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The ATP level and the number of mesophilic bacteria, thermophilic bacteria, moulds and yeasts were examined in different composts prepared from lupine (Lupinus angustifolius cv Mirela). During the first weeks of composting, the mesophiles increased slowly and the thermophile phase follows. After eight weeks of composting the number of thermophiles decreased rapidly and development of mesophilic bacteria and fungi was observed. From five ATP extraction methods, the best results were obtained from Celsis-Lumac extracting mixtures and it was chosen for further experiments. The ATP level increased at the beginning of composting and decreased after 8 weeks of the process. After this time, ATP content began to rise to the achieved maximum during the 12th week of composting. There is no correlation between the number of microorganisms in compost and the ATP level.
The study has been carried out in order to optimise the conditions for the biodegradation of potato slops with a mixed population of thermophilic and mesophilic bacteria.
Optimizing production of α-amylase production by Thermoactinomyces vulgaris isolated from Egyptian soil was studied. The optimum incubation period, temperature and initial pH of medium for organism growth and enzyme yield were around 24 h, 55°C and 7.0, respectively. Maximum α-amylase activity was observed in a medium containing starch as carbon source. The other tested carbohydrates (cellulose, glucose, galactose, xylose, arabinose, lactose and maltose) inhibited the enzyme production. Adding tryptone as a nitrogen source exhibited a maximum activity of α-amylase. Bactopeptone and yeast extract gave also high activity comparing to the other nitrogen sources (NH₄Cl, NH₄NO₃, NaNO₃, KNO₃, CH₃CO2 NH₄). Electrophoresis profile of the produced two α-amylase isozymes indicated that the same pattern at about 135145 kDa under different conditions. The optimum pH and temperature of the enzyme activity were 8.0 and 60°C, respectively and enzyme was stable at 50°C over 6 hours. The enzyme was significantly inhibited by the addition of metal ions (Na⁺, Co²⁺ and Ca²⁺) whereas Cl⁻ seemed to act as activator. The enzyme was not affected by 0.1 mM EDTA while higher concentration (10 mM EDTA) totally inactivated the enzyme.
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