Collect. Czech. Chem. Commun.
2001, 66, 1707-1719
https://doi.org/10.1135/cccc20011707
Enzymological Characterization of Secreted Proteinases from Candida parapsilosis and Candida lusitaniae
Olga Hrušková-Heidingsfeldováa, Jiří Dostála, Petr Hamalb, Jarmila Pazlarovác, Tomáš Rumlc and Iva Pichováa,*
a Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, 166 10 Prague 6, Czech Republic
b Institute of Microbiology, Faculty of Medicine, Palacký University, 771 46 Olomouc, Czech Republic
c Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague, 166 28 Prague 6, Czech Republic
Abstract
Opportunistic pathogens of the genus Candida produce secreted aspartic proteinases (Saps) that are considered as one of the virulence factors. While Saps of C. albicans and C. tropicalis have been studied extensively, information concerning proteinases secreted by other pathogenic Candida species is scarce. To our knowledge, enzymologic characterizations of Sap of C. parapsilosis (Sapp1p) and C. lusitaniae (Saplp) are limited. We have purified Saps of C. parapsilosis and C. lusitaniae from yeast culture supernatants and detected only one gene product of both Sapp1p and Saplp using isoelectric focusing and N-terminal sequencing. Molecular weight of Saplp determined by SDS-PAGE is approximately 42 000. For the highest enzyme activity, both Sapp1p and Saplp require pH ranging from 3 to 4 and temperature between 27-40 °C for Saplp and 45 °C for Sapp1p, respectively. At physiological temperature, both the proteinases are stable. The characterization of Saps of clinical isolates of C. parapsilosis and C. lusitaniae should contribute to design of novel drugs specifically targeted on proteinases.
Keywords: Candida parapsilosis; Candida lusitaniae; Aspartic proteinase; pH optimum; Thermal stability; Proteolytic enzymes; Isolation; Yeasts; Anticandidal agents.
References: 31 live references.
