Diuron degradation by Phanerochaete chrysosporium BKM- F-1767 in synthetic and natural media

When incubated in synthetic (N-limited) medium and on ashwood chips, Phanerochaete chrysosporium BKM-F-1767 degraded 14 and 10 mg/l diuron, respectively. The wood chips were used as support and sole nutrient source for the fungus. A higher degradation efficiency was found in ashwood culture as compared to the liquid culture, probably as a result of the synergetic effect of attached fungal growth, presence of limiting-substrate conditions and the microenvironment provided by ashwood, all favorable for production of high extracellular enzyme titres. Diuron degradation occured during the idiophasic growth, in the presence of manganese peroxidase, detected as dominant enzyme in both cultures.     

Susceptibility of fibronectin to degradation by various gram-negative and gram-positive oral micro-organisms

The degradative effects on tritiated human plasma fibronectin (FN) of proteases associated with twenty five Gram-negative (GN) and fifteen Gram-positive (GP) oral microbial isolates were examined. Ninety-two per cent of the GN and 20% of the GP isolates degraded the FN. In the GN group, the degradative effects were greatest for Bacteroides gingivalis and Treponema denticola, while in the GP group Streptococcus faecalis produced appreciable, and the two Lactobacillus casei isolates moderate and low, levels of FN degradation.     

Amylopectin degradation in pea chloroplast extracts

Phosphorolysis rather than phosphorylation of amylolysis products was found to be the major pathway of sugar phosphate formation from amylopectin by pea (Pisum sativum L.) chloroplast stromal proteins. The K_m for inorganic phosphate incorporation was 2.5 mm, and ATP did not stimulate amylopectin-dependent phosphate incorporation. Arsenate (10 mm) inhibited phosphate incorporation into glucose monophosphates up to 46% and phosphoglucomutase activity 96%, resulting in glucose 1-phosphate accumulation as a product of amylopectin degradation. The intracellular distribution of enzymes of starch utilization was determined. Phosphorylase, phosphoglucomutase, and hexokinase were found in the chloroplast and cytoplasm, while β-amylase was restricted to the cytoplasm. Maltase was not detectable; maltose phosphorylase was active in the chloroplast.     

Effect of copper on the degradation of phenanthrene by soil micro-organisms

AIMS: The effect of copper on the degradation by soil micro-organisms of phenanthrene, a polycyclic aromatic hydrocarbon, was investigated. METHODS AND RESULTS: Inert nylon filters were incubated in the soil for 28 days at 25 degrees C. Each filter was inoculated with a soil suspension, phenanthrene (400 ppm), copper (0, 70, 700 or 7000 ppm) and nitrogen/phosphorus sources. The filters were assessed for phenanthrene degradation, microbial respiration and colonization. Phenanthrene degradation proceeded even at toxic copper levels (700/7000 ppm), indicating the presence of phenanthrene-degrading, copper-resistant and/or -tolerant microbes. However, copper at these high levels reduced microbial activity (CO2 evolution). CONCLUSION: High levels of copper caused an incomplete mineralization of phenanthrene and possible accumulation of its metabolites. SIGNIFICANCE AND IMPACT OF THE STUDY: The presence of heavy metals in soils could seriously affect the bioremediation of PAH-polluted environments.     

Synthesis and degradation of nitrite reductase in pea leaves

We have shown in a previous publication (Gupta, Beevers 1983 J Exp Bot 34: 1455-1462) that the level of extractable nitrite reductase activity in pea (Pisum sativum cv Burpeeana) leaves is subject to environmental perturbations. In the current study, we have used rocket immunoelectrophoresis to quantitate the level of nitrite reductase protein in extracts from pea plants subjected to various environmental treatments. The level of nitrite reductase cross-reacting material closely followed the level of assayable nitrite reductase activity. The environmental conditions which enhanced the level of extractable nitrite reductase activity resulted in an increased level of nitrite reductase cross-reacting material in the extracts. In contrast, environmental conditions which resulted in a decrease in the level of extractable nitrite reductase activity produced a decline in cross-reacting material. These results indicate that the environmentally induced modulation of extractable nitrite reductase activity involves alteration of enzyme level and is not mediated by a reversible activation-inactivation of the existing enzyme.     

Enzymatic degradation of raffinose family sugars in chickpea flour

The use of crude -galactosidase from Gibberella fujikuroi to reduce the flatulence-inducing raffinose family sugars in chickpea flour was studied. Crude enzyme treatment of chickpea flour resulted in complete hydrolysis of sugars of the raffinose family. This method could be useful on commercial scale.     

Effects of minerals on feed degradation and protein synthesis by rumen micro-organisms in a dual effluent fermenter.

