Waste Management 23 (2003) 835–843

www.elsevier.com/locate/wasman

Towards zero discharge of chromium-containing leather waste

through improved alkali hydrolysis
Changdao Mua,*, Wei Lina,b, Mingrang Zhanga, Qingshi Zhub
a
The Key Laboratory of Leather Chemistry and Engineering of Ministry of Education, Sichuan University, Chengdu 610065, Sichuan, China
b
The Open Laboratory of Bond-Selective Chemistry, Department of Chemical Physics, University of Science and Technology of China, Hefei,
230026 Anhui, China

Accepted 18 February 2003

Abstract
The treatment of chromium-containing leather waste (CCLW), the major solid waste generated at the post-tanning operations of
leather processing, has the potential to generate value-added leather chemicals. Various alkali and enzymatic hydrolysis were
compared, and calcium oxide was found to be important for effective (but still incomplete) hydrolysis. Three possible reasons are
given for the incomplete hydrolysis under alkaline conditions. Data for 19 amino acids are presented for four different treatment
products. On the basis of the results, a novel three-step CCLW treatment process is proposed. The gelatin extracted in the first step
is chemically modified to produce leather finishing agents. The collagen hydrolysates isolated in the second step are used as pro-
teinic retanning agents by chemical modification. The remaining chrome cake is further hydrolyzed with acids in the third step, and
the obtained chromium-containing protein hydrolysates could be used for the preparation of chromium-containing retanning
agents for leather industry. The proposed three-step process provides a feasible zero discharge process for the treatment of CCLW.
# 2003 Elsevier Ltd. All rights reserved.

