10 1 Full Volume (PDF)(jcmb.halic.edu.tr) - Journal of Cell and ...

More documents

Recommendations

Info

Journal of Cell and Molecular Biology <strong>10</strong>(1): 1-11, 2012 Review Article 1 Haliç University, Printed in Turkey. http://<strong>jcmb</strong>.<strong>halic</strong>.<strong>edu</strong>.tr Production and industrial applications of laccase enzyme Muhammad IMRAN *1,2 , Muhammad J. ASAD 1 , Saqib H. HADRI 1 and Sajid MEHMOOD 2 1 Department of Biochemistry, Pir Mehr Ali Shah Arid Agriculture University, Rawalpindi, Pakistan 2 Department of Biochemistry and Biotechnology, University of Gujrat, Pakistan (* author for correspondence; mirzaimran42@gmail.com) Received: 22 April 2011; Accepted: 15 May 2012 Abstract Laccase is an enzyme that has potential ability of oxidation. It belongs to those enzymes, which have innate properties of reactive radical production, and its utilization in many fields has been ignored because of its unavailability in the commercial field. There are diverse sources of laccase producing organisms like bacteria, fungi and plants. Textile, pulp and paper industries discharge a huge quantity of waste in the environment, and the disposal of this waste is a big problem. To solve this problem, work has done to discover such an enzyme, which can detoxify these wastes and is not harmful to the environment. Laccases use oxygen and produce water as by product. They can degrade a range of compounds including phenolic and non-phenolic compounds. They also have ability to detoxify a range of environmental pollutants. Their property to act on a range of substrates and also to detoxify a range of pollutants have made them to be usable for several purposes in many industries including paper, pulp, textile and petrochemical industries. Keywords: Laccase, solid state fermentation, oxidation, enzyme, fungi. Lakkaz enziminin üretimi ve endüstriyel uygulamaları Özet Lakkaz, potansiyel oksidasyon yeteneği olan bir enzimdir. Reaktif radikal üretim özelliği olan enzimlere dahildir ve birçok alandaki kullanımı, ticari alanda uygun olmaması nedeniyle göz ardı edilmektedir. Bakteri, mantar ve bitki gibi lakkaz üreten çeşitli organizma kaynakları vardır. Tekstil, kağıt hamuru ve kağıt endüstrisi çevreye büyük miktarda atık salmaktadır ve bu atıkların uzaklaştırılması büyük bir problemdir. Bu sorunu çözmek üzere, atıkları detoksifiye eden ve çevreye zararlı olmayan bir enzim keşfetmek için çalışmalar yapılmıştır. Bu enzim oksijen kullanır ve yan ürün olarak su üretir. Lakkaz, fenolik ve fenolik olamayan bileşikleri içeren bir dizi bileşiği parçalayabilir. Ayrıca, bir dizi çevresel kirleticiyi detoksifiye etme yeteneği vardır. Çeşitli substratlar üzerine etki etme ve ayrıca bir dizi kirliliği detoksifiye etme özelliği, bu enzimleri çeşitli amaçlarla tekstil, kâğıt hamuru, kâğıt ve petrokimya endüstrisini kapsayan birçok endüstride kullanılabilir kılmaktadır. Anahtar kelimeler: Lakkaz, katı hal fermentasyonu, oksidasyon, enzim, mantarlar. Introduction Laccase was first discovered in the sap of the Japanese lacquer tree Rhus vernicifera, and its characteristic as a metal containing oxidase was discovered by Bertrand in 1985 (Giardina et al., 20<strong>10</strong>). Since then, laccases have also been found in various basidiomycetous and ascomycetous fungi and thus far fungal laccases have accounted for the most important group of multicopper oxidases (MCOs) with respect to number and extent of characterization (Giardina et al., 20<strong>10</strong>). The large quantity of laccases have been widely reported inside white-rot fungi. A number of
2Muhammad IMRAN et al. laccase genes have been isolated and distinguished for this purpose (Mayer and Staples, 2002). The improvement in laccase appearance, characterized by an increase in protein and mRNA level, was illustrated with Picnoprus cinnabarinus, Pleurotus sajor caju and Trametes versicolor (Eggert et al. 1996, Solden and Dobson 2001, Collins and Dobson 1997). A number of species of genus Pleurotus have been explained as manufacturers of laccase (Leonowicz et al. 2001). We freshly reported that a strain of P. pulmonarius produce laccase as the main ligninolytic enzymes while cultured on wheat bran solid state medium (Souza et al. 2002). In the current study, numerous phenolic and aromatic compounds structurally related to lignin were calculated for their capability to arouse laccase production by P. pulmonarius. (Solden and Dobson, 2001). P. pulmonarius was proficient of mounting on a wide variety of phenolic and aromatic compounds. Laccase production by P. pulmonarius could be considerably improved by including an equimolar combination of ferulic acid and vanillin as inducer. The construction of different laccase isoform in reply to phenolics implicates a possible task of this enzyme in the detoxification processes (Souza et al., 2002) Numerous white-rot fungi, counting Trametes versicolor, make extra cellular copper-containing phenol oxidases (E C 1.