Appl Microbiol Biotechnol (2001) 56:81–87

DOI 10.1007/s002530000587

MINI-REVIEW

G. McMullan · C. Meehan · A. Conneely · N. Kirby
T. Robinson · P. Nigam · I. M. Banat · R. Marchant
W. F. Smyth

Microbial decolourisation and degradation of textile dyes
Received: 12 October 2000 / Received revision: 22 November 2000 / Accepted: 24 November 2000 / Published online: 19 May 2001
© Springer-Verlag 2001

Abstract Dyes and dyestuffs find use in a wide range of
industries but are of primary importance to textile manufacturing. Wastewater from the textile industry can contain a variety of polluting substances including dyes. Increasingly, environmental legislation is being imposed to
control the release of dyes, in particular azo-based compounds, into the environment. The ability of microorganisms to decolourise and metabolise dyes has long been
known, and the use of bioremediation based technologies
for treating textile wastewater has attracted interest.
Within this review, we investigate the mechanisms by
which diverse categories of microorganisms, such as the
white-rot fungi and anaerobic bacterial consortia, bring
about the degradation of dyestuffs.

Introduction
Dyes and dyestuffs are widely used within the food,
pharmaceutical, cosmetic, textile and leather industries.
Over 100,000 commercially available dyes exist and
more than 7×105 tonnes of dyestuff are produced annually (Meyer 1981; Zollinger 1987). The human health
impact of dyes used in the food industry, especially
azo dyes and their degradation products, has caused concern for a number of years, with legislation controlling
their use being developed in a variety of countries
(Hildenbrand et al. 1999). Increasingly, the environmental and subsequent health effects of dyes released in
textile industry wastewater are becoming subject to
scientific scrutiny. Wastewater from the textile industry
is a complex mixture of many polluting substances rangG. McMullan (✉) · C. Meehan · A. Conneely · N. Kirby
I.M. Banat · R. Marchant
School of Environmental Studies, University of Ulster, Coleraine,
County Londonderry, BT52 1SA, UK
e-mail: g.mcmullan@ulst.ac.uk
Tel.: +44-28-70324755, Fax: +44-28-70324911
T. Robinson · P. Nigam · W.F. Smyth
School of Biomedical Sciences, University of Ulster, Coleraine,
County Londonderry, BT52 1SA, UK

ing from organochlorine-based pesticides to heavy
metals associated with dyes and the dyeing process
(Correia et al. 1994).
During textile processing, inefficiencies in dyeing result in large amounts of the dyestuff being directly lost to
the wastewater, which ultimately finds its way into the
environment. The amount of dye lost is dependent upon
the class of dye application used, varying from only 2%
loss when using basic dyes to a 50% loss when certain
reactive dyes are used (for a comprehensive review of
this area, the types of dyes found in textile effluent and
colour discharge consent limits see O’Neill et al. 1999).
Due to increasingly stringent environmental legislation,
the textile industry in the UK and elsewhere is seeking to
develop effective wastewater remediation technologies,
especially those that allow colour removal that is largely
unaffected by conventional treatment systems (O’Neill
et al. 2000). Despite the existence of a variety of chemical and physical treatment processes, bioremediation of
textile effluent is still seen as an attractive solution due
to its reputation as a low-cost, environmentally friendly,
and publicly acceptable treatment technology (Banat
et al. 1996).
A number of biological processes such as biosorption
have been proposed as having potential application in
removal of dyes from textile wastewater (Bustard et al.
1998); however, this review will focus upon the decolourisation and degradation of textile dyes by both mixed
and axenic cultures of bacteria and fungi.

Bacterial decolourisation and degradation
of textile dyes
Actinomycetes
Actinomycetes, particularly Streptomyces species, are
known to produce extracellular peroxidases that have a
role in the biodegradation of lignin. These prokaryotic
peroxidases are involved in the initial oxidation of lignin
to produce various water-soluble polymeric compounds.