1. Introduction In recent years, China has been the largest leather

Leather industry provides the necessities, such as lea-
ther shoes and garments, while using the by-products of
the meat industry. However, the leather-making pro-
cess, in turn, generates by-products and wastes. It is
known that only 20% of wet salted hides/skins are con-
verted into commercial leather, while 25% becomes
chromium-containing leather waste (CCLW), and the
remainder becomes non-tanned waste or is lost in
wastewater as fat, soluble protein and solid suspended
pollutants (Alexander et al., 1991). Environmental
pollution is a difficult problem for world leather indus-
try (Kumaraguru et al., 1998; Cabeza et al., 1998a). In
past decades, a lot of effort has been made to study the
solid collagenous wastes, including isolation of protein
products from CCLW. Unfortunately, most of these
processes reported bring about new residues during
treatment.
* Corresponding author. Tel.: +86-28-8540-2197; fax: +86-28-
8546-0819.
E-mail address: muchangdao@263.net (C. Mu).
0956-053X/03/$ - see front matter # 2003 Elsevier Ltd. All rights reserved.
doi:10.1016/S0956-053X(03)00040-0
manufacturing country, typically from pigskin proces-
sing. Over 700,000 metric tons of CCLW are generated
each year from the Chinese leather industry, and several
times this amount is produced worldwide. In many pla-
ces, large quantities of solid leather wastes are disposed
by landfill (Brown et al., 1996). Increased environmental
restrictions and escalating landfill costs have encour-
aged the leather industry to develop cleaner technology
by minimizing wastes generated and maximizing those
reused.
The CCLW, also called chrome leather wastes, leather
scraps or chrome shavings, are produced in post-tan-
ning operations, such as trimming, splitting, shaving
and buffering processes. The CCLW mainly consists of
collagen and Cr(III) complexes, which could be treated
to give the potential resources of collagen protein and
chromium (Heidemann, 1991). In past decades, leather
researchers have made a lot of effort to study the re-use
of leather waste. Before 1970 reports dominantly
focused on uses not requiring extensive pretreatment of
the tanned wastes, including the manufacture of insula-
tors, building materials, fibrous sheets and shoe soles. In
836 C. Mu et al. / Waste Management 23 (2003) 835–843
addition, the method of making paper was introduced
to produce both leather and paper substitutes. Between
1970 and 1993, a lot of publications and patents con-
centrated on hydrolyzing CCLW to recycle amino acids
and peptides for use in feeds and fertilizers (Alves Dos
Reis and Beleza, 1991a,b; Ohtsuka, 1973; Taylor et al.,
1992b, 1993a). Various treatment methods have been
developed during this period. Basic hydrolysis, such as
using Ca(OH)2 with steam (Guardini, 1983; Holloway,
1978) or NaOH (Galatik et al., 1988) at elevated tem-
perature and/or pressure (Maire and Lipsett, 1980), acid
hydrolysis (Wojciech, 1998), and enzymatic hydrolysis
(Sivaparvathi et al., 1986a,b) were used for chrome
recovery and the isolation of protein fractions. Peroxide
treatments (Cot et al., 1991; Cot and Aramon, 1986) can
get collagen fiber and Cr(VI) by oxidization of leather
scraps. Wet air oxidation and incineration of CCLW
(Imai and Okamura, 1991) were used only to recycle
chromium(VI). Unfortunately, strong toxic Cr(VI) by-
products were generated in these reactions, thus requir-
ing an additional reductive step. The removal of chro-
mium is, however, never complete and needs many
repetitions, which is very expensive. Moreover, the more
often the procedure is repeated, the more the decom-
position of the collagen proceeds and collagen goes into
solution, resulting in a mixture of Cr(VI) with protein.
Brown et al. did systematical laboratory (Cabeza et
al., 1999a; Taylor et al., 1993b, 1997, 1998a) and pilot
scale (Cabeza et al., 1998d, 1999b; Taylor et al., 1998b)
studies on the treatment of CCLW in the past 10 years.
The initial one-step process developed by them involved
the use of alkaline proteolytic enzymes to isolate a
chrome-free, hydrolysate product that can be used as
feed or fertilizer (Taylor et al., 1990, 1992b). A newer
two-step process was to obtain a gelable protein, with
potential uses in adhesives, cosmetics, films, encapsula-
tion or emulsifying, etc. in the first step, and a hydro-
lysate in the second step. In this process the CCLW
were digested with an initial alkali step and with an
alkaline protease second step (Taylor et al., 1991, 1992a,
1993a, 1994), or using two consecutive enzymes (Cabeza
et al., 1997, 1998b, 1999c) in the two-step process.
However, a chrome cake, consisting of residue protein
crosslinked with chromium, remained as a by-product
in both treatment processes (Cabeza et al., 1998c).
Therefore, a complicated multi-step chemical operation,
including sulfuric acid dissolving, sodium hydroxide
precipitation, filtering and washing, were used to purify
the chrome cake for the chrome recovery (Cabeza et al.,
1998d, 1999b). This process produces wastewater with
salts and protein residues, requiring further treatment.
The collagen hydrolysate of CCLW once separated
from the chromium might have potential use as a lea-
ther tanning or finishing agent. Manzo and Fedele
(1994, 1996) not only demonstrated that the con-
densates, produced by the hydrolysis of CCLW and
reaction with formaldehyde after chromium hydroxide
separation, showed very good tanning capability. They
also studied the possibility of utilizing the hydrolysate
or its copolymers with methyl methacrylate or acrylo-
nitrile in leather finishing (Manzo et al., 1989). Unfor-
tunately, they only utilized the collagen hydrolysate of
CCLW, the ‘‘chrome cake’’ was not investigated.
Research over several years in our laboratory has
been designed to fully utilize CCLW and convert them
into value-added products, avoiding the production of
any other waste. In the present study, we focus on
establishing an appropriate hydrolysis method to yield
the desired recyclable products. We also consider the
feasibility of completely utilizing CCLW with zero dis-
charge.
2. Experimental
2.1. Analysis of chrome-containing leather waste
CCLW obtained from a commercial pigskin tannery
were kept at room temperature and analyzed for pH,
moisture, ash, Total Kjeldahl Nitrogen (TKN), chro-
mium and fat by normal methods. Moisture was deter-
mined by heating the sample at 110
C for 12 h. Ash in
the dried products was determined by heating the sam-
ple at 600
C for 4 hours. TKN was determined by the
semi-micro Kjeldahl method. Chromium was deter-
mined using a Perkin-Elmer model AA7003 atomic
absorption spectrophotometer. Fat was extracted with
chloroform.
2.2. Studies on hydrolysis methods
2.2.1. Alkali hydrolysis
One hundred grams of CCLW were shaken in 1 l of
water, and added 10 g CaO, or 10 g MgO, or 7 g NaOH
at 98
C for 3, 6 and 24 h, respectively. Then the sam-
ples were filtered warm through Büchner porcelain fun-
nels with Whatman No. 1 filter paper under vacuum
condition. The filtered protein solutions were stored at
4
C, and the protein yield was calculated based on the
dry weight of the waste. The remained chrome sludge
was kept at room temperature for further analysis and
treatment.
2.2.2. Enzymatic hydrolysis
One hundred grams of CCLW were shaken in 1 L of
water and 3 g MgO at room temperature for 4 h. This
pretreatment step is necessary to obtain the optimal pH
for the enzymatic digestion. Then 2 g alkaline protease,
such as 2709 enzyme (Wenjiang enzyme Inc., China), or
1398 enzyme (Wenjiang enzyme Inc., China), or Trypsin
(Wenjiang enzyme Inc., China), or Alcalase 2.5 L
(Novozymes Inc., China), was added at their individual
 C. Mu et al. / Waste Management 23 (2003) 835–843 837