<strong>10</strong>.3.2), named laccases (Birhanli and Yesilada, 2006). The two major likely natural functions attributed to fungal laccases are, first, their participation in lignin degradation, mutually with supplementary ligninolytic enzymes such as peroxidases, and second, their function in fungal virulence as key cause in pathogenesis in opposition to plant hosts (Gianfreda et al., 1999). As well, laccases display in vivo other functions that are the foundation of several industrial applications. For instance, in Aspergillus nidulans, laccases take action on pigment development in fungal spores (Smith et al., 1997). A number of fungi also ooze laccases to take away either potentially toxic phenols released through lignin degradation or toxins formed by others organisms. As a result, the enzyme has probable applications in the textile industries, dye, as well as for the degradation of a variety of xenobiotics, which are recognized as ecological pollutants (Rama et al. 1998, Jolivalt et al. 1999, Mougin et al., 2000). Laccase-producing fungi have also been reported to be helpful apparatus for xenobiotic removal in liquid effluents as well as in soil bioremediation (Gianfreda et al. 1999, Jolivalt et al. 2000). Our outcomes demonstrate that the resulting alteration products themselves are likely to encourage biological effects moreover on degrading or non-target organisms. So, an entire characterization of these compounds is essential for an entire assessment of the remediation processes (Souza et al., 2002). Laccase represents a family of coppercontaining polyphenol oxidases (PPO) & are usually called multicopper oxidases (MCO) (Birhanli and Yesilada, 2006; Arora and Sharma, 20<strong>10</strong>; Giardina et al., 20<strong>10</strong>). Laccases catalyze the oxidation of various substituted phenolic compounds by using molecular oxygen as the electron acceptor (Sharma et al., 2007). These enzymes have less substrate specificity and have the ability to degrade a range of xenobiotics including industrial colored wastewaters (Souza et al., 2006). Laccases exhibit broad substrate range, which varies from one laccase to another. Although it is known to be diphenol oxidase, monophenols like 2, 6-dimethoxy phenol or guaiacol are better substrates than phenols (e.g., catechol or hydroquinone) (Baldrian, 2006; Arora and Sharma, 20<strong>10</strong>). Laccases catalyze monoelectronic oxidation of molecules to corresponding reactive radicals with the help of four copper atoms, which form the main catalytic core of the laccase, accompanied with the diminution of oxygen to water molecules and simultaneous oxidation of substrate to produce radicals (Arora and Sharma, 20<strong>10</strong>). All substrates cannot be directly oxidized by laccases, either because of their large size which restricts their penetration into the enzyme active site or because of their particular high redox potential. To overcome this hindrance, suitable chemical mediators are used which are oxidized by the laccase and their oxidized forms are then able to interact with high redox potential substrate targets (Arora and Sharma, 20<strong>10</strong>). In fungi, laccases carry out a variety of physiological roles including morphogenesis, fungal plant pathogen/host interaction, stress defense, and lignin degradation (Gianfreda et al., 1999; Giardina et al., 20<strong>10</strong>). Laccases have been found in nearly all woodrotting fungi analyzed so far (Heinzkill and Messner, 1997; Giardina et al., 20<strong>10</strong>) and are almost ubiquitary enzymes as they have been isolated from plants, from some kinds of bacteria, and from insects too (Enguita et al., 2003; Sharma et al., 2007; Giardina et al., 20<strong>10</strong>).
Page 1 and 2: Journal of Cell and Molecular Biolo
Page 3 and 4: Haliç University Faculty of Arts a
Page 8 and 9: Laccase has many applications in ot
Page 10 and 11: dimethoxyphenol (2, 6-DMP). Kinetic
Page 12 and 13: pharmaceutical importance that has
Page 14 and 15: Gianfreda L, Xu F, Bollag JM. Lacca
Page 16: isoforms by Pleurotus pulmonarius i
Page 19 and 20: 14 Tasnim FARASAT et al. practicing
Page 21 and 22: 16 Tasnim FARASAT et al. Figure 2.
Page 23 and 24: 18 Tasnim FARASAT et al. Noronha M,
Page 25 and 26: 20 Alexander V. ATAMAN et al. Intro
Page 27 and 28: 22 Alexander V. ATAMAN et al. Table
Page 29 and 30: 24 Alexander V. ATAMAN et al. In so
Page 31 and 32: 26 Alexander V. ATAMAN et al. Matar
Page 33 and 34: 28 Engin AYNACI et al. Giriş Akci
Page 35 and 36: 30 Engin AYNACI et al. Tablo 2. Ha
Page 37 and 38: 32 Engin AYNACI et al. Yang X, Xion
Page 39 and 40: 34Ragini SHARMA et al. Introduction
Page 41 and 42: 36Ragini SHARMA et al. lymphocytes
Page 43 and 44: 38Ragini SHARMA et al. Discussion C
Page 45 and 46: 40Ragini SHARMA et al. Kosnett. Glo
Page 47 and 48: 42 Raziye MOHAMMADPOUR et al. Intro
Page 49 and 50: 44 Raziye MOHAMMADPOUR et al. Table
Page 51 and 52: 46 Raziye MOHAMMADPOUR et al. Figur
Page 53 and 54: 48 Raziye MOHAMMADPOUR et al. Caspa
Page 55 and 56:
50 Raziye MOHAMMADPOUR et al. Figur
Page 57 and 58:
52 Raziye MOHAMMADPOUR et al. promo
Page 59 and 60:
54 Raziye MOHAMMADPOUR et al. the c
Page 61 and 62:
56 Muhammad IRFAN et al. Introducti
Page 63 and 64:
58 Muhammad IRFAN et al. Effect of
Page 65 and 66:
60 Muhammad IRFAN et al. Figure 5.
Page 67 and 68:
62 Muhammad IRFAN et al. Figure 9.
Page 69 and 70:
64 Muhammad IRFAN et al. Nimkar MD,
Page 71 and 72:
66 Abstract: A brief, informative a
Page 73 and 74:
68 may ask one referee to comment o
show all

10 1 Full Volume (PDF)(jcmb.halic.edu.tr) - Journal of Cell and ...

Create successful ePaper yourself

Delete template?

Save as template?