Title : Therapeutic drug development using biopolymer degrading enzymes
Abstract:
Biopolymers play critical roles in structure, function, storage, and regulation of biological processes in living beings. Bacterial biopolymers, such as alginate, lipopolysaccharides (LPS), polyhydroxyalkanoates (PHAs), and exopolysaccharides (EPS), play a crucial role in the pathogenicity and biofilm formation of many bacteria. Human biopolymers such as proteins (collagen), nucleic acids, polysaccharides, and lipid assemblies are essential macromolecules for performing various functions. Biopolymer degrading enzymes are emerging as powerful candidates for the development of novel therapeutic drugs due to their ability to target and break down complex biological macromolecules. Enzymes including proteases, glycosidases, lipases, and polysaccharide degrading enzymes, perform specific biochemical activity thus make them ideal for designing enzyme based therapies aimed at a range of diseases Nowadays, these enzymes are being explored as antibiofilm, anti-inflammatory and thrombolytic enzyme drugs for cancer therapy and drug delivery respiratory and mucolytic enzyme drugs. Keeping in mind, enormous therapeutic potential of biopolymer degrading enzymes, collagenase KU665299 from Chryseobacterium contaminans and alginate lyase SG4? from Paenibacillus lautus is investigated in this work. Alginate lyase SG4? exhibit strong biofilm-disrupting activity against Pseudomonas aeruginosa, a major pathogen in lung infections associated with cystic fibrosis (CF). The enzyme disrupted up to 64.6% of alginate-based biofilms and increased the bactericidal activity of gentamicin and amikacin. Simultaneously, collagenase KU665299 showed great promise for thrombolytic therapy by efficiently breaking down blood clots in 40 minutes at 37°C. Together, these enzymes exemplify promising bio-therapeutic agents—alginate lyase for treating biofilm-associated infections and collagenase for clot resolution—offering targeted, enzymatic approaches to critical clinical challenges.