optimal temperature for 3, 6 and 24 h, respectively.
Then the solution was filtered warm through Whatman
No. 1 filter paper in porcelain funnels under vacuum
condition. The filtered protein solutions and remained
chrome sludge were analyzed and treated as before.
2.3. Multi-step alkali hydrolysis
for 3–5 h. The resultant chromium-containing protein
hydrolysates solution was slowly adjusted to the appro-
priate pH value with sodium bicarbonate for prepara-
tion of retanning agents.
2.6. Analysis of recycled products from three-step
process

One hundred grams of CCLW were shaken in 1 l of
water and 10 g CaO at 98
C for 3 h. The protein solu-
tion was filtered and separated, stored at 4
C. Then, the
chrome sludge was continuously hydrolyzed four times
at 98
C for 3 h, with 2 g CaO and 100 ml water added
each time. All of hydrolysates filtered were calculated
into the total protein yield. The mixed hydrolyzed pro-
tein solutions and the final chrome cake (containing
protein residues and chromium) were stored at 4
C for
the analysis of amino acid composition.
The recovered samples from three-step process were
analyzed for pH, ash, protein as TKN, chromium, cal-
cium or magnesium. The molecular weight ranges of
protein fractions were estimated by SDS–PAGE (poly-
acrylamide gel electrophoresis in sodium sulfate) and
ÄKTATM explorer (Amershampharmacia, Inc.) GFC
(gel filtration chromatograph).
3. Results

2.4. Analysis of amino acid composition 3.1. Analyses of chrome leather waste

The amino acid compositions of the hydrolyzed pro-
tein products and the residue protein in chrome cake
were determined using a Hitachi model 835-50 analyzer.
The results were compared with natural type I collagen
and pickled pigskin obtained from the same pigskin
tannery.
Table 1 shows the analysis results of the CCLW used
in our experiments. It indicates that the waste contains
about 4% chromic oxide and about 80% protein (the
nitrogen content of collagen is 18%).
3.2. Comparison of alkali and enzymatic hydrolysis

2.5. Three-step hydrolysis process
In the first step, 100 g of the CCLW were suspended
in water and CaO/NaOH was added to increase the
alkalinity to pH=11  0.5. The reaction mixture was
stirred at 70–80
C for 3.5 h, then filtered warm to
separate the gelatin from chrome sludge. In the second
step, 100 g water and 2 g CaO were added to the chrome
sludge at 97–99
C for 3–4 h. Then the mixture was fil-
tered warm through the filter press to separate the col-
lagen hydrolysates from the chrome cake. During the
whole process, pH was controlled at 9–10 to maintain
optimum alkalinity for avoiding chrome dissolution. In
the third step, the chrome cake was dissolved in con-
centrated sulfuric acid with a pH of 1.0–2.0, at 97–99
C
Table 2 presents the protein yields via various alkali
hydrolysis or enzymatic treatment assisted by magne-
sium oxide.
3.3. Amino acid composition of different products from
multi-step alkali hydrolysis
The chromed scraps, with alkali alone or alkali-assis-
tant protease treated, were difficult to completely
hydrolyze, even when increasing dosage of alkali and
enzymes, prolonging reaction time or enhancing hydro-
lysis temperature. Typically, in multi-step alkali hydro-
Table 2
Efficiency of basifiers and enzymes on hydrolysis the waste

