Stability of a new fungal keratinase (CROSBI ID 469604)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Gradišar, Helena ; Hublin, Andrea ; Friedrich, Jožica ; Vasić-Rački, Đurđa
engleski
Stability of a new fungal keratinase
Keratinases are proteolytic enzymes which catalyze keratin hydrolisis. They have fifferent characteristics, because they could be produced by different microbial sources. Some keratinases are extracellular enzymes showing a high stability. The selcted non-pathogenic fungal strain was cultivated in submerged aerobic conditions. Crude keratinase was prepared by ultrafiltration of the culture filtrate and subsequent lyophilization of the retentate. Protein pattern of the crude enzyme was detected by SDS-PAGE electrophoresis. Enzyme activity was measured on human callus, using a modified method according to Takichi et al (1982), or hemoglobin as the enzyme substrates, using a method of Boehringer Manheim (1973). The influences of temperature, pH and type of buffer om the stability of crude keratinase was investigated. The half-life of the crude enzyme at the pH 7.5 and 40 C was 5 hours. Howewer, at 30 C the enzyme still retained nearly 20% of its activity after 48 hours of incubation. By measuring pH stability at room temperature the activity of the crude enzyme was still above 40 % after 48 hours in the pH range from 6.0 tp 8.0. The results obtained were compared with the characteristics of the commercial fungal keratinolytic enzyme proteinase K.
stability; keratinase
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
Podaci o prilogu
P-123-x.
1998.
objavljeno
Podaci o matičnoj publikaciji
Cordoba: Sociedad Espanola de Biotechnologia
Podaci o skupu
International Symposium on Stability and Stabilization of Biocatalysts
poster
19.04.1998-22.04.1998
Córdoba, Španjolska