• Yadvinder Singh
• NeelamVerma
• VikasHooda

The Presence of Diamine oxidase (DAO) has gained tremendous attention in food and allied industries for guarding food freshness and safety.All the commercial application of enzymes as biocatalysts requires simple but efficient methods to immobilize the enzyme to yield highly stable and active biocatalysts. In this study, DAO was extracted, purified and immobilized by entrapment in matrix sodium alginate in presence of the enzyme. The optimal parameters of free and immobilized DAO activity were evaluated against the substrate, Putrescinedihydrochloride and the results showed that the stabilities were significantly enhanced compared with free counterpart. The optimum working pH was 7.5 where both free and immobilized enzyme showed their maximum activity.. Free enzyme showed maximum activity at 37°C while immobilized enzyme showed stable activity at a wide range of temperature. Residual activity of the immobilized enzyme was 59% of the initial activity after being recycled 10 times. Therefore, this method may provide an excellent support for enzyme immobilization having better catalytic ability in large scale applications in biotechnological industries.

Diamine oxidase enzyme; entrapment immobilization, Comparative Study of Enzyme properties

"Efficient immobilization of Diamine Oxidase by entrapment and study of optimum parameters", International Journal of Emerging Technologies and Innovative Research (www.jetir.org), ISSN:2349-5162, Vol.6, Issue 6, page no.501-515, June-2019, Available :http://www.jetir.org/papers/JETIR1908C65.pdf

"Efficient immobilization of Diamine Oxidase by entrapment and study of optimum parameters", International Journal of Emerging Technologies and Innovative Research (www.jetir.org | UGC and issn Approved), ISSN:2349-5162, Vol.6, Issue 6, page no. pp501-515, June-2019, Available at : http://www.jetir.org/papers/JETIR1908C65.pdf