Basifiers/enzymes Protein yield (%)a Filtered under vacuum

Table 1
Analyses of chrome leather waste 3h 6h 24 h

Parameter Measure CaO (10%, 98
C) 46.5 68 69.5 Easiest

MgO (10%, 98
C) 38.6 59.8 65.4 Easier
PH 4.09 NaOH (7%, 98
C) 48.2 69.8 71.9 Easy
Moisture 510% 2709 (2%,38
C)b 27.5 30.6 33.4 Difficulty
Asha 11.5% 1398 (2%, 38
C)b 20.2 22.6 23.4 Difficulty
TKNa,b 16.55% Trypsin (2%, 38
C)b 25.3 27.8 31 Difficulty
Chrome oxide (Cr2O3)a 3.72% Alcalase (2%, 72
C)b 30.3 35 39.7 Difficulty
Fata 1.18%
a
Calculated as weight percent based on the dry weight of the
a leather scraps.
Moisture-free basis.
b b
Ash-free basis. Pretreatment with 3% MgO at room temperature for 4 h.
838 C. Mu et al. / Waste Management 23 (2003) 835–843

Table 3
Amino acid compositions of the hydrolysate and the residue protein
(mol%)

Amino Collagen Pickled Hydrolysates Protein

acid (type I) pigskin residues

Thr 1.6 1.19 0.563 0.848

Val 2.3 2.33 3.408 8.137
Leu 2.5 1.99 2.713 4.706
Ile 1.2 1.05 1.031 3.123
Lys 2.8 2.53 2.003 1.923
Hyl 0.7 0.61 1.417 3.126
Tyr 0.4 0.29 0 0.873
Phe 1.3 1.37 2.020 2.664
Met 0.6 0.34 0.786 3.824
Gly 32.7 31.56 35.730 29.109
Hyp 8.6 6.22 2.461 2.331
Pro 13.0 14.72 15.329 12.127
Ala 11.4 10.40 12.971 10.054 Fig. 1. Hydrolysis time dependence of total protein yield in multi-step
Arg 5.2 5.91 3.374 4.091 alkali treatments.
Asp 4.6 4.56 4.051 2.944
Cys 0 0.35 0.621 0 3.4. Establishing a three-step hydrolysis process
Glu 7.5 7.76 6.962 4.995
His 0.5 0.52 0.411 0.534
Ser 3.1 3.00 1.197 1.835
Experiments were conducted on CCLW using a series
NH3 2.240 2.312 of hydrolysis processes. The procedure is outlined in
Unknown 0.714 0.443 Fig. 3. The CCLW are treated with basifiers to extract
Total 100.0 96.7 99.288 99.556 gelatin in the first step and polypeptide in the second,
respectively; and the remaining chrome cake is further
treated with acids to obtain chromium-containing pro-
lysis, as shown in Fig. 1, more than 25% of protein tein hydrolysates. The chemical and physical properties
fraction remained in the ‘‘chrome cake’’ as protein resi- of each product extracted in the three steps are com-
dues, and further increase of the total protein yield is pared in Table 4.
negligible after three hydrolysis treatments.
Table 3 presents the amino acid compositions of the
hydrolysates and the residue protein in chrome cake. In 4. Discussion
order to better compare the differences, the reference
values of the type I collagen (Heidemann, 1993) and the Table 2 shows that the basifiers, i.e., CaO, MgO and
determined values of pickled pigskin are also listed in NaOH, are more efficient and easier to filter than the
Table 3. It shows that the pickled pigskin has a similar enzymes when hydrolyzing the CCLW. We believe that
amino acids composition and content to the type I col- calcium oxide as the source of alkalinity had three sig-
lagen due to dominant type I collagen in a hide/skin nificant advantages over magnesium oxide or sodium
after being pretreated before tanning. The little cystine hydroxide. Firstly, the coagulating properties of calcium
(Cys) that appears in the pickled pigskin can be attrib- sulfate (sulfuric acid group resulted from tanning pro-
uted to type III collagen or hair root in pickled skin. cess) seemed to the precipitation of chromium hydrox-
Most amino acid contents of hydrolysates and protein ide, and the coprecipitation of the two compounds
residues are quite different from that of type I collagen assisted in the separation of chromium hydroxide from
due to alkali hydrolysis. the hydrolysis liquor by plate and frame filtration. Sec-