Indeed. In 1989. Streptomyces sp. chromofuscus A11 and P. extracellular peroxidases had been shown to be produced by Streptomyces species and the enzymes were shown to have substrate specificities similar to the Mn(II)-peroxidase of P. . coupled with their finding that enhanced dye decolourisation could be achieved as a result of extracellular H2O2 production when strains were grown in the presence of glucose. 1982. Orange I azoreductase[NAD(P)H:1-(4′-sulfophenylazo)-4-naphthol oxidoreductase] and Orange II azoreductase [NAD(P)H:1(4′-sulfophenylazo)-2-naphthol oxidoreductase]. and Thermomonospora fusca MT800. chrysosporium (Paszczynski et al. oxidation. Burke and Crawford (1998) partially purified a novel extracellular peroxidase from S. Previously. ranging from the azo compound Reactive Red 147 to the phthalocyanine Reactive Blue 116. were purified and characterised from a Pseudomonas strain K24 (Zimmermann et al. Other aerobic bacteria With the notable exception of the actinomyctetes. Further purification of the peroxidase in question is required to finally confirm its true biochemical nature. no correlation between decolourising activity and ligninolytic activity (as measured by oxidation of veratryl alcohol. Both these enzymes have now been classified as being the same enzyme. 1984). utilisation of syringic or coumaric acid. with the gene oxyR. This resulted in the simultaneous split of the azo linkage both symmetrically and asymmetrically to produce intermediates which subsequently undergo several redox reactions before producing more stable intermediates (Fig. with a strong correlation between the ability of the isolate to decolourise dyes and its ligninolytic capability. known correctly as azobenzene reductase (EC 1. The enzymatic processes involved in the decolourisation of this dye remain unexplained. and dealkylation reactions against various xenobiotic compounds (Goszczynski et al. a group based at the University of Idaho and led by Don Crawford initiated an investigation into the ability of ligninolytic microbes. Recently. The ability of actinomycetes to decolourise and mineralise textile dyes was initially investigated by three groups. apparently having some regulatory role (Ramachandran et al. Finally. both white-rot fungi and Streptomycetes. RBBR and Poly B-411. 1994). The finding that actinomycetes are capable of the aerobic decolourisation and degradation of azo dyes was significant given the recalcitrance of the compounds to degradation by other bacteria under such conditions. as well as the azo dye Remazol Brilliant Blue R (RBBR) (Pasti and Crawford 1991). Poly B-411 and Poly R-478. with the third dye. Initial work confirmed that decolourisation was related to the ligninolytic capabilities of the isolate but that the bacterial enzymatic systems responsible for degradation of azo dyes had a different specificity than those of the white-rot fungus P. 1). Of particular interest in this study was the investigators’ use of actual textile effluents in the screening process. screened 20 strains of actinomycetes. identical results were essentially obtained. chrysosporium was elucidated in a series of elegant experiments (Goszczynski et al. 1992). chrysosporium (Pasti and Crawford 1991). It was proposed that the peroxidases of both organisms converted the azo dye to a cation radical that was susceptible to the nucleophilic attack of water or hydrogen peroxide.7). 2000). Initially. With two of the dyes. Each dye was structurally distinct. strain EC22. The peroxidase was found to have a substrate specificity similar to that of fungal Mn-peroxidases and was not inhibited by KCN. the isolation of bacteria capable of the aerobic decolourisation and mineralisation of dyes. This observation. The molecular mechanism by which this peroxidase is induced has also recently been investigated. Ball et al. suggested the involvement of peroxidases in the decolourisation process. to mineralise and decolourise textile dyes. especially sulfonated azo dyes. 14 streptomycetes were investigated for their ability to decolourise two polymeric dyes. and acid-precipitable polymeric lignins) was observed. Further work was carried out by Crawford’s group to investigate the mechanism by which Streptomyces chromofuscus A11 decolourised and mineralised azo dyes. In addition.6.82 Actinomycetes have also been shown to catalyse hydroxylation. for their ability to decolourise the polymeric dye Poly R (Ball et al. 1994). including one notable report on the greening of instant chocolate puddings (Dykes et al. representing a wide range of genera. The widespread ability of actinomycetes to bring about dye decolourisation was demonstrated by positive results being obtained for 83 of the isolates. Zhou and Zimmermann (1993) embarked on an even larger screening process in which the decolourising capabilities of 159 actinomycetes were investigated. but most significantly. Poly R-478. oxygen-insensitive azoreductases. Certain carboxylated analogues of sulfonated azo compounds are also utilised aerobically as sole carbon and energy source by preadapted bacteria. 1994). Interestingly. Five separate effluents each containing a single dye of known concentration were used. Subsequently. Only three of the 20 strains were observed to significantly decolourise the dye: Streptomyces badius 252. viridosporus T7A in an effort to identify the class of peroxidase involved in dye decolourisation by Streptomyces species. N-terminal amino acid sequences of the peroxidase were found to share significant homology with a fungal Mn-peroxidase and actinomycete cellulases. has proven difficult. the actual decolourisation and degradation pathway for two azo dyes by both S. Subsequently. 1989).6. an inhibitor of hemeperoxidases (Magnuson 1996). which encodes an oxygen stress regulatory protein. A number of reports exist suggesting the aerobic conversion of specific azo dyes.

