001. Dunaevsky, Y.E., Popova,  V.V., Semenova, T.A., Beliakova, G.A. and Belozersky, M.A. A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia. Fungal inhibitors of proteolytic enzymes: Classification, properties, possible biological roles, and perspectives for practical use.Biochimie, 101, 2014, Pages: 10 - 20.

Peptidase inhibitors are ubiquitous regulatory proteins controlling catalytic activity of proteolytic enzymes. Interest in these proteins increased substantially after it became clear that they can be used for therapy of various important diseases including cancer, malaria, and autoimmune and neurodegenerative diseases. In this review we summarize available data on peptidase inhibitors from fungi, emphasizing their properties, biological role, and possible practical applications of these proteins in the future. A number of fungal peptidase inhibitors with unique structure and specificity of action have no sequence homology with other classes of peptidase inhibitors, thus representing new and specific candidates for therapeutic use. The main classifications of inhibitors in current use are considered. Available data on structure, mechanisms and conditions of action, and diversity of functions of peptidase inhibitors of fungi are analyzed. It is mentioned that on one side the unique properties of some inhibitors can be used for selective inhibition of peptidases responsible for initiation and development of pathogenic processes. On the other side, general inhibitory activity of other inhibitors towards peptidases of various catalytic classes might be able to provide efficient defense of transgenic plants against insect pests by overcoming compensatory synthesis of new peptidases by these pests in response to introduction of a fungal inhibitor. Together, the data analyzed in this review reveal that fungal inhibitors extend the spectrum of known peptidase inhibitors potentially suitable for use in medicine and agriculture.

Keywords: Fungi; Peptidase inhibitors; Proteolytic enzymes; Practical application; Medicine; Agriculture.

002. Karthik, L., Kumar, G., Keswani, T., Bhattacharyya, A., Sarath Chandar, S. and Bhaskara Rao, K. V. Environmental Biotechnology Division, School of Bio Sciences and Technology, VIT University, Vellore, Tamil nadu, India. Protease inhibitors from marine actinobacteria as a potential source for antimalarial compound. PLoS ONE, 9(3), 2014, e90972.

The study was planned to screen the marine actinobacterial extract for the protease inhibitor activity and its anti- Pf activity under in vitro and in vivo conditions. Out of 100 isolates, only 3 isolates exhibited moderate to high protease inhibitor activities on trypsin, chymotrypsin and proteinase K. Based on protease inhibitor activity 3 isolates were chosen for further studies. The potential isolate was characterized by polyphasic approach and identified as Streptomycessp LK3 (JF710608). The lead compound was identified as peptide from Streptomyces sp LK3. The double-reciprocal plot displayed inhibition mode is non-competitive and it confirms the irreversible nature of protease inhibitor. The peptide from Streptomyces sp LK3 extract showed significant anti plasmodial activity (IC₅₀: 25.78 µg/ml). In in vivo model, the highest level of parasitemia suppression (≈45%) was observed in 600 mg/kg of the peptide. These analyses revealed no significant changes in the spleen and liver tissue during 8 dpi. The results confirmed up-regulation of TGF-β and down regulation of TNF-α in tissue and serum level in PbA infected peptide treated mice compared to PbA infection. The results obtained infer that the peptide possesses anti- Pf activity activity. It suggests that the extracts have novel metabolites and could be considered as a potential source for drug development.

003.Choudhary, B., Nagpure, A. and Gupta, R.K. University School of Biotechnology, Guru Gobind Singh Indraprastha University, Dwarka, New Delhi, India.Fungal cell-wall lytic enzymes, antifungal metabolite(s) production, and characterization from Streptomyces exfoliatus MT9 for controlling fruit-rotting fungi. Journal of Basic Microbiology, 2014.

An antifungal actinomycete strain MT9 was isolated from Loktak Lake, Manipur, India and its cultural characteristics, fatty acid methyl ester, 16S rRNA gene analysis suggests that strain MT9 is identical to Streptomyces exfoliatus. Strain MT9 displayed strong and broad-spectrum antagonism towards several fruit-rotting fungi by mycelial growth suppression. Crude fungal cell-wall lytic enzymes, i.e., chitinase, ß-1,3-glucanase, and protease produced by S. exfoliatus MT9 were optimally active at pH 8.0 and 50°C, pH 5.0 and 60°C, pH 9.0 and 70°C, respectively. All three mycolytic enzymes had good stability over a wide pH range of 5.0–10.0, with protease being more thermostable than both chitinase and ß-1,3-glucanase. Interestingly zymogram analysis revealed that S. exfoliatus MT9 secretes six distinct chitinase isoenzymes with approximate molecular weights of 9.42, 13.93, 27.87, 36.43, 54.95 and 103.27kDa, six active protease isoenzymes with apparent molecular weights of 12.45, 30.20, 37.45, 46.32, 52.46 and 131.46kDa, and an active band of 119.39kDa as ß-1,3-glucanase enzyme. Extracellular fluid and its organic solvent extracts also exhibited inhibitory activity to various fruit-rotting fungi. The MIC value of n-butanol extract was 2–25µg/ml against tested fruit-rotting fungi. Antifungal secondary metabolite(s) was found to be polyene in nature. To the best of our knowledge, this is the first report on extracellular production of fungal cell-wall lytic enzymes and antifungal metabolites by bioactive S. exfoliatus MT9 under submerged fermentation.

Keywords: Cell-wall lytic enzymes; Fruit-rotting fungi; Streptomyces exfoliatus; Zymogram