Arthrobacter sp. lipase immobilization for improvement in stability and enantioselectivity

@article{Chaubey2006ArthrobacterSL,
  title={Arthrobacter sp. lipase immobilization for improvement in stability and enantioselectivity},
  author={Asha Chaubey and Rajinder Parshad and Surrinder Koul and Subhash Chandra Taneja and Ghulam Nabi Qazi},
  journal={Applied Microbiology and Biotechnology},
  year={2006},
  volume={73},
  pages={598-606}
}
Arthrobacter sp. lipase (ABL, MTCC no. 5125) is being recognized as an efficient enzyme for the resolution of drugs and their intermediates. The immobilization of ABL on various matrices for its enantioselectivity, stability, and reusability has been studied. Immobilization by covalent bonding on sepharose and silica afforded a maximum of 380 and 40 IU/g activity, respectively, whereas sol–gel entrapment provided a maximum of 150 IU/g activity in dry powder. The immobilized enzyme displayed… CONTINUE READING