[Influence of coordination compounds of germanium (IV) and stannum (IV) on activity of some microbial enzymes with glycolytic and proteolytic action].

Influence of coordinative compounds of germanium (IV) and stanum (IV) (complexes of germanium (IV) with nicotinamide (Nad) [GeCl2(Nad)4]Cl2 (1) and complexes of stanum (IV) with 2-hydroxybenzoilhydrazone 4-dimetylaminobenzaldehide (2-OH-HBdb) [SnCl4(2-OH-Bdb-H)] (2), 3-hydroxy-2-naphtoilhydrazone 2-hydroxynaphtaldehide (3-OH-H2Lnf) [SnCl3(3-OH-HLnf)] (3) and izonicotinoilhydrazone 2-hydroxyibenzaldehide [SnCl3 (Is·H)] (4) on activity of peptidases 1 and 2 Bacillus thuringiensis, α-L-rhamnosidase Cryptococcus albidus, Eupenicillium erubescens and α-amylase Aspergillus flavus var. oryzae. Results testify that all studied compounds differ on their influence on activity of the enzymes tested: significantly don't change elastolytic activity of peptidases 1 and 2 B. thuringiensis, completely inhibit A. flavus var. oryzae amylase, activate or oppress of α-L-rhamnosidase C. albidus and E. erubescens. Considerable differences in compounds (3, 4) on activity observed in case of the last. It's possible that peculiarity of influence (1) in compare with (2-4) is connected with existence of different central atoms of complexants: germanium (IV) (1) and stanum (IV) (2-4). A certain analogy in oppression of C. albidus α-L-rhamnosidase by compounds (1) and (4) can explain with presence of a pyridinic ring at molecules of their ligands. The less activsty displayed compound (2) with coordinative knot {SnCl4ON}. Nature of compounds (3, 4) activity was absolutely different: essential increase of activity of C. albidus α-L-rhamnosidase and full oppression of E. erubescens α-L-rhamnosidase by compound (3), while the action of compound (4) was feed back. Taking into account identical coordination knot {SnCl3O2N} the major role in this case play change of a hydrazide fragment in molecules of their ligands.

Development of macrolide lactone antibiotic brefeldin A fermentation process with Eupenicillium brefeldianum ZJB082702.

In this work, a robust brefeldin A-synthesizing fungus, Eupenicillium brefeldianum ZJB082702, was bred from a Murraya paniculata endophytic fungus E. brefeldianum A1163. Using one-factor-at-a-time experimental design, optimization of media composition for E. brefeldianum ZJB082702 fermenting brefeldin A was conducted. Outcomes indicated that mixed carbon source and mixed nitrogen source were of c ritical importance to brefeldin A fermentation. After 6d culture in the optimized fermentation media, composed of (gl(-1)) 13.33 starch, 26.67 glucose, 1.0 yeast extract powder, 1.0 corn steep liquor, 0.5 soybean meal, 0.75 NaNO(3), 2.5 malt extract, 6.0 CaCO(3), 3.0 MgSO(4), 4.0 KH(2)PO(4), 1.0 × 10(-2) CuSO(4), brefeldin A yield peaked at 1304.7 mgl(-1), 648.2 mgl(-1) in 500 ml baffled flask and 15 l stirred fermentor respectively, formed as a growth associated type of secondary metabolite based on fermentation profile analysis.

[Optimization of cultivation conditions of alpha-L-rhamnosidases producers-- representatives of different taxonomic groups of microorganisms].

Influence ofsome technological parameters of cultivation ofproducers Cryptococcus albidus, Eupenicillinum erubescens, Bacillus sp. on the process of synthesis of extracellular enzyme alpha-L-rhamnosidase has been studied. The authors have determined optimal sources of carbon (0.2-0.3% rhamnose) and nitrogen (0.2% sodium nitrate for C. albidus and E. erubescens and ammonium sulphate for Bacillus sp.) (the ratio 1:2), cultivation temperature (28 degrees C, 25 degrees C, 42 degrees C, respectively) for maximum synthesis of alpha-L-rhamnosidase. Use of the medium with initial pH value from 4 to 8 was most efficient for all the studied strains. The maximum level of alpha-L-rhamnosidase activity of E. erubescens and Bacillus sp. was established at the value of sulphite number of 0.44, while for C. albidus--it was 0.56. Maximum alpha-L-rhamnosidase activity of C. albidus, E. erubescens, Bacillus sp. is achieved at 4, 8 days and 27 hours of cultivation, respectively. The cultures being grown in selected conditions, the alpha-L-rhamnosidase synthesis has increased by 30, 50 and 20%, respectively.

Molecular organization of the mating-type loci in the homothallic Ascomycete Eupenicillium crustaceum.

Eupenicillium species are the teleomorphic (sexual) forms of anamorphic (asexual) members of the genus Penicillium, which contains many species of industrial importance. Here we describe the first molecular analysis of the mating-type (MAT) locus from a homothallic (self-fertile) Eupenicillium species, E. crustaceum. This ascomycete is a sexual relative of the penicillin producer Penicillium chrysogenum, which while long considered asexual, was recently shown to possess the required genetic machinery for heterothallic breeding. The E. crustaceum genome contains two MAT loci, MAT1-1 and MAT1-2, in an arrangement characteristic of other known homothallic euascomycetes, such as Neosartorya fischeri. MAT1-1 is flanked by conserved APN2 (DNA lyase) and SLA2 (cytoskeleton assembly control) genes and encodes a homologue of the α-box domain protein MAT1-1-1. Conversely, MAT1-2 carries a HMG-domain gene MAT1-2-1, and is flanked by a degenerate SLA2 gene and an intact homologue of the P. chrysogenum ORF Pc20g08960. Here we demonstrate the transcriptional expression of both mating-type genes during vegetative development. Furthermore, the MAT1-1-1 and MAT1-2-1 sequences were used to resolve the phylogenetic relationship of E. crustaceum with other ascomycetes. Phylogenetic trees confirmed a very close relationship between the homothallic E. crustaceum and the supposedly heterothallic P. chrysogenum. This close taxonomic association makes E. crustaceum an ideal candidate for future expression and evolutionary studies of sexual reproduction, with the ultimate aim of inducing sex in P. chrysogenum.