In dual outflow continuous fermenters on a 75:25 hay/barley diet, feed degradation and protein synthesis by mixed rumen microbes were tested in relation to the concentrations of HPO4(2-), HCO3- and Cl- and Na+/K+ ratio in artificial saliva, by applying a 16-run Franquart design, and by fitting second-order polynomial models. The HPO4(2-), HCO3-, Cl- concentrations and Na+/K+ ratio ranged from 0.1 to 4 g.L-1, from 0.5 to 7 g.L-1, from 0.1 to 0.5 g.L-1 and from 0.5 to 15 g.g-1, respectively. Buffer salts, particularly HPO4(2-), were the major factors while Cl- concentration had negligible effects on microbial metabolism. Maximal neutral detergent fibre, acid detergent fibre and organic matter degradabilities occurred at intermediate values of HPO4(2-) and HCO3- concentrations. The outflow of microbial protein and the efficiency of microbial protein synthesis, which varied from 26.2 to 37.1 g.N.kg-1 of organic matter truly degraded, reached minima at the centre of the experimental domain.     

Utilization and degradation of an ester-based synthetic lubricant by Acinetobacter lwoffi

An oil-degrading bacterium, Acinetobacter lwoffi, isolated by elective culture from the Medway estuary, utilized an ester-based synthetic lubricating oil EMKARATE DE 155 as sole carbon and energy source. Analysis of culture supernatants by gas chromatography showed the accumulation of a nondegradable metabolite 1,1,1 Tris (hydroxymethyl) propane in addition to two metabolizable fatty acids, octanoic and decanoic acids as products of the synthetic oil degradation. Esterase activities were subsequently demonstrated in oil and acetate-grown cells. The synthetic oil therefore appears to be partially biodegradable in the environment.     

Utilization and degradation of an ester-based synthetic lubricant by Acinetobacter lwoffi

An oil-degrading bacterium, Acinetobacter lwoffi, isolated by elective culture from the Medway estuary, utilized an ester-based synthetic lubricating oil EMKARATE DE 155 as sole carbon and energy source. Analysis of culture supernatants by gas chromatography showed the accumulation of a nondegradable metabolite 1,1,1 Tris (hydroxymethyl) propane in addition to two metabolizable fatty acids, octanoic and decanoic acids as products of the synthetic oil degradation. Esterase activities were subsequently demonstrated in oil and acetate-grown cells. The synthetic oil therefore appears to be partially biodegradable in the environment.     

Phytate hydrolysis by germfree and conventional rats.

Phytic acid is naturally occurring compound that reduces intestinal absorption of many metals. Early work suggests that some dietary phytate may be hydrolyzed in the large intestines by bacteria, but more recently nutritionists have suggested that a mucosal enzyme is responsible. This paper reports a study intended to resolve this controversy. The hydrolysis of dietary phytic acid was measured in germfree and conventional rats fed either of two diets that differed in their calcium content. Negligible phytate hydrolysis occurred in the germfree rats, whereas 22 and 56% of the phytic acid was hydrolyzed by conventional rats fed high- and low-calcium diets, respectively. We concluded that bacteria were responsible for the hydrolysis of phytate in these diets and that any activity of endogenous enzyme was negligible.     

Enzyme levels in pea seedlings grown on highly salinized media

The levels of 18 enzymes were determined in leaves, stems, and roots of 11-day-old pea seedlings grown in a liquid medium or in the same medium containing, in addition, 5 atmospheres of either NaCl, KCl, Na₂SO₄, or K₂SO₄. Though the plants grown in saline media were stunted, the specific activities of the enzymes were the same in the given tissues of all plants. Also, the electrophoretic pattern of isozymes of malate dehydrogenase was not altered by growth of the plants in a saline medium. However, the isozyme pattern of peroxidase from roots of salt-grown plants was altered in that two of the five detectable isozymes migrated a little more slowly than those in extracts from nonsaline plant tissues.     

Phytate dephosphorylation by free and immobilized cells ofSaccharomyces cerevisiae

Summary Saccharomyces cerevisiae in the form of baker's yeast, cells cultivated on a yeast extract-peptone-glucose medium, as well as cells immobilized in 18% (w/v) polyacrylamide gel showed the ability to hydrolyze 1.727 mM sodium phytate solution at 45°C, pH 4.6, in a stirred tank reactor. Seventy percent yield of dephosphorylation was observed after 2 h using a baker's yeast concentration of 5.8 g dry matter per 100 ml. Hydrolytic activity at 1.8–2.0 M Pi min^–1 was observed between 1st and 3rd h of the reaction in cells cultured 24 or 48 h. No inhibition by the substrate was found at sodium phytate concentrations of 0.587–1.727 mM. After 1.5 h of hydrolysis a single, well distinguished peak ofmyo-inositol-triphosphate was the main product found. By means of immobilization the stability of the biocatalyst was enhanced 3.3-fold and reached its half-life at 64 ninety-minute runs.     

Inhibition of hepatic protein degradation by synthetic analogues of chymostatin

Analogues of the microbial proteinase inhibitor chymostatin have been synthesized. The two most promising analogues were tested on protein turnover in isolated rat hepatocytes. Their effect is much similar to the effect of chymostatin, but the analogues are even more powerful inhibitors, probably due to an increased effect on lysosomal thiol proteinases. The analogues blocked most of the lysosomal (i.e. methylamine-sensitive) degradation of endogenous protein and caused a 50% inhibition of the non-lysosomal degradation; the effect occurred rapidly and was reversed upon washing the cells. One of the analogues, Z-Arg-Leu-Phe(H), is the most potent inhibitor of hepatic protein degradation so far found.