Purification of a moderate thermotolerant Bacillus coagulans BTS1 lipase and its properties in a hydro-gel system.
Acta Microbiol Immunol Hung
; 53(1): 77-87, 2006 Mar.
Article
in En
| MEDLINE
| ID: mdl-16696551
ABSTRACT
An alkaline thermotolerant lipase of Bacillus coagulans BTS1 was successively purified by ammonium sulfate precipitation and DEAE anion exchange chromatography. The purified lipase immobilized in alginate beads showed an optimal activity at pH 7.5 and 55 degrees C. A pH of 5.0 or 10.0 completely quenched the activity of immobilized lipase. The alginate-bound lipase retained its activity following exposure to most of the organic solvents including amines, alkanes and alcohols. Chloride salt of Al3+, Co2+, Mg2+ and NH4+ modulated the lipase activity of alginate-immobilized enzyme. The alginate entrapped lipase showed a preferentially high activity towards p-nitrophenyl palmitate (C 16) and activity of matrix increased following exposure to SDS. Moreover, the immobilized lipase retained more than 50% of its activity after 3rd cycle of reuse.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Palmitates
/
Bacillus
/
Enzymes, Immobilized
/
Lipase
Language:
En
Journal:
Acta Microbiol Immunol Hung
Journal subject:
ALERGIA E IMUNOLOGIA
/
MICROBIOLOGIA
Year:
2006
Document type:
Article
Affiliation country:
India
Publication country:
HU
/
HUNGARY
/
HUNGRIA