Title Peptidazių iš Geobacillus thermoleovorans DSM 15325 kolagenolizinio aktyvumo analizė: M3 proteolizinių fermentų šeimos M3B pošeimio oligopeptidazės ir U32 proteolizinių fermentų šeimos peptidazės charakterizavimas /
Translation of Title The collagenolytic activity analysis of Geobacillus thermoleovorans DSM 15325 peptidases: characterization of M3 proteolytic enzymes family M3B subfamily oligopeptidase and U32 proteolytic enzymes family peptidase.
Authors Jasilionis, Andrius
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Pages 158
Keywords [eng] collagenases ; collagen ; geobacilli
Abstract [eng] The full understanding of laws of nature cannot be accomplished without comprehensive characterisation of collagenolysis as collagen is a major structural protein in organisms. The diversity of collagenolytic peptidases from non-pathogenic bacteria remains only fragmentary characterized, whereas the characterization of the diversity of collagenolytic peptidases from eukaryotes and pathogenic bacteria are far more comprehensive. The determined constitutive production of collagenases by moderate thermophile Geobacillus thermoleovorans DSM 15325 confirms the ability of thermophiles to be ever ready for collagen uptake. The identification of constitutive collagenolytic peptidases variety produced by geobacilli lead to substantial development of collagen degradation model and confirms importance of collagenolytic potential for adaptive plasticity of bacteria. Determined M3 family M3B subfamily oligopeptidases, secreted by geobacilli, characteristics indicate oligopeptidases nutritional importance for bacteria during the adaption for environmental changes. Combination of oligopeptidases characteristics also outlines biotechnological applicability of this thermostable hydrolase. Determined U32 family peptidase from geobacilli characteristics ensure objective understanding of U32 family peptidases characteristics and functional importance. U32 family peptidases ability to specifically in vitro interact with dsRNA was never determined for collagenolytic peptidases previously.
Dissertation Institution Vilniaus universitetas.
Type Doctoral thesis
Language Lithuanian
Publication date 2016