1992). [9b] 4-hydroxybenzenesulfonamide. R1=R2=O and B=O. which then entered the β-ketoadipic acid pathway. Recently. however. 1998). methyl violet. which results in dye decolourisation and the production of colourless aromatic amines. [4a] 4-nitrosobenzenesulfonic acid. 1998). [7b] 2-methoxy-4-aminophenol.6-dimethyl-1.4-benzoquinone. by a strain of Pseudomonas mendocina MCM B-402. substitution pattern b (as in II). Anaerobic bacterial decolourisation and degradation of textile dyes Under anaerobic conditions many bacteria have been reported to readily decolourise azo-dyes. and B=NH. Under anoxic conditions. [12] ammonia. the ability of bacteria to aerobically metabolise other dye classes has also attracted interest but yielded little success. [11a] azobenzene-4. [8a] sulfanilic acid. was used by the isolate as sole carbon and energy source. [10a] benzenesulfonic acid. (Reproduced from Goszczynski et al. Attempts to characterise the enzyme responsible for the azo-bond cleavage in crude cell extracts have so far proven unsuccessful. Substitution pattern a (as in I). their environmental impact is now also troublesome. The initial step in bacterial azo dye metabolism under anaerobic conditions involves the reductive cleavage of the azo linkage. but their existence is rationalised as necessary intermediates for the observed final products. mendocina degraded the dye via a number of unidentified metabolites to phenol. In addition to azo dyes. Sarnaik and Kanekar (1999) described the aerobic mineralisation of the triphenylmethane dye. Methyl violet. and carcinogenicity of such compounds is well-documented and has been reviewed elsewhere (Chung et al. the bacteria bring about the reductive cleavage of the azo linkage. Whilst concerns have long been expressed over the threat that such compounds have on human health. which has some commercial applications in addition to its recognised use as a bacteriological and histological stain. The potential toxicity. [9a] 4-hydroxybenznesulfonic acid. R2=OCH. Reports indicate that intestinal bacteria decolourise certain azo dyes and their polymeric derivatives at roughly . [6b] 2-methoxyhydroquinone. This process is catalysed by a variety of soluble cytoplasmic enzymes with low-substrate specificity which are known trivially as “azoreductases”. [8b] sulfanilamide. Blhmel et al. these enzymes facilitate the transfer of electrons via soluble flavins to the azo dye. uncertain. Preliminary studies identified that P. [2a] 2. Initially.83 Fig. Baughmann and Weber (1994) demonstrated that in anoxic sediment environments uncharged azo dyes readily undergo biologically (and presumably microbial)-mediated reduction to the corresponding amines. [10b] benzenesulfonamide. Recently. which is then reduced.4′-disulfonic acid. capable of utilising the model sulphonated azo compound 4-carboxy-4′-sulfoazobenzene (CSAB) as sole carbon and energy source. however. Elucidation of the degradation pathway demonstrated that the azo linkage of CSAB undergoes an initial reductive cleavage to form 4-aminobenzoate and 4-aminobenzenesulfonate. 1994) Despite this it has been argued that unequivocal evidence for aerobic bacterial mineralisation of these compounds is absent from the literature (Blhmel et al. (1998) reported the isolation of an unidentified bacterial strain. S5 (Genbank accession number AF019037). R1=H. The role that such cytoplasmic enzymes have in vivo is. 1 Proposed pathway for peroxidase-catalysed degradation of sulfonated azo dyes. The compounds represented by numbers in brackets have been found in reaction mixtures. which are subsequently metabolised by conventional aromatic catabolic pathways (Blhmel et al. mutagenicity. The compounds in parentheses have not been found.