Table 4
Properties of the recovered products from a three-step process

Samples pH Asha,b Ca/Mga,b Cra,b TKNa,b Main molecular

weight distribution (kD)

Gelatin 6 6.3 0.04 0.0150 17.4 40 110

Polypeptide 6 8.8 0.12 0.0740 16.9 10 50
Chromium-containinghydrolysate 2 46 – 8.6 10.5 0.2 10
a
Moisture free basis.
b
Expressed as percentage.
c
Ash free basis.
 C. Mu et al. / Waste Management 23 (2003) 835–843
ondly, the total ash of the resultant hydrolysate was
minimized when using Calcium oxide, and can con-
sistently be maintained below 10% on a dry-basis. This
agrees with results reported elsewhere (Stockman,
1996). Third, using NaOH in the treatment of CCLW
can lead to a rapid increase of alkali strength at the
initial stage, thus resulting in excessive digestion of col-
lagen. Chromium hydroxide is an amphoteric hydroxide
and it will be dissolved when the liquor pH is below 5.5
or over 12 [as shown in Eq. (1)]. It seems that using
Ca(OH)2 resulted in steady hydrolysis due to its buffer-
ing property.
OH OH
Cr3þ *
) CrðOHÞ3 # *
) CrO
2 ð1Þ
Hþ Hþ
As shown in Table 5, the 14 kinds of amino acid
contents differ greatly between the protein residues and
hydrolysates. Non-polar amino acids (Val, Phe, Leu, Ile
and Met), alkaline amino acid (Hyl, Arg and His) and
Fig. 2. A schematic of oxolation chromium(III) complexes formed during basification and its complexation with protein carboxyl.
839
hydroxy-amino-acid (Ser, Tyr and Thr) have much
higher contents in protein residues than in the hydro-
lysates, while the hydrophilic acidic amino acids (Asp
and Glu) contents of protein residues are lower than
that of the hydrolysates. Note that the alkaline amino
acids are hydrophobic under alkaline conditions.
Therefore, we can conclude that the protein residues in
chrome cake were difficult to hydrolyze and dissolve in
alkaline solution.
We see three possible reasons for the incomplete
hydrolysis of CCLW in our experiments.
1. Hydrophobic interaction: Non-polar amino acids
and alkaline amino acids are all hydrophobic in
alkaline conditions, and because they are com-
mon in the residue protein, they could form
hydrophobic domains and tight clusters inacces-
sible to water, leading to the protein resisting
hydrolysis.
840 C. Mu et al. / Waste Management 23 (2003) 835–843

2. Covalent bridges: The products in the residue
protein might have covalent cross-linking formed
between alkaline amino acids and hydroxy amino
acids. These covalent bonds might break under
acidic conditions leading to the complete hydro-
lysis of protein residues with acids to obtain
chromium-containing protein hydrolysates.
3. Cross-linking with chromium(III) complex:
Under alkaline condition (pH < 12), most of the
coordinated chromium are divorced from the
carboxyl groups on the side chain of aspartic acid
(Asp) and glutamic acid (Glu) and precipitated as
Cr(OH)3. However, oxolation chromium(III)
complexes formed during basification (as sche-
matically shown in Fig. 2) have strong resistance
to alkali. It could crosslink with the carboxyl
groups of a few Asp and Glu, or protein hydro-
lysates, and form insoluble macromolecular
metal complexes. When using peroxide to oxidize
the Cr(III) to Cr(IV), we found that most of the
protein residues were dissolved soon even in
alkaline solution, which supports this possibility.
In addition, a certain amount of cystine (Cys)
appeared in the hydrolysates, but not in chrome

