Abstract

β-glucuronidase enzyme belongs to the hydrolase family which perform breakdown of complex carbohydrates. β- glucuronidases are large biomolecule consists of polypeptide chains and are widely included eukaryotes and prokaryotes, however their parasitic sources are extremely constrained. β-glucuronidase from fungal source could be profoundly valuable as a result of its high selectivity and stability over extensive variety of pH and temperature which makes it exceptionally reasonable for mechanical applications. Number of studies have been conducted to test the enzyme stability by immobilization which can easily be detached from biomaterials and nano particles for repeated use in the chemical reaction. β-glucuronidase is also comprehensively use in industry for protein catalyzed reactions. For this purpose enzyme was isolated and cloned from many sources such as Penicillium purpurogenum Li-3 ZnO-NP, sodium alginate, sepabeads etc. These studies revealed that β-glucuronidase shows maximum catalytic activity at pH below 7 after immobilization on biomaterials and on divalent metal ions. The catalyst turns out to be more effective and has higher fondness for the substrate. Key words: β-glucuronidase, immobilization and polypeptide chains

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