Production of extracellular enzymes during the solubilisation of straw by Thermomonospora fusca BD25

Trigo, C.; Ball, Andrew S.

doi:10.1007/bf00221233

Cited by 28 publications

(9 citation statements)

References 29 publications

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“…Our results show that the transformation of glyphosate to AMPA in soil can also be explained by the activity of enzymes such as MnP and laccase from white rot fungi. In addition, several actinomycetes, notably streptomycetes, are able to produce extracellular peroxidases involved in degradation of lignocelluloses (Arias et al 2003;Trigo and Ball 1994;Tuncer et al 2004). As common soil-dwelling microorganisms (Goodfellow and Williams 1983), their contribution to the degradation of glyphosate may thus also be important.…”

Section: Discussionmentioning

confidence: 99%

Degradation of glyphosate and other pesticides by ligninolytic enzymes

2009

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The ability of pure manganese peroxidase (MnP), laccase, lignin peroxidase (LiP) and horseradish peroxidase (HRP) to degrade the widely used herbicide glyphosate and other pesticides was studied in separate in vitro assays with addition of different mediators. Complete degradation of glyphosate was obtained with MnP, MnSO4 and Tween 80, with or without H2O2. In the presence of MnSO4, with or without H(2)O(2), MnP also transformed the herbicide, but to a lower rate. Laccase degraded glyphosate in the presence of (a) 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS), (b) MnSO(4) and Tween 80 and (c) ABTS, MnSO4 and Tween 80. The metabolite AMPA was detected in all cases where degradation of glyphosate occurred and was not degraded. The LiP was tested alone or with MnSO4, Tween 80, veratryl alcohol or H2O2 and in the HRP assay the enzyme was added alone or with H2O2 in the reaction mixture. However, these enzymes did not degrade glyphosate. Further experiments using MnP together with MnSO4 and Tween 80 showed that the enzyme was also able to degrade glyphosate in its commercial formulation Roundup Bio. The same enzyme mixture was tested for degradation of 22 other pesticides and degradation products present in a mixture and all the compounds were transformed, with degradation percentages ranging between 20 and 100%. Our results highlight the potential of ligninolytic enzymes to degrade pesticides. Moreover, they suggest that the formation of AMPA, the main metabolite of glyphosate degradation found in soils, can be a result of the activity of lignin-degrading enzymes.

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Section: Discussionmentioning

confidence: 99%

Degradation of glyphosate and other pesticides by ligninolytic enzymes

2009

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“…The production of extracellular peroxidases is a common trait amongst actinomycetes [21]. The role of these enzymes in the degradation of lignin has yet to be established.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a novel non-haem-containing extracellular peroxidase from Thermomonospora fusca

Ball

Trigo

1995

Biochemical Society Transactions

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“…Another group of organisms in which extracellular peroxidases have been identified are actinobacteria (Ball and Trigo, 1995;Mercer et al, 1996;Rob et al, 1996;Kang et al, 1999;Tuncer et al, 2004). Degradation of lignin and lignin-degrading enzymes has also been reported for actinobacteria, mainly from the Thermomonospora fusca BD25 (Trigo and Ball, 1994;Ball and Trigo, 1995;Rob et al, 1996), Streptomyces avermitilis UAH30 (Rob et al, 1997), Streptomyces albus ATCC 3005 (Antonopoluos et al, 2001), Streptomyces sp. UAH47 (Hernandez et al, 2001), and Streptomyces sp.…”

Section: Introductionmentioning

confidence: 94%

“…The extracellular endo-xylanases, cellulases, and peroxidases produced by actinobacteria, generally exhibit a pH optima between 5.0 and 8.0 (McCarthy et al, 1985;Wilson, 1992;Trigo and Ball, 1994). Optimum pH for peroxidase activity produced by Streptomyces sp.…”

Section: Fig 3 -The Effect Of Cultivation Ph (A) and Temperature (B)mentioning

confidence: 99%

Production and partial characterization of extracellular peroxidase produced byStreptomyces sp. F6616 isolated in Turkey

et al. 2009

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-Streptomyces sp. F6616 was found to produce higher levels of extracellular peroxidase activity (0.535 U/ mL) without any inducers than other actinobacteria which are previously reported. Maximum specific peroxidase activity (6.21 U/mg of protein) was obtained after 72 h of incubation at 30 °C in a minimal salt medium (pH 8.0) containing (in wt/v) 0.6% yeast extract and 0.8% ball-milled wheat straw corresponding to a C:N ratio of 4.6:1. Characterization of the peroxidase revealed that the optimal temperature for the enzyme activity, using the standard 2,4-dichlorophenol (2,4-DCP) assay was 50 °C, when the enzyme reaction was performed at pH 8.0. A study of the effect of temperature on the stability of peroxidase over time, showed that the enzyme was stable at 50 °C, with a half-life of 145 min, while at higher temperature the stability and activity was reduced such that at 60 °C the half-life of the enzyme was 30 min. The optimum pH for the activity of the enzyme occurred between pH 9.0 and 10.0. The apparent K m and V max values for the peroxidase preparations were determined to be 1.52 mmol/L and 1.84 U/mg protein, respectively using 2,4-DCP as a substrate. Characterization of the peroxidase activity revealed activity against 2,4-DCP, L-3,4-dihydroxyphenylalanine (L-DOPA), 2,4,5-trichlorophenol and other chlorophenols in the presence of hydrogen peroxide. However, inhibition of peroxidase activity with the addition of potassium cyanide and sodium azide, suggested the presence of heme component in the tertiary structure of the enzyme.

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Production of extracellular enzymes during the solubilisation of straw by Thermomonospora fusca BD25

Cited by 28 publications

References 29 publications

Degradation of glyphosate and other pesticides by ligninolytic enzymes

Degradation of glyphosate and other pesticides by ligninolytic enzymes

Characterization of a novel non-haem-containing extracellular peroxidase from Thermomonospora fusca

Production and partial characterization of extracellular peroxidase produced byStreptomyces sp. F6616 isolated in Turkey

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