Purification and Partial characterization of manganese peroxidase from Bacillus pumilus AND Paenibacillus sp.

Oliveira, Patrícia Lopes de; Duarte, Marta Cristina Teixeira; Ponezi, Alexandre Nunes; Durrant, Lúcia Regina

doi:10.1590/s1517-83822009000400012

Cited by 59 publications

(28 citation statements)

References 7 publications

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“…Lower optimum temperatures of 25˚C and 35˚C have been reported for POXs from B. pumilus and Paenibacillus sp. [22] while POX from Loweporus lividus MTCC-1178 was optimally active at 24˚C [29]. The difference in optimum temperature of the POXs under study could be related to some structural differences in the total peroxidases.…”

Section: Effect Of Temperature On Total Pox Activity and Stabilitymentioning

confidence: 91%

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Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Olajuyigbe¹,

Ehiosun²,

Jaiyesimi³

2015

AER

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Peroxidases (POXs) are the key extracellular enzymes produced by crude oil degrading microbes. Knowledge of optimum conditions for POXs activity is crucial for providing effective environment for bioremediation. In this study, physicochemical properties of POXs produced by Actinomyces israelii and Actinomyces viscosus during growth on crude oil were studied. The POXs exhibited similarities in activity and stability with striking differences in response to two divalent metal ions. The POXs from both species had optimum pH of 7.0 and were very stable over a narrow pH range (6.0 -8.0). The POXs demonstrated similar thermostability exhibiting relative residual activity of 62% at 50˚C after 30 min incubation and 45% residual activity at the same temperature after 60 min despite the fact that POXs from A. viscosus and A. israelii had optimum temperatures of 50˚C and 40˚C, respectively. The POXs from A. viscosus and A. israelii were greatly activated by Fe 2+ at 5.0 and 10.0 mM. The enzymes were both strongly inhibited by Cu 2+ , Mg 2+ and Hg 2+ . Surprisingly, these congeneric POXs demonstrated striking differences in their response to Ca 2+ and Mn 2+ . POX from A. viscosus was activated by Ca 2+ and Mn 2+ exhibiting relative activity of 136% and 106% at 5 mM, respectively. In contrast, POX from A. israelii was strongly inhibited by Ca 2+ and Mn 2+ exhibiting 62.5% relative activity in the presence of 5 mM of each metal ion. Increasing the concentration of Ca 2+ and Mn 2+ led to further activation of POX from A. viscosus and inhibition of POX from A. israelii. Results provide deeper insights into functional properties of studied POXs from closely related microbes. The physicochemical properties are very similar; however, notable differences provide a strong basis for structural characterization of these congeneric enzymes.

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Section: Effect Of Temperature On Total Pox Activity and Stabilitymentioning

confidence: 91%

“…Some studies have reported optimum pH for POXs from fungi in the range of 4.0 -7.0 [20]- [22] while there are reports showing pH optimum in range of 2.0 -5.0 for fungal POXs [23]- [25]. In contrast, recently reported bacterial POXs from Pseudomonas sp.…”

Section: Effect Of Ph On Total Pox Activity and Stabilitymentioning

confidence: 93%

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Olajuyigbe¹,

Ehiosun²,

Jaiyesimi³

2015

AER

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“…It was stated in a previous report that some of the ligninolytic bacteria isolated from soil are thermophilic strains (Oliveira et al 2009). …”

Section: Bioresourcescommentioning

confidence: 99%

“…Based on the observation, the Lac enzyme activity is low compared to LiP and MnP in all three strains. For effect of pH in the production of lignin degrading enzymes by isolated bacteria, selected pH range from 7.0 to 9.0 were selected according to previous studies of isolated ligninolytic bacteria in Oliveira et al (2009). This report stated that most of ligninolytic bacteria which were isolated from soil positively affected the growth and production of enzymes toward alkaline pH.…”

Section: Production Of Ligninolytic Enzymesmentioning

confidence: 99%

“…In previous studies, most of the isolated ligninolytic bacteria could only produce two main ligninolytic enzymes, especially a combination of MnP and Lac enzyme production (Shi et al 2013;Chen et al 2012 andOliveira et al 2009). Meanwhile, in this study, all three isolated strains produced all three main ligninolytic enzymes: LiP, MnP, and Lac.…”

