ABSTRACT
Contamination with harmful chemical substances, including organic compounds of the BTEX and PAH groups, constitutes one of the major threats to the functioning of soil habitat. Excessive contents of the above substances can exert adverse effects on soil organisms, reduce biodiversity, and thus deteriorate soil quality. The threat to soil ecosystems within areas particularly exposed to contamination with accumulating chemical compounds was assessed using the Ecological Risk Assessment (ERA) with a multi-stage Triad (triage rapid initial assessment) procedure (taking into account the different lines of evidence). The article presents the results of chemical and ecotoxicological study of soils sampled at sites affected by contamination from petrochemical industry. The study results provided foundations for developing the site specific ERA framework for the area examined.
Subject(s)
Petroleum Pollution/analysis , Plant Development/drug effects , Soil Pollutants/analysis , Soil Pollutants/toxicity , Chromatography, Gas , Ecotoxicology , Mass Spectrometry , Poland , Polycyclic Aromatic Hydrocarbons/analysis , Polycyclic Aromatic Hydrocarbons/toxicity , Principal Component Analysis , Risk Assessment , Volatile Organic Compounds/analysis , Volatile Organic Compounds/toxicityABSTRACT
An intracellular aminopeptidase N synthesized by Pseudomonas putida Lup was purified and characterized. The approx. 150-fold purified enzyme showed highest activity against A-beta-naphthylamide at pH 7.5 and at temperature 40 degrees C and was 100% thermostable for 240 min at 40 degrees C. P putida lup aminopeptidase N is a monomer with molecular mass approx. 99 kDa determined by SDS-PAGE and gel permeation chromatography. The enzyme has broad substrate specificity, but is the most active against protein substrates with N-terminal alanine and arginine. The activity of P. putida Lup aminopeptidase N is strongly inhibited in the presence of specific metallopeptidase inhibitors and is partly recovered in the presence of Zn2+ and Co2+ ions. Co2+, Mg2+ and Ca2+ ions increased the activity of the enzyme. Moreover, the enzyme was inhibited by inhibitors of cysteine enzymes. Analysis of fragments of the amino acid sequence of the purified enzyme demonstrated high similarity to PepN of Pseudomonas putida GB-1.