such as lignin peroxidase (LiP).4-phenylenediamine) accumulating in the reactor. Anaerobic-aerobic biodegradation of dyes To overcome the problem of the relative recalcitrance of azo dye breakdown products under anoxic conditions. which distinguishes them from biodegradative bacteria that tend to be rather substrate-specific (Reddy 1995). the decolourisation of dyes has been used by others to rapidly assess the biodegradative capabilities of diverse white-rot fungi (Field et al. the first report appeared in the literature of sulfonated azo dyes being decolourised. 2000. Unfortunately. as well as a variety of other isolates are increasingly being studied (Conneely et al. whilst MnP oxidises Mn2+ to Mn3+ which is able to oxidise many phenolic compounds (Glenn et al.11. which has a complex polymeric structure. BN6 coimmobilised with an uncharacterised 5-aminosalicylatedegrading isolate in alginate beads. all readily reduced the triphenylmethane dye malachite green. atomic absorption spectrometry. Whilst P.1. These observations suggest that it may be possible to develop biofilm-based reactors for the complete mineralisation of industrial-dye-contaminated wastewaters. which are then metabolised relatively easily under aerobic conditions. 1998. In 1997. was possible. A detailed review on the anaerobic treatment of textile effluents can be found elsewhere (Delee et al. mouse. 1999). Swamy and Ramsay 1999). At the aerobic surface of the beads. Figure 1). (1997) demonstrated that a range of axenic bacterial cultures which are commonly found in the human gastro-intestinal tract. complete mineralisation of only one of the azo cleavage products. and polarography (Conneely et al. Recently. the degradative pathways utilised by white-rot fungi other than P. complete mineralisation of the molecule is difficult. and rat intestines. 1994. As it is unlikely that these polymeric dye molecules. This subject will be returned to below in the section “Current state of the art”. LiP catalyses the oxidation of non-phenolic aromatic compounds such as veratryl alcohol. the bacterial metabolism of other dye molecules under anoxic conditions has also been studied. chrysosporium remains the most widely studied of white-rot fungi.3. 2000. Subsequently. This group of organisms is central to the global carbon cycle as a result of their ability to mineralise the woody plant material lignin. (1997) reported the partial mineralisation of the azo dye Mordant Orange 1 by a methanogenic granular sludge in a continuous-upflow anaerobic sludge blanket. Trametes (Coriolus) versicolor. 1999). The decolourisation of dyes by white-rot fungi was first reported by Glenn and Gold (1983). Laccase (benzenediol:oxygen oxidoreductase. 1986). Initial data indicated that the dye structure was readily de- . again by P. Kudlich et al. EC 1. 1997). In 1990. due to the inherent complexity both of the dye molecules themselves and the enzymatic mechanisms involved. with the other product (1. 6A2NS was also converted to 5AS by Sphingomonas sp. Whilst the anaerobic reduction of azo dyes is relatively easy to achieve. Bjerkandera adusta. The metabolite produced. described the complete mineralisation of the sulphonated azo dye Mordant Yellow 3 by the bacterium Sphingomonas sp. BN6 before being mineralised by cells of the isolate 5AS1. manganese peroxidase (MnP) (EC 1. is a suspected carcinogen and raises concerns over the continued use of malachite green in aquaculture in various regions worldwide. can actually pass through the bacterial cell membrane.13). a number of groups have used a two-stage treatment process (Oxspring et al. In addition to azo dyes. who developed a method to measure ligninolytic activity of Phanerochaete chrysosporium based upon the decolourisation of a number of sulfonated polymeric dyes. but briefly. 1998). In this study. These enzymes and their catalytic properties are reviewed elsewhere (Hattaka 1994). chrysosporium remain unstudied. Fungal decolourisation and degradation of textile dyes White-rot fungi By far the most widely studied of dye-decolourising microorganisms are the white-rot fungi.2) is a copper-containing enzyme that catalyses the oxidation of phenolic substrates by coupling it to the reduction of oxygen to water (Edens et al. white-rot fungi have been found to be capable of mineralising a diverse range of persistent organic pollutants. 2000). chrysosporium (Cripps et al. however. Although the beads were maintained under aerobic conditions. Heinfling et al. O’Neill et al. In addition to their natural substrate. despite the exploitation of powerful analytical techniques (Smyth et al. The ability of these fungi to degrade such a range of organic compounds results from the relatively non-specific nature of their ligninolytic enzymes. Pointing et al. their centres maintained anoxic conditions and it was here that cells of Sphingomonas sp. In the first anaerobic stage. 1993). and a degradation pathway for this isolate was elucidated (Goszczynski et al. 1990). as well as consortia of microbes from human. Pleurotus and Phlebia species. leucomalachite green. 1999. the azo dye is readily reduced to the corresponding colourless aromatic amines.84 equivalent rates (Brown 1981). then the possibility of non-cytoplasmic “azoreductase” capabilities exists (Keck et al. Kirby et al. 1999).10. BN6 reductively cleaved Mordant Yellow 3 to produce 5-aminosalicylate and 6-aminonaphthalene-2-sulfonate. Donlon et al. chrysosporium using such analytical tools as HPLC. our own group began attempts to elucidate the degradation pathway of copper-phthalocyanine dyes by P. 5-aminosalicylic acid. 1996. and laccase. Henderson et al. or highly charged sulphonated azo dyes.

