Premium
Immobilization, stability and esterification studies of a lipase from a Bacillus sp.
Author(s) -
Dosanjh Nirpjit S.,
Kaur Jagdeep
Publication year - 2002
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20010070
Subject(s) - thermostability , lipase , immobilized enzyme , chemistry , thermal stability , enzyme , triacylglycerol lipase , chromatography , organic chemistry
In the present paper a comparative account of the immobilization of a Bacillus lipase on different solid supports with different surface properties and their thermostability is presented. Immobilization enhanced the thermostability of lipase. At higher temperatures, lipase immobilized and cross‐linked on a hydrophobic surface showed the maximum thermostability. The optimum temperature for immobilized lipase was 9 °C higher than for the free enzyme, while the pH optima were the same. The half‐life of soluble lipase at 50 °C was calculated to be 4.5 h, while immobilized lipase did not lose any activity even after 8 h. The temperature stability (for 1 h) of immobilized enzyme was enhanced from 50 to 60 °C in comparison with non‐immobilized enzyme. Applications of immobilized lipase for esterification are also presented.