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Synthesis of a- and b-naphthyl acetate by alginate-immobilized lipase of Bacillus coagulans MTCC-6375  NEW TRENDS IN BIOENCAPSULATION - Part 2


Minerva Biotecnologica 2006 March;18(1):31-7

Copyright © 2006 EDIZIONI MINERVA MEDICA

lingua: Inglese

Synthesis of a- and b-naphthyl acetate by alginate-immobilized lipase of Bacillus coagulans MTCC-6375

Kaushal R. K. 1, Chimni S. S. 2, Kanwar S. S. 1

1 Department of Biotechnology Himachal Pradesh University Shimla (Himachal Pradesh), India
2 Department of Chemistry Guru Nanak Dev University, Amritsar, India


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Aim. A purified lipase of Bacillus coagulans MTCC-6375 entrapped in alginate beads exhibited an optimal activity at 55 °C and pH 8.5 towards p-nitrophenyl palmitate.
Methods. The immobilized lipase matrix washed extensively in n-nonane catalyzed optimal formation of a- and b-naphthyl acetate from a-naphthol or b-naphthol and acetic acid (1: 3 to 1: 5, v/v) after 9 h and 6 h, respectively at a temperature of 55 °C in n-nonane. The immobilized-lipase was recyclable but leached out approximately 2/3rd of its original hydrolytic activity during the 4th cycles of reuse. The immobilized lipase was stable in the presence of various alcohols (viz. primary, secondary and tertiary) and alkanes.
Results. However, immobilized lipase was relatively more hydrolytic toward longer C-length acyl esters (p-nitrophenyl acetate, C: 16) than other p-nitrophenyl acyl esters of shorter acyl moiety.
Conclusion. The present study suggested potential application(s) of lipase of Bacillus coagulans MTCC-6375 in organic synthesis.

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