Enhanced expression of a recombinant bacterial laccase at low temperature and microaerobic conditions: purification and biochemical characterization

Mohammadian, Mahdi; Fathi‐Roudsari, Mehrnoosh; Mollania, Nasrin; Badoei-dalfard, Arastoo; Khajeh, Khosro

doi:10.1007/s10295-010-0734-5

Cited by 81 publications

(65 citation statements)

References 36 publications

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“…HR03 has been determined [14]. Niladevi et al [24] have found that an unusual halotolerant-alkaline laccase from Streptomyces psammoticus has a molecular mass of about 43 kDa and recently Mohammadian et al [25] determined a molecular weight of 65 kDa for a laccase from Bacillus sp. HR03.…”

Section: Discussionmentioning

confidence: 99%

The Determination of Assay for Laccase of Bacillus subtilis WPI with Two Classes of Chemical Compounds as Substrates

et al. 2012

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Ligninolytic enzyme complexes are involved in lignin degradation. Among them laccases are outstanding because they use molecular oxygen as a co-substrate instead of hydrogen peroxide as used by peroxidases. Bacterial laccase of Bacillus genus was first reported in Claus and Filip (Microbiol Res 152:209-216, 1997), since then more bacterial laccases have been found. In this research, laccase-producing bacteria were screened from pulp and paper industry wastewater, bagass and sugarcane rhizosphere. Nutrient agar medium containing 0.5 mM of guaiacol was used. It was observed that the laccase-producing strains developed brown colour from which 16 strains of Bacillus were identified. One of the isolated strains was identified as Bacillus subtilis WPI based on the results of biochemical tests and 16S rDNA sequence analysis. This strain showed laccase-like activity towards the oxidizing substrates ABTS and guaiacol. In this study guaiacol was used as the substrate of laccase activity assay. For determination of laccase activity of this isolate guaiacol was used as a substrate of assay for the first time in this study. SDS-PAGE and Native-PAGE confirmed the presence of laccase.

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Section: Discussionmentioning

confidence: 99%

The Determination of Assay for Laccase of Bacillus subtilis WPI with Two Classes of Chemical Compounds as Substrates

et al. 2012

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“…Table 1 summarizes the kinetic parameters obtained for six different BODs at their optimum pH (Durand et al 2012a, b;Durao et al 2008;Kataoka et al 2005b;Koschorreck et al 2008;Mohammadian et al 2010). Insight from crystals structures combined with molecular modelling would be desirable, in order to elucidate the obvious differences among BODs in substrate affinities (Table 1).…”

Section: Biochemical Characterizationmentioning

confidence: 97%

“…The conjugated form results from the transformation of the unconjugated bilirubin in the liver by the enzyme hepatic glucuronyl transferase. The detection of unconjugated bilirubin is more specifically used in newborns where the liver is not mature enough to convert the unconjugated bilirubin to conjugated bilirubin resulting in jaundice affecting~60-80 % of newborns (Goldfinch and Maguire 1988;Kirk 2008; Table 1 Comparison between the kinetics parameters of the BOD from B. pumilus (Durand et al 2012b), B. licheniformis (Koschorreck et al 2008), Bacillus HR03 (Mohammadian et al 2010), B. subtilis (Durao et al 2008), M. verrucaria (Kataoka et al 2005b) and M. oryzae (Durand et al 2012a Mullon et al 1989;Nakamura and Lee 1977). Conjugated bilirubin is known to be a better indicator of liver function and is used in the diagnosis of jaundice and hyperbilirubinemia (Doumas et al 1987(Doumas et al , 1999Kirihigashi et al 2000;Kosaka et al 1987Kosaka et al , 1998Million et al 1988;Mullon and Langer 1987;Perry et al 1986;Soltys et al 1992).…”

Section: Bilirubin and Medical Sensorsmentioning

confidence: 99%

Features and applications of bilirubin oxidases

Mano

2012

Appl Microbiol Biotechnol

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Discovered in 1981 by Tanaka and Murao (Agric Biol Chem 45:2383-2384, 1981), bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu(+/2+) ions. It catalyzes the oxidation of bilirubin to biliverdin, hence the classification of bilirubin oxidase, and has been primarily used in the determination of bilirubin in serum and thereby in the diagnostic of jaundice. Unlike laccases, the most studied MCOs, BODs display a high activity and stability at neutral pH, a high tolerance towards chloride anions and other chelators, and for some species, a high thermal tolerance. Therefore, BODs could potentially be an alternative to laccase which are so far mainly restricted to applications in acid media. Because of growing interest in BODs for numerous applications under mild pH conditions, based on the number of patents and publications published in the last 5 years, here I will summarize the available data on the biochemical properties of BODs, their occurrence, and their possible biotechnological use in (1) the field of Healthcare for the elaboration of biofuel cells or bilirubin sensors or (2) the field of environmentally desirable applications such as depollution, decolorization of dyes, and pulp bleaching.

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“…The purified laccase showed the lowest K m values (31.2 μ M ) for oxidizing ABTS when compared to the other tested substrates, and the K m value was also significantly lower than other Bacillus strains, which fell in the range of 44-1,404 μ M [Lu et al, 2013;Mohammadian et al, 2010;Sondhi et al, 2014], indicating that the laccase from Bacillus sp. A4 has a much higher affinity for ABTS substrate.…”

Section: Discussionmentioning

confidence: 99%

Overexpression of a Laccase with Dye Decolorization Activity from Bacillus sp. Induced in Escherichia coli

Guo

Zheng²,

Jiang³

et al. 2017

Microb Physiol

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Laccases from bacteria have been widely studied in the past 2 decades due to the higher growth rate of bacteria and their excellent thermal and alkaline pH stability. In this study, a novel laccase gene was cloned from Bacillus sp., analyzed, and functionally expressed in Escherichia coli. The laccase was highly induced in the E. coli expression system with a maximum intracellular activity of 16 U mg^-1 protein. The optimal temperature and pH of the purified laccase were 40°C and 4.6, respectively, when ABTS (2,2'-azino-bis[3-ethylbenzothiazoline-6-sulfonate]) was used as the substrate. The purified laccase showed high stability in the pH range of 3.0-9.0, and retained more than 70% of its activity after 24 h of incubation at 40°C with a pH value of 9.0. Furthermore, the enzyme exhibited extremely high temperature and ion metal tolerance. The half-life of the purified laccase at 70°C was 15.9 h. The purified laccase could efficiently decolorize 3 chemical dyes, especially in the presence of ABTS as a mediator. The high production of this laccase in E. coli and exceptional characteristics of the recombinant enzyme protein make it a promising candidate for industrial applications.

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Enhanced expression of a recombinant bacterial laccase at low temperature and microaerobic conditions: purification and biochemical characterization

Cited by 81 publications

References 36 publications

The Determination of Assay for Laccase of Bacillus subtilis WPI with Two Classes of Chemical Compounds as Substrates

The Determination of Assay for Laccase of Bacillus subtilis WPI with Two Classes of Chemical Compounds as Substrates

Features and applications of bilirubin oxidases

Overexpression of a Laccase with Dye Decolorization Activity from <b><i>Bacillus</i></b> sp. Induced in <b><i>Escherichia coli</i></b>

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