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1.
PLoS One ; 9(2): e89108, 2014.
Article in English | MEDLINE | ID: mdl-24551229

ABSTRACT

While it is known that several Actinobacteria produce enzymes that decompose polysaccharides or phenolic compounds in dead plant biomass, the occurrence of these traits in the environment remains largely unclear. The aim of this work was to screen isolated actinobacterial strains to explore their ability to produce extracellular enzymes that participate in the degradation of polysaccharides and their ability to cometabolically transform phenolic compounds of various complexities. Actinobacterial strains were isolated from meadow and forest soils and screened for their ability to grow on lignocellulose. The potential to transform (14)C-labelled phenolic substrates (dehydrogenation polymer (DHP), lignin and catechol) and to produce a range of extracellular, hydrolytic enzymes was investigated in three strains of Streptomyces spp. that possessed high lignocellulose degrading activity. Isolated strains showed high variation in their ability to produce cellulose- and hemicellulose-degrading enzymes and were able to mineralise up to 1.1% and to solubilise up to 4% of poplar lignin and to mineralise up to 11.4% and to solubilise up to 64% of catechol, while only minimal mineralisation of DHP was observed. The results confirm the potential importance of Actinobacteria in lignocellulose degradation, although it is likely that the decomposition of biopolymers is limited to strains that represent only a minor portion of the entire community, while the range of simple, carbon-containing compounds that serve as sources for actinobacterial growth is relatively wide.


Subject(s)
Bacterial Proteins/biosynthesis , Catechols/metabolism , Cellulose/metabolism , Lignin/metabolism , Soil Microbiology , Streptomyces/enzymology , Biodegradation, Environmental , Biomass , Carbon Radioisotopes , Cellulose 1,4-beta-Cellobiosidase/biosynthesis , Hydrolysis , Kinetics , Populus/chemistry , Streptomyces/isolation & purification , Trees/chemistry , Xylosidases/biosynthesis , beta-Glucosidase/biosynthesis
2.
Appl Environ Microbiol ; 68(7): 3442-8, 2002 Jul.
Article in English | MEDLINE | ID: mdl-12089026

ABSTRACT

The basidiomycete Collybia dryophila K209, which colonizes forest soil, was found to decompose a natural humic acid isolated from pine-forest litter (LHA) and a synthetic (14)C-labeled humic acid ((14)C-HA) prepared from [U-(14)C]catechol in liquid culture. Degradation resulted in the formation of polar, lower-molecular-mass fulvic acid (FA) and carbon dioxide. HA decomposition was considerably enhanced in the presence of Mn(2+) (200 microM), leading to 75% conversion of LHA and 50% mineralization of (14)C-HA (compared to 60% and 20%, respectively, in the absence of Mn(2+)). There was a strong indication that manganese peroxidase (MnP), the production of which was noticeably increased in Mn(2+)-supplemented cultures, was responsible for this effect. The enzyme was produced as a single protein with a pI of 4.7 and a molecular mass of 44 kDa. During solid-state cultivation, C. dryophila released substantial amounts of water-soluble FA (predominantly of 0.9 kDa molecular mass) from insoluble litter material. The results indicate that basidiomycetes such as C. dryophila which colonize forest litter and soil are involved in humus turnover by their recycling of high-molecular-mass humic substances. Extracellular MnP seems to be a key enzyme in the conversion process.


Subject(s)
Basidiomycota/metabolism , Humic Substances/metabolism , Pinus/chemistry , Basidiomycota/physiology , Carbon Radioisotopes , Peroxidases/isolation & purification , Peroxidases/metabolism , Pinus/metabolism , Plant Leaves/chemistry , Plant Leaves/metabolism
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