Their work focused upon the gram-negative isolate Sphingomonas sp. xenophaga (Russ et al. 2000). chrysosporium. been shown to represent a novel species named Sphingomonas xenophaga after its ability to “eat foreign compounds” (Stolz et al. Whilst it is clear that enzymes such as LiP. non-ligninolytic.6-trinitrotoluene in P.chrysosporium ligninolytic enzymes. candidumDec1-based bioreactors to be developed for the treatment of diverse organic pollutants including dyestuffs.4. 1997. and manganese-independent peroxidase activities also produced by the isolate. The potential importance of this isolate for dye decolourisation rests with its robustness in comparison to P. It was demonstrated that an extracellular mechanism of dye reduction existed in addition to the nonspecific cytoplasmic enzymes which functioned as “azoreductases” by transferring electrons via reduced flavin groups to the dye molecule and thus bringing about a purely chemical reduction. and other peroxidases previously reported (Kim and Shoda 1999a). Detailed investigations have been carried out on one such isolate. The plasma membrane redox system of white-rot fungi has been proposed as a potential mechanism for dye decolourisation. Kudlich et al. In many early studies. Vyas and Molitoris (1995) proposed that such observations indicate that decolourisation is not a single-step reaction and that these intermediate steps can be missed if enzyme activities are high. 2000). These findings demonstrate that the cytoplasmic azoreductases previously described in the literature are likely to be a laboratory artefact and . Recently the gene (dyp) encoding DyP was cloned into the heterologous expression host Aspergillus oryzae to allow greater protein production in a safe host (Sugano et al. Kirby (1999). and from LiP and veratryl alcohol oxidase activities. Non-white-rot fungi Whilst degradation pathways utilised by these fungi are not described in the literature. chrysosporium and other white-rot fungi. found little evidence to suggest that such a mechanism was involved in decolourisation of Remazol Black B by strains of P. dyes were only added to culture media when conditions for the production of ligninolytic enzymes prevailed. 2000). 1990). having a novel haeme-binding region. To investigate if cytoplasmic enzymes played any role in dye decolourisation in vivo. is unaffected by the shear forces of shake flasks or stirred tank reactors (Kim and Shoda 1998. The activity was named RBBR oxygenase as it possessed a catalytic metal centre (possiblely haeme) and was inhibited by a number of known oxygenase inhibitors (Vyas and Molitoris 1995). Germany (Keck et al. DyP is produced constitutively and. 1997. ostreatus but are well-known in other white-rot fungi. who found that such a mechanism was responsible for the degradation of 2. Current state of the art The role of bacterial cytoplasmic and extracellular “azoreductases” in azo dye reduction in vivo has recently been clarified by investigators at the University of Stuttgart. Kudlich et al. 1997) (Fig. however. Molecular analysis of the protein confirmed that DyP is distinct from other peroxidases in the plant peroxidase superfamily. which were not detectable in P. care must be taken not to exclude the possibility of the existence of other degradative mechanisms. candidum which had properties distinct from LiP. For example. coli and S. or Phlebia tremellosa. T. (Cripps et al. both free copper and organo-copper breakdown products were found in culture supernatants and further work is needed to elucidate their identity. thus excluding the potential discovery of other. This activity was distinct from the MnP. and laccase play a significant role in dye metabolism by white-rot fungi. Russ et al. Pasti and Crawford (1991) have suggested the existence of alternative systems or enzymes in dye decolourisation by white-rot fungi. Such properties should allow a number of G. in whole cell studies these strains showed little improvement in their dyedecolourising capabilities. Vyas and Molitoris (1995) discovered that Pleurotus ostreatus produced an unusual enzyme during the solidstate fermentation of wheat straw that was capable of Remazol Brilliant Blue R (RBBR) decolourisation. a strain of Geotrichum candidum Dec1 iso- lated from soil and capable of decolourising a number of anthraquinone dyes (Kim et al. 2). however. 1995). (1997) demonstrated that certain quinone-based compounds generated during metabolism of specific substrates acted as mediators shuttling redox equivalents to azo dye molecules from the bacterial membrane (Keck et al. versicolor. through molecular analysis. a glycosylated haeme-based peroxidase (DyP) was purified from G. processes.85 graded. laccase. however. The broad substrate specificity exhibited by this isolate led Kim and Shoda (1999a) to propose the existence of an extracellular peroxidase-type enzyme. horseradish peroxidase. chrysosporium. a flavin reductase [NAD(P)H:flavin oxidoreductase] was cloned and overexpressed in both E. which has recently. 1999b). Supportive evidence was obtained by Stahl and Aust (1993). 1997. 2000). 1997). and it is interesting to draw parallels between this and the redox-mediated mechanisms utilised by bacteria under anaerobic conditions. MnP. Subsequently. BN6. In cell extracts the strains with overexpressed flavin reductase demonstrated elevated azo reductase activity. unlike the activity of P. MnP. Keck et al. resulting in decolourisation. it is expected that they would be similar to those reported to be involved in the metabolism of other aromatic hydrocarbons (Wunderwald et al. The work of Vyas and Molitoris is also of note as it documents a phenomenon seen by many researchers of white-rot fungal dye decolourisation: the sequential change of blue dyes to colourless through a rainbow of intermediates (Kirby 1999).

