence of IR absorption peaks in region 648-686cm-1
and 713-731cm-1 characteristic of -Cl group in liquid reaction mixture
when modifying the hydrosylate with epichlorhydrin in alkaline
environment.
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TABLE II
Characteristics of chrome-tanned leather waste hydrolysate modified with epichlorhydrin
XEpich
Epichlorhydrin
Starting
Reacted
mmol
Reacted
mmol
Mmol
Starting
mmol
Reacted
mmol
Series I.
0.053
0.2293
0.3097
57.40
0.5841
0.3033
51.93
1.08
0.98
0.094
0.1428
0.3952
73.32
1.0710
0.3394
31.69
1.99
0.86
0.074
0.131
0.171
0.203
Series II.
0.1916
0.1034
0.0746
0.0846
0.3474
0.4269
0.4644
0.4544
64.45
79.20
86.16
84.30
0.8276
1.5578
2.1420
2.6289
0.3236
0.3643
0.3863
0.4015
39.10
23.38
18.03
15.32
1.53
2.89
3.97
4.88
0.93
0.85
0.83
0.88
0.053
0.3564
0.1820
33.77
0.5841
0.3042
52.08
1.08
1.67
0.234
0.2889
0.2502
53.50
3.1644
0.4155
13.13
5.87
1.66
0.094
0.171
0.286
0.335
0.376
0.3545
0.2608
0.1379
0.1051
0.1041
0.1845
0.2782
0.4011
0.4339
0.4339
34.23
51.61
74.41
80.50
80.50
1.0710
2.1420
4.1380
5.2091
6.2310
0.3399
0.3864
0.4234
0.4419
0.4569
31.74
18.04
10.23
8.48
7.33
1.99
3.97
7.68
29.66
11.56
1.84
1.39
1.06
1.02
1.05
Agents applicable to modifying hydrolysate of chrometanned leather waste are substances of bifunctional
character, capable of entering into cross-linking reactions
with its functional groups. Choice is limited by a
requirement to perform the cross-linking reaction in an
aqueous or, at most, an aqueous-alcoholic environment
(solubility of hydrolysate). In the not very wide
concentration range of both reactants, cross-linking
reactions usually lead to formation of initially thermoreversible, subsequently thermo-irreversible gels swelling
in water.
The ability of swelling in water gradually deteriorates
with increasing cross-link density, and the gel acquires the
character of thermosetting (reactoplastic), poorly soluble,
non-fusible material whose processing by standard
procedures is somewhat more complicated. At the same
time, its biodegradability also deteriorates.
An alternative solution is cross-linking of hydrolysate
with bifunctional cross-linking agents possessing markedly
different reactivities of their functional groups as, for
example, epichlorhydrin. In an an aqueous-alkaline
environment such a reaction does not lead to gel formation
(phenomenon accompanying cross-linking of collagen
hydrolysates) despite the fact that a decrease in the primary
amino groups of the hydrolysate demonstrates clearly
enough the reaction of both substances. A state of
equilibrium is established in the reaction mixture,
characterised by 70-85% of initially present primary amino
groups of hydrolysate having reacted (see Figure 1).
The detected decrease in -Cl groups of epichlorhydrin in
the reaction mixture corresponds to a decrease in primary
amino groups, while the found decrease in oxirane rings of
epichlorhydrin merely ranges within limits of experimental
error. In an aqueous-alkaline environment, epichlorhydrin
then binds to hydrolysate at one point and actual
hydrolysate cross-linking does not occur in this stage of the
reaction. The mutual ratio of reacted EPICH and -NH2
Discussion
XEPICH
TABLE III
Characteristics of DSC exothermal peaks of dry films of reaction mixtures from TABLE 1
Ratio
EPICH:NH2
in film
Experiments of series I.
1.323
0.053
1.689
0.074
0.094
2.377
0.131
3.523
0.171
5.178
0.203
4.746
Experiments of series II
0.053
0.588
0.094
0.659
0.171
0.916
0.234
0.924
0.286
1.416
0.355
1.661
0.376
1.742
Tinit. oC
Tmax oC
Tfinal oC
Enthalpy
Q (J/g)
mmol/g of
cross-links
in film
203.0
195.4
190.7
190.5
190.8
193.8
215.0
209.2
201.5
202.9
203.1
204.6
233.8
233.0
232.3
232.9
232.0
230.0
0.31
1.06
0.82
1.11
1.84
1.92
0.0033
0.010
0.008
0.011
0.018
0.019
203.1
201.5
185.0
181.5
187.2
183.8
181.5
212.0
211.2
202.4
200.4
205.6
201.5
201.50
237.2
237.1
236.0
232.5
227.8
230.0
230.8
19.20
16.78
14.38
13.95
8.40
5.60
4.80
0.188
0.164
0.141
0.136
0.082
0.055
0.047
Note:
*)
Mass fraction of epichlorhydrin (EPICH) in liquid reaction mixture with hydrolysate
**) Calculated from mean value of enthalpy of condensation reaction of epoxy groups with
amino groups 102.15 kJ/mol see / 20,21 /
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Acknowledgement
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