Fig. 3. Outline of three-step process for treatment and utilization of chromium-containing leather wastes.
 C. Mu et al. / Waste Management 23 (2003) 835–843 841

cake, which indicates that the S–S crosslinking in
cystine has nothing to do with the residue protein.
The results presented here are for the CCLW of one
specific tannery; however, we have found that the chro-
mic oxide and protein contents of CCLW vary within
relatively narrow ranges. As a result, we believe the
treatment procedures proposed could be easily adjusted
for other CCLW.
The gelatin isolated by hydrolysis (see Fig. 3) could be
chemically modified for the preparation of proteinic
leather finishing agents, a highly value-added product.
A possible flow chart is given in Fig. 4. In this scheme,
the recovered collagen polypeptides (i.e., protein
hydrolysates) are chemically modified with certain
bifunctional monomers of acrylic acid series and mod-
ified wax to produce leather retanning agents. The
chromium containing hydrolysates are further modified
with acrylic acid series monomers and developed into
retanning agent which can be recycled into tanning and
retanning process. The detailed preparation and use of
the final products will be the subject of future work. A
patent has been applied for (Mu et al. 2000) and pilot
scale studies are being carried out at present.

Fig. 4. Flow diagram of the procedure for gelatin modification to produce leather finishing.
842 C. Mu et al. / Waste Management 23 (2003) 835–843

Table 5
Comparison of some amino acids in hydrolysates and protein residues (mol%)

Amino acid Side chain group Performance of the Group Hydrolysates Protein residues

Val –CH2–(CH3)2 Nonpolar–hydrophobic 3.408 8.137

Phe –CH2–C6H6 Nonpolar–hydrophobic 2.020 2.664
Leu –CH2CH2–(CH3)2 Nonpolar–hydrophobic 2.713 4.706
Ile –CH (CH3)–CH2CH3 Nonpolar–hydrophobic 1.031 3.123
Met –CH2CH2–S–CH3 Nonpolar–hydrophobic 0.786 3.824
Ser –CH2–OH Polar–hydrophilic 1.197 1.835
Tyr –CH2–C6H6–OH Polar–hydrophilic 0 0.873
Thr –CHOH–CH3 Polar–hydrophilic 0.563 0.848
Hyl –CH2CH2CHOH–NH2 Alkali–hydrophilic 1.417 3.126
Arg Alkali–hydrophilic 3.374 4.091

His Alkali–hydrophilic 0.411 0.534

Asp -CH2COOH Acidic–hydrophilic 4.051 2.944

Glu –CH2CH2COOH Acidic–hydrophilic 6.962 4.995
Cys –CH2–S–S–CH2– Cross–linking 0.621 0

5. Conclusions Foundation of Chinese Academy of Science (No.

The comparisons of various alkali and enzymatic
hydrolysis show that CaO as a source of alkalinity had
advantages over MgO, NaOH and enzymes plus MgO
pretreatment. By analysis of amino acid compositions, it
can be concluded that the residue protein in chrome
cake was difficult to hydrolyze completely under alka-
line conditions due to hydrophobic interaction, covalent
bridges, or cross-linking induced by chromium/carboxyl
groups complexation. A three-step process is presented
for the treatment of chrome leather waste and extrac-
tion of valuable products at different stages. The gelatin
has potential to be chemically modified to produce
value-added leather finishing agents. The collagen
hydrolysate has potential to be used as proteinic retan-
ning agents by modification. As a third step, the
remaining chrome cake has the potential to be further
hydrolyzed with acids to obtain chromium-containing
hydrolysates suitable for the preparation of chromium-
containing proteinic retanning agents. This research
indicates great potential to avoid the trouble and pollu-
tion shown in other research (Cabeza et al., 1998d,
1999b) when treating chrome cake for chromium
recovery. This process can help the leather industry in
solving the difficult CCLW disposal problem and obtain
economic benefits.
Acknowledgements
Financial support from the National Nature Science
Foundation of China (NNSFC, No 29877017), the
KJ951-A1-510) and Kuancheng Wang Postdoctoral
Work Fund are gratefully acknowledged. The open
laboratory of Bond-Selective Chemistry in USTC pro-
vided some analysis facilities.
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