User:Mpuri11

Naringinase has become biotechnologically important due to its role in debittering citrus fruit juices, in the manufacture of rhamnose, preparation of prunin and biotransformation of antibiotics [1]. For complete modification/degradation of bittering components, concerted efforts were made either to develop soluble enzymes or microbes capable of metabolizing naringin.The use of enzymes with significant industrial application is increasing but there are few reports available on the production of naringinase, most of them are either guarded secrets of the industry or are patented [2]. Naringinase has been entrapped in alginate matrix [3] and covalently immobilized on hen egg white [4] & wood chips [5] for achieving debittering of kinnow fruit juice.

[1]Puri, M. and Banerjee, U.C. 2000. Production, purification and characterization of the debittering enzyme naringinase. Biotechnology Advances 18, 207- 217. [IF 5.2] [2] Puri, M., Banerjee, A. and Banerjee, U.C. 2005. Studies on the optimization of process parameters for the production of naringinase by Aspergillus niger MTCC 1344. Process Biochemistry 40(1), 195-201.[IF 2.336] [3] Puri, M., Marwaha, S.S. and Kothari, R.M.1996. Comparative kinetic characterisation of soluble and alginate entrapped naringinase. Enzyme Microbial Technology 18, 281-285. [4] Puri,M., Seth, M., Marwaha, S.S. and Kothari, R.M. 2001. Debittering of kinnow mandarin juice by covalently immobilized naringinase on hen egg white. Food Biotechnol. 15(1), 15-27. [5] Puri, M, Kaur, S. and Kennedy, J.F.K. 2005. Studies on the improvement in the catalytic activity of enzymes for the transformation of flavonoids. Journal of Chemical Technology and Biotechnology 80:1160-1165.