Immobilization, stability and esterification studies of a lipase from a Bacillus sp.
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 degrees C higher than for the free enzyme, while the pH optima were the same. The half-life of soluble lipase at 50 degrees 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 degrees C in comparison with non-immobilized enzyme. Applications of immobilized lipase for esterification are also presented.
Dosanjh
Nirpjit S
NS
Department of Biotechnology, Panjab University, Chandigarh 160014, India.
Kaur
Jagdeep
J
D000429:Alcohol Oxidoreductases / Q000737:chemistry; D001407:Bacillus / Q000201:enzymology*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D004951:Esterification; D005227:Fatty Acids / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000096:biosynthesis* / Q000737:chemistry*; D000432:Methanol / Q000737:chemistry; D019301:Oleic Acid / Q000737:chemistry; D011137:Polystyrenes; D012685:Sepharose / Q000031:analogs & derivatives*; D012822:Silicon Dioxide; D013379:Substrate Specificity; D013696:Temperature
D004800:Enzymes, Immobilized; D005227:Fatty Acids; D011137:Polystyrenes; D019301:Oleic Acid; C065649:Diaion HP 20; C020927:phenyl-sepharose; D012822:Silicon Dioxide; D012685:Sepharose; D000429:Alcohol Oxidoreductases; C060833:butanol dehydrogenase; D008049:Lipase; D000432:Methanol