SLIME PRODUCTION AND DNase ACTIVITY OF STAPHYLOCOCCI ISOLATED FROM RAW MILK

In this study, 851 Staphylococci isolates isolated from 38 raw milk samples were investigated for DNase activity and slime production. The 851 Staphylococci isolates were identified as 704 Staphylococcus aureus and 147 coagulase-negative staphylococci. Coagulase – negative staphylococci isolates were classified as 32.7% S. cohnii, 19.7% S. hominis, 19.1% S. xylosus, 12.9% S. epidermidis, 8.2% S. capitis, 4.8% S. haemolyticus, 1.4% S. simulans and 1.4% S. saprophyticus by using Dichotomous scheme. DNase agar was used to investigate for DNase activity. DNase activity was found in 93.6% of 704 S. aureus and 10.2% of 147 coagulase – negative staphylococci. DNase activity was positive in 42.9% of S. haemolyticus, 20.7% of S. hominis, 17.9% of S. xylosus and 2.1% of S. cohnii isolates. No DNase activity was found in S. epidermidis, S. capitis, S. simulans and S. saprophyticus isolates. Slime production of S. aureus and coagulase – negative staphylococci from raw milk samples was investigated by using Congo Red Agar method. Slime production was positive in 5.1% of S. aureus and 42.2% of 147 coagulase – negative staphylococci. Slime production was positive in 100% of S. simulans, 68.4% of S. epidermidis, 50% of S. cohnii, 50% of S. saprophyticus, 37.9% of S. hominis, 32.1% of S. xylosus and 16.7% of S. capitis isolates. None of the 7 S. haemolyticus isolates had slime production. In conclusion, slime production and DNase activity are important virulence factors to identify pathogenic staphylococci.     

AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM, LYCOPERDON PERLATUM

Lycoperdon perlatum Pers. (Lycoperdaceae, Agaricales, Agaricomycetidae, Agaricomycetes, Basidiomycota, Fungi) was evaluated for its esterolytic potential. Native electrophoresis of the crude extracts showed four bands having Rf values of 0.34, 0.39, 0.52 and 0.59. The esterase showed the highest activity toward a short-chain substrate, p -nitrophenyl acetate. Optimum reaction conditions for L. perlatum crude extract were attained at pH 8.0 and 40C. Esterolytic activity of enzyme extract was stimulated in the presence of Mn^{2 +} , Fe^{2 +} , Ca^{2 +} and Zn^{2 +} in the reaction mixture. The enzyme activity was stimulated by incubation at pH 6.0 but retained 77% of its original activity at its optimum pH after 24 h. Thermal inactivation was displayed after incubation for 20 min at various temperatures above 30C. At 1 mM final concentration, 2-mercaptoethanol, dithiothreitol, ethylenediamine tetraacetic acid and p -methylphenyl sulfonylfluoride inhibited the esterolytic reaction. These results support that the crude L. perlatum extract possesses an esterolytic activity having properties similar to other esterases.

PRACTICAL APPLICATIONS

Esterases catalyzing the cleavage and formation of ester bonds are known α/β-hydrolases (EC 3.1.1.X). Esterases are used for the synthesis of flavor esters for the food industry, modification of triglycerides for fat and oil industry and resolution of racemic mixtures used for the synthesis of fine chemicals for the pharmaceutical industry. Therefore, the search for new enzyme sources is important for the development of new enzymes and applications.     

Synthesis and investigation of optical properties of ZnS nanostructures

Structural characterizations of wurtzite zinc sulfide (ZnS) nanostructures synthesized by vapour–liquid–solid technique (VLS) were carried out by scanning electron microscopy (SEM), energy dispersive spectroscopy (EDS) and X-ray diffraction (XRD) analyses. Spectral dependence of photoluminescence (PL) was also carried out for optical characterization. PL results indicate that the bandgap energy of bulk ZnS which is 3·68 eV at room temperature changes from 3·7 eV to 3·72 eV depending on the size of the structures. We also supported these results by calculating the bandgap energies theoretically with using the infinite potential well approximation for 1D structures.