The SAS proposals for participation in FP6 projects
are listed in blocks according to the FP6 priority theme structure

FP6 priority
1.1.5   Food Quality and Safety
Title of the proposal

Pectolytic enzymes of plants, yeasts and fungi- their production, characterization and the relationship between the structure and the function

Slovak Academy of Sciences, Laboratory of Pectolytic Enzymes, Institute of Chemistry,
Dubravska cesta 9, 842 38 Bratislava, Slovak Republic
+421 2 5941 0212

Research subject for a potential FP6 project

The objective of this proposal is to study the production of multiple forms of pectolytic enzymes, mainly polygalacturonase, produced by plants, fungi and yeasts. The latter are the object of our interest at present time because the pectinase production in yeasts and yeast-like microor-ganisms has received only little attention in comparison with fungal, bacterial and plant poly-galacturonases. As a result, some novel forms of these enzymes may be found. Various factors, including ecological changes of environment, which can influence the production of multiple forms of this enzyme, are studied. However, the aim of our work is to prepare homogeneous forms of individual polygalacturonases forms, to characterize them, to study their structure and structure-function relationship, and to compare them with the known ones.

Recent international cooperation of the research team

- primary structures: Karolinska Institutet, Dept. of Medical Biochem. Biophys., S -171 77 Stockholm, Sweden (Prof. H. Jornvall); - tertiary structures: Biomedical Centrum, Dept. of Molecular Biology, S – 751 24 Uppsala, Sweden (Prof. H. Eklund); - various: Faculty of Chemistry, Technical University of Brno, Purkynova 118, CZ – 612 00 Brno, Czech Republic (Dr. J. Omelkova)

Proposer´s relevant publications related to the research subject

1. O. Markovic, H. Jornvall: The primary structure of the tomato enzyme. Eur. J. Biochem. 158 (1986) 455-462.
2. O. Markovic, H. Jornvall: Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active segments. Protein Science 1 (1992) 1288-1292.
3. E. Stratilova, O. Markovic, D. Skrovinova, L. Rexova-Benkova, H. Jornvall: Pectinase Aspergillus sp. polygalacturonase: multiplicity, divergence, and structural patterns linking fungal, bacterial, and plant polygalacturonases. J. Prot. Chem. 12 (1993) 15-22.
4. E. Stratilova, M. Dzurova, O. Markovic, H. Jornvall: An essential tyrosine residue of Aspergillus polygalacturonase. FEBS Lett. 382 (1996) 164-166.
5. E. Stratilova, D. Mislovicova, M. Kacurakova, E. Machova, N. Kolarova, O. Markovic, H. Jornvall: The glycoprotein character of multiple forms of Aspergillus polygalacturonase. J. Prot. Chem. 17 (1998) 173-179.
6. E. Stratilova, E. Breierova, R. Vadkertiova, E. Machova, A. Malovikova, E. Slavikova: The adaptability of methylotrophic yeast Candida boidinii on media containing pectic substances. Can. J. Microbiol. 44 (1998) 173-179.
7. O. Markovic, S. Janecek: Pectin degrading glycoside hydrolases of family 28: sequence-structural features, specifities and evolution, Prot. Engineering 9 (615-631) 2001.