Lema J M (1995) Production of lignin peroxidase by Phanerochaete chrysosporium in a packed-bed bioreactor in semi-continuous mode. Environ Sci Technol 28:267–276 Blhmel S. De Bont JAM (1993) Screening for ligninolytic fungi applicable to the biodegradation of xenobiotics. Timm RG. chrysosporium (Kirby 1999). Bioprocess Eng 19:427–430 Chung KT. (1995). FEMS Microbiol Letts 165:43–50 . A range of reactor systems aimed at optimising production of ligninolytic enzymes has been developed. with the exception of Allemann et al. Environ Technol 15:917–929 Cripps C. Stevens SE Jr. who investigated pentachlorophenol. Goins TQ. Appl Environ Microbiol 56:1114–1118 Delée W. Nigam P. Appl Environ Microbiol 65:3071–3074 Feijoo G. FEMS Microbiol Lett 179:333–337 Correia VM. 1986). Water Res 29:61–67 Ball AS. respectively. McMullan G. 1995). 2000). Appl Environ Microbiol 55:1642–1644 Banat IM. Biores Technol 58:217–227 Baughman GL. Orange II azo dye. Dosoretz D. In addition. Whilst many groups have demonstrated the ability of white-rot fungi to decolourise and degrade textile dyes. robust. Pasti-Grigsby MB. Zhang et al. J Chem Technol Biotechnol 73:323–335 Donlon B. Appl Environ Microbiol 64:2315–2317 Brown JP (1981) Reduction of polymeric azo and nitro dyes by intestinal bacteria. Marchant R (1996) Microbial decolorization of textile-dye-containing effluents: a review. Appl Microbiol Biotechnol 49:523–530 Bustard M. Vonholy A (1994) Azoreductase activity in bacteria associated with the greening of instant chocolate puddings. Gold MH (1986) Mn(II) oxidation is the principal function of the extracellular Mn peroxidase from Phanerochaete chrysosporium. (2000). and it may be that extraction and concentration of dyes and other pollutants is required before bioremediation is feasible (Nigam et al. Smyth WF. Appl Environ Microbiol 45:1741–1747 Glenn JK. Gold MH (1983) Decolorization of several polymeric dyes by the lignin-degrading basidiomycete Phanerochaete chrysosporium. Betts WB. the development of potential remediation solutions for the textile industry based upon these microorganisms has been slow. Crawford RL. Feijoo-Costa G. Stephenson T. Akileswara L. Dooley D. References Alleman BC. Pinheiro HM (1998) Anaerobic treatment of textile effluents: a review. Razo-Flores E. and Everzol Turquoise Blue G dye degradation. Bumpus JA.86 Fig. McCarthy AJ (1989) Degradation of ligninrelated compounds by actinomycetes. Field J (1997) Detoxification and partial mineralization of the azo dye Mordant Orange 1 in a continuous upflow anaerobic sludge-blanket reactor. J Bacteriol 176:1339–1347 Hattaka A (1994) Lignin-modifying enzymes from selected whiterot fungi – production and role in lignin degradation. Our own group utilised the rotating-tube bioreactor system described by Allemann et al. Singh D. the volumes of effluent generated by many of the larger dyeing plants worldwide needs to be considered. Crawford DL (1998) Use of azo dye ligand chromatography for the partial purification of a novel extracellular peroxidase from Streptomyces viridosporus T7A. many problems still face researchers in this area due to the lack of reliable. (2000) also provided evidence that reports of aerobic azo reductases could be explained by the isolates in which such a phenomenon was described having elevated flavin reductase activities. Crawford DL (1994) New pathway for degradation of sulfonated azo dyes by microbial peroxidases of by Phanerochaete chrysosporium and Streptomyces chromofuscus. 2 Proposed mechanism for the redox mediator (RM)-dependent reduction of azo dyes by strain BN6. Weber EJ (1994) Transformation of dyes and related compounds in anoxic sediment: kinetics and products. Swarts H. McMullan G (1999) Metabolism of the phthalocyanine textile dye remazol turquoise blue by Phanerochaete chrysosporium. Contzen M. Stolz A. Appl Microbiol Biotechnol 47:83–90 Dykes GA. This reactor configuration proved to be robust enough to continuously decolourise three different mixed azo dye effluents by greater than 90% over the 38-day operating period (Kirby 1999). Bergbauer M. Cerniglia CR (1992) The reduction of azo dyes by the intestinal microflora. Few of these studies have focused upon the ability