Section: Bioresourcescommentioning

confidence: 99%

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Production of Ligninolytic Enzymes by Newly Isolated Bacteria from Palm Oil Plantation Soils

Rahman

Aziz

et al. 2013

BioResources

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Three aerobic lignin-degrading bacterial strains were isolated from palm oil plantation soils. The bacterial isolates were screened using a selective nutrient medium of minimum salt media (MSM), with kraft lignin as lignin substrate and methylene blue as the ligninolytic dye indicator. The newly isolated bacterial strains SHC1, SHC2, and SHC3 were found to have the potential to tolerate high concentrations of kraft lignin and produced all three main ligninolytic enzymes (lignin peroxidase, manganese peroxidase, and laccase); these strains may therefore be useful in the degradation of lignin in oil palm empty fruit bunch biomass. The production of ligninolytic enzymes was carried out by means of submerged fermentation for 7 days using 2 mm of oil palm empty fruit bunch (OPEFB) fiber as a substrate. These bacterial isolates were characterized using biochemical tests from Biolog and identified using 16S rRNA gene sequencing analysis, which identified the strains SHC1, SHC2, and SHC3 as Bacillus sp., Ochrobactrum sp., and Leucobacter sp., respectively with 99% sequence similarity. Bacillus sp. SHC1 produced the highest manganese peroxidase (MnP) of 2313.4 U/L on the third day and the highest lignin peroxidase (LiP) of 209.30 U/L on the fifth day of fermentation. The optimum pH and temperature for the production of ligninolytic enzymes by Bacillus sp. SHC1 were pH 8 and 30 °C.

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Biofuels: Fungal, Bacterial and Insect Degraders of Lignocellulose

Sethi

Scharf

2013

Encyclopedia of Life Sciences

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Lignocellulose is the main structural component of plant cell walls and can be degraded into simple sugars with the help of hydrolytic enzymes. Lignocellulose is composed of three polymers: cellulose, hemicellulose and lignin. Certain fungi, bacteria and insects have evolved the ability to degrade lignocellulose. Cellulose is degraded to glucose by the synergistic action of three distinct classes of enzymes: endoglucanases, exoglucanases and β‐glucosidases. Owing to its variable structure and organisation, hemicellulose degradation requires various enzymes with diverse modes of action, which include endoxylanases, endomannanases, β‐xylosidases, β‐mannosidases, β‐galactosidases, α‐glucuronidases, α‐arabinofurnosidases, α‐galactosidases, acetyl xylan esterases, feruloyl esterases and glucuronyl esterases. Lignin degradation is much more difficult due to its complex structure and bonding to carbohydrate complexes. It requires oxidative enzymes, such as lignin peroxidases, manganese peroxidases, versatile peroxidases, laccases, and several other auxiliary enzymes. Commercial biofuel production from lignocellulosic materials can be achieved by artificially producing these cellulases, hemicellulases and lignases in recombinant form. Key Concepts: Lignocellulose is the most abundant renewable resource of energy on the Earth. Lignocellulose is a general term referring to a natural complex of three biopolymers: cellulose, hemicellulose and lignin. Simple sugar can be released from lignocellulose using three categories of enzymes: cellulases, hemicellulase and lignases. Released sugars from lignocellulose can be fermented into biofuel (ethanol). Wood‐rotting fungi such as white‐rot, brown‐rot and soft‐rot fungi can degrade lignocellulose. Aerobic and anaerobic bacteria such as Bacillus, Streptomyces, Cellulomonas and Clostridium possess lignocellulose‐degrading enzymes. Wood and plant‐feeding insects such termites, roaches, longhorn beetles and grasshoppers are rich sources of novel lignocellulases genes. Lignocellulases of fungal, bacterial and insect origin can be artificially/recombinantly produced in various protein expression systems. Fungal, bacterial and insect lignocellulases are expected to play important roles in the development of successful lignocellulose conversion technologies.

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Purification and Partial characterization of manganese peroxidase from Bacillus pumilus AND Paenibacillus sp.

Abstract: The production of manganese peroxidase (MnP) from Bacillus pumilus and Paenibacillus sp.

Cited by 59 publications

References 7 publications

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Production of Ligninolytic Enzymes by Newly Isolated Bacteria from Palm Oil Plantation Soils

Biofuels: Fungal, Bacterial and Insect Degraders of Lignocellulose

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