Biotechnol Rep (Amst). 2017 Jan 03;13:49-57. doi: 10.1016/j.btre.2016.12.005. eCollection 2017 Mar.
A valuable peroxidase activity from the novel species .
Biotechnology reports (Amsterdam, Netherlands)
Carmine Casciello, Fabio Tonin, Francesca Berini, Elisa Fasoli, Flavia Marinelli, Loredano Pollegioni, Elena Rosini
Affiliations
Affiliations
- Department of Biotechnology and Life Sciences, University of Insubria, via J.H. Dunant 3, 21100 Varese, Italy; The Protein Factory Research Center, Politecnico of Milano and University of Insubria, via Mancinelli 7, 20131 Milano, Italy.
- Department of Chemistry, Materials and Chemical Engineering "Giulio Natta", Politecnico of Milano, via Mancinelli 7, 20131, Milano, Italy.
PMID: 28352563
PMCID: PMC5361131 DOI: 10.1016/j.btre.2016.12.005
Abstract
Degradation of lignin constitutes a key step in processing biomass to become useful monomers but it remains challenging. Compared to fungi, bacteria are much less characterized with respect to their lignin metabolism, although it is reported that many soil bacteria, especially actinomycetes, attack and solubilize lignin. In this work, we screened 43 filamentous actinomycetes by assaying their activity on chemically different substrates including a soluble and semi-degraded lignin derivative (known as alkali lignin or Kraft lignin), and we discovered a novel and valuable peroxidase activity produced by the recently classified actinomycete
Keywords: 2,4-DCP, 2,4-dichlorophenol; 2,6-DMP, 2,6-dimethoxyphenol; ABTS, 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid); Alkali lignin; DyP, dye decolorizing peroxidase; Filamentous actinomycetes; Kraft lignin; LiP, lignin peroxidase; MAM, mannitol agar medium; MM-L, minimal salt medium plus lignin; MnP, manganese peroxidase; Nonomuraea gerenzanensis; Peroxidases; RB5, reactive black 5; RBBR, remazol brilliant blue R; VP, versatile peroxidase
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