ISOLATION, CHARACTERISATION AND OPTIMIZATION OF IMMOBILIZED L-ASPARGINASE- ANTICANCER ENZYM FROM ASPERGILLUS NIGER

Authors

  • Supriya.ch*; SaisriLakshmi.G; SrikalaKommaReddy ;Hemasree. Nagaleela.ch Author

DOI:

https://doi.org/10.48047/

Keywords:

L-Aspariginase, Immobilization, Asparigine, Temperature.

Abstract

L-Aspariginase, an anticancer enzyme fits to a cluster of homologous amino hydrolases which catalyses the
hydrolysis of aminoacid L-asparigine to L-aspartate and ammonia to regulate can cereous disorders. The present
study deals with screening, isolation and optimization of L-aspariginase Producing fungal strain of soil sample from
different areas of AP , India. L-Aspariginase activity was detected on the basis of pink colored surrounding the
growth colony. A total of 132 colonies were screened and isolated from all the samples. Based on the zone diameter
L-aspariginaseacitivity is concluded, L- aspariginaseacitivity is optimized at 28o
c and Immobilized Aspariginase
showed more activity than the free enzymes.

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Published

2021-05-29