of such reactors to remediate pollutants. (Reproduced from Keck et al. Lutz M. tritici. Crit Rev Microbiol 18:175–190 Conneely A. and economic white-rot-fungi-based reactors. packed-bed reactors (Feijoo et al. Finally. Gilbertson RL (1995) Degradation of pentachlorophenol by fixed films of white rot fungi in rotating tube bioreactors. Martinez AT. 1997) play no significant role in dye decolourisation in vivo. and rotating disk reactors (Kirk et al. Appl Environ Microbiol 60:3027–3029 Edens WA. Paszczynski A. Judd SJ (1994) Characterisation of textile wastewaters – a review. including stirred tank reactors (Linko 1988). Arch Biochem Biophys 251: 688–696 Goszczynski S. J Biotechnol 42:247–253 Field JA. Lettinga G. (1999). (1995) to investigate the remediation of actual textile effluent by P. Luijten M. Russ et al. Martinez MJ. Szewzyk U (1998) Purification and characterization of peroxidases from the dye-decolorizing fungus Bjerkandera adusta. Trends Biotechnol 11:44–48 Glenn JK. De Jong E. O’Neill C. Whilst such findings are encouraging. Hawkes FR. Aust SD (1990) Biodegradation of azo and heterocyclic dyes by Phanerochaete chrysosporium. Henson JM (1999) Purification and characterization of secreted laccase of Gaeumannomyces graminis var. FEMS Microbiol Rev 13:125–135 Heinfling A. Logan BE. Knackmuss HJ (1998) Isolation of a bacterial strain with the ability to utilize the sulfonated azo compound 4-carboxy-4′-sulfo-azobenzene as the sole source of carbon and energy. McHale AP (1998) Biosorption of textile dyes by biomass derived from Kluyveromyces marxianus IMB3. and Kapdan et al. Appl Environ Microbiol 41:1283–1286 Burke NS.

Int Arch Occup Environ Health 72 (Suppl 3):M52-M56 Kapdan IK. measurement. Klein J. Hawkes FR. McMullan G. Ph. Biotechnol Bioeng 62:114–119 Kim SJ. Leisinger T (1984) Comparison of 2 bacterial azoreductases acquired during adaption to growth on azo dyes. strain BN6. Armour G. Cook AM. Klein J. University of Idaho Meyer U (1981)Biodegradation of synthetic organic colorants. Enz Microbiol Technol 8:27–32 Kudlich M. Wodarz R. Lopez A. pp 371–385 Nigam P. Appl Microbiol Biotechnol 52:251–254 Smyth WF. Kudlich M. McMullan G (1999) Application of electrospray mass spectometry in the detection and determination of Remazol textile dyes. Marchant R. Curr Opin Biotechnol 6:320–328 Russ R. FEMS Symposium 12. J Chem Technol Biotechnol 74:1009–1018 O’Neill C. FEMS Microbiol Lett 107:157–162 Zimmermann T. ahpX and oxyR in Streptomyces viridosporus T7Aa lignocellulose degrading actinomycete. Biotechnol Tech 12:497–499 Kim SJ. Hawkes DL. Tien M. McMullan G. Nakano R. 61:3919–2927 Wunderwald U. Sasaki K. Shoda M (2000) Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase. Appl Environ Microbiol 66:1429–1434 Sarnaik S.N which degrade xenobiotic aromatic compounds. Stolz A. Environ. Enz Microbiol Technol 10:410– 417 Magnuson TS (1996) Biochemical and genetic studies on the lignocellulose degradation system of Streptomyces viridiosporus T7A. McMullan G (2000) Physical removal of textile dyes from effluents and solid-state fermentation of dye-adsorbed agricultural residues. Zimmermann W (1993) Decolorization of industrial effluents containing reactive dyes by actinomycetes. properties and applications of organic dyes and pigments. Kargi F. Shoda M (1999a) Decolorization of molasses and a dye by a newly isolated strain of fungus Geotrichum candidum Dec 1. Knapp JS. Kanekar P (1999) Biodegradation of methyl violet by Pseudomonas mendocina MCM B-402. for strains BN6T and N. FEMS Microbiol Lett 188:93–96 Kirk TK. Hawkes DL. Arch Microbiol 138:37–43 Zollinger H (1987) Colour chemistry – synthesis. Mattes R (1997) Reduction of azo dyes by redox mediators originating in the naphthalenesulfonic acid degradation pathway of Sphingomonas sp. McClean S. Cerniglia CE (1997) Reduction of malchite green to leucomalachite green by intestinal bacteria. Gasser F. University of Ulster. Kulla HG. Esteves S. the enzyme initiating azo dye degradation by Pseudomonas KF46. Eur J Biochem 129:197– 203 Zimmermann T. Hirai M. Appl Environ Microbiol 58: 3598–3604 Pointing SB. DNA Sequence 11:51–60 Reddy CA (1995) The potential for white-rot fungi in the treatment of pollutants. Leisinger