[ABILITY OF MICROORGANISMS FROM DIFFERENT ECOLOGICAL NICHES TO HYDROLYZE THE INSOLUBLE PROTEINS]

Area of Science:

• Microbiology and Enzymology
• Biotechnology and Bioprospecting

Context:

• Investigating microbial enzymes capable of degrading recalcitrant animal proteins (collagen, fibrin, elastin, keratin) is crucial for various industrial applications.
• Bacterial and streptomycete strains were isolated from diverse environmental sources, including marine and freshwater ecosystems, and animal-associated environments (dolphins).

Purpose:

• To screen and identify microbial producers of proteases with specificity towards insoluble and sparingly soluble protein substrates of animal origin.
• To evaluate the potential of bacterial and streptomycete isolates as sources for extracellular keratinases and collagenases.

Summary:

• Bacterial strains from dolphin enclosures demonstrated hydrolysis of collagen and elastin but lacked extracellular keratinase activity.
• Streptomycete strains isolated from coastal soils (Black Sea and Atlantic Ocean) showed potential as producers of extracellular keratinase and collagenase.
• The highest enzymatic activity was observed in streptomycete strains from coastal soil areas in Saky, exhibiting up to 5 U/mg.

Impact:

• Identifies promising microbial candidates, particularly streptomycetes from specific soil environments, for the biotechnological production of keratinase and collagenase.
• Contributes to the discovery of novel enzymes for applications in industries such as leather processing, detergent formulation, and waste management.
• Highlights the potential of extremophilic or specialized microbial communities in coastal regions as reservoirs for industrially relevant enzymes.