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Immobilization and stability studies of a lipase from thermophilic Bacillus sp: The effect of process parameters on immobilization of enzyme Electron. J. Biotechnol.
Nawani,Neerupma; Singh,Rajvinder; Kaur,Jagdeep.
A thermostable lipase was partially purified from the culture supernatant of a thermophilic Bacillus sp. The enzyme is optimally active at 60ºC and pH 8.0. The enzyme showed enhancement in activity in presence of benzene or hexane (30% v/v each). The activity (assayed by determining the release of pNP from pNP laurate) was stimulated up to 60% of these solvents in enzyme reaction mixture. The catalytic properties of this thermostable enzyme can be further improved via the use of different immobilization techniques and reaction conditions. Enzyme was immobilized on different solid supports and their enzyme activity and stability was compared. The enzyme was adsorbed on silica and HP-20 beads followed by cross-linking with gluteraldehyde on HP-20,...
Tipo: Journal article Palavras-chave: Esterification; Immobilization; Lipase; Thermostability.
Ano: 2006 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000500011
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