T (1982) Properties of purified orange II azoreductase. Singh D. Appl Environ Microbiol 66:1754–1758 Swamy J. which decolorizes various dyes. Biotechnol Lett 18:527–528 Pasti MB. pp 92–100 . Croan S. Enz Microbiol Technol 24:48–53 Zhou W. Biodegradation 8:379–385 Zhang F-M. Banat IM. Fritsche W (1997) Transformation of difluorinated phenols by Penicillium frequentans Bi 7/2. Marchant R.D. Rau R. Biores Technol 74:179–179 O’Neill C. Marchant R (1996) Decolourisation and metabolism of the reactive textile dye Remazol Black B. Dartsch PC (1999) Azo dyes and carcinogenic aromatic amines in cell culture. nov. Appl Environ Microbiol 63:4099–4101 Hildenbrand S. Ph. Pinheiro HM. J Ferment Bioeng 79:601–607 Kirby N (1999) Bioremediation of textile industry wastewater by white-rot fungi. Stolz A (1997) Localization of the enzyme system involved in the anaerobic reduction of azo dyes by Sphingomonas sp. In: Leisinger T. Ishikawa K. Vrijmoed LLP (2000) Dye decolorization by sub-tropical basidiomycetous fungi and the effect of metals on decolorizing ability. Keck A. thesis. Crawford DL (2000) Isolation and analysis of three peroxide sensor regulatory gene homologs ahpC. Appl Environ Microbiol 63:3691–3694 Linko S (1988) Production and characterization of extracellular lignin peroxidase from immobilized Phanerochaete chrysosporium in a 10-l bioreactor. Appl Environ Microbiol 63:3684– 3690 Kim SJ. discharge consents and simulation: a review. UK Kirby N. Crawford DL (1992) Mineralization of sulfonated azo dyes and sulfanilic acid by Phanerochaete chrysosporium and Streptomyces chromofuscus. by an immobilized microbial consortium. Smyth WF. Farrel RL (1986) Production of multiple ligninases by Phanerochaete chrysosporium: effect of selected growth conditions and use of a mutant strain. Tapley KN (1999) Development of bioreactor systems for decolorization of Orange II using white rot fungus. Shoda M (1995) Characteristics of a newly isolated fungus. Denner EBM. J Chromatogr A 854:259–274 Stahl JD. Goszczynski S. Knackmuss HJ. Marchant R (2000) Biological decolorization of textile dyestuff by Coriolus versicolor in a packed column reactor.D. Academic. Nuesch J (eds) Microbial degradation of xenobiotic and recalcitrant compounds. Schmahl FW. Hutter R. Heinze TM. Kulla HG. Shoda M (1998) Decolorization of molasses by a new isolate of Geotrichum candidum in a jar fermentor. Wilcox S (2000) Azo-dye degradation in an anaerobic-aerobic treatment system operating on simulated textile effluent. Lourenco ND. Appl Environ Microbiol 65:1029– 1035 Kim SJ. Appl Microbiol Biotechnol 53:249–254 Oxspring DA. Banat I. O’Kane E. Microbiol. Hawkes FR. Magnuson TS. Kreisel G. Int J Syst Evol Microbiol 50:35– 41 Sugano Y. VCH. Schmidt-Maag C. Kampfer P (2000) Description of Sphingomonas xenophaga sp. Molitoris HP (1995) Involvment of an extracellular H2O2-dependent ligninolytic activity of the white rot fungus Pleurotus ostreatus in the decolourisation of Remazol Brilliant Blue R. McHale AP. Appl. Hofrichter M. Biochem Biophys Res Commun 192:477–482 Stolz A. Schmitt TC. Ramsay JA (1999) The evaluation of white rot fungi in the decoloration of textile dyes. Aust SD (1993) Metabolism and detoxification of TNT by Phanerochaete chrysosporium.87 Henderson AL. Busse HJ. Pasti-Grigsby MB. Enz Microbiol Technol 24:130–137 Vyas BRM. McMullan G (2000) Decolourisation of synthetic textile dyes by Phlebia tremellosa. Geotrichum candidum Dec 1. strain BN6 and effect of artificial redox mediators on the rate of azo dye reduction. Murtagh KE. Environ Technol 21:231–236 Keck A. Can J Microbiol 37:902–907 Paszczynrki A. Shoda M (1999b) Purification and characterization of a novel peroxidase from Geotrichum candidum Dec 1 involved in decolorization of dyes. Crawford RL. Stolz A (2000) The function of cytoplasmic flavin reductases in the reduction of azo dyes by bacteria. thesis. Crawford DL (1991) Relationships between the abilities of streptomycetes to decolorize three anthron-type dyes and to degrade lignocellulose. Bucher VVC. London. New York. Delée W (1999) Colour in textile effluents – sources. of Geotrichum candidum Dec 1. Egli T. DyP. World J Microbiol Biotechnol 16:199–205 Ramachandran S. Kimmel R.