lip2 lipase
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Author(s):  
Emna Moujehed ◽  
Zied Zarai ◽  
Haifa Khemir ◽  
Neila Miled ◽  
Mohamed Salah Bchir ◽  
...  


Biochimie ◽  
2014 ◽  
Vol 102 ◽  
pp. 145-153 ◽  
Author(s):  
Anaïs Bénarouche ◽  
Vanessa Point ◽  
Frédéric Carrière ◽  
Jean-François Cavalier


2011 ◽  
Vol 47 (8) ◽  
pp. 744-753 ◽  
Author(s):  
E. Yu. Yuzbasheva ◽  
T. V. Yuzbashev ◽  
T. K. Konstantinova ◽  
I. A. Laptev ◽  
N. I. Perkovskaya ◽  
...  


2011 ◽  
Vol 156 (2) ◽  
pp. 117-124 ◽  
Author(s):  
Florence Bordes ◽  
Laurence Tarquis ◽  
Jean-Marc Nicaud ◽  
Alain Marty


2011 ◽  
Vol 91 (3) ◽  
pp. 645-654 ◽  
Author(s):  
Evgeniya Y. Yuzbasheva ◽  
Tigran V. Yuzbashev ◽  
Ivan A. Laptev ◽  
Tatiana K. Konstantinova ◽  
Sergey P. Sineoky


Author(s):  
Ahmed Aloulou ◽  
Jorge A. Rodriguez ◽  
Delphine Puccinelli ◽  
Nicolas Mouz ◽  
Julien Leclaire ◽  
...  


2002 ◽  
Vol 366 (2) ◽  
pp. 603-611 ◽  
Author(s):  
Guan-Chiun LEE ◽  
Li-Chiun LEE ◽  
Vasyl SAVA ◽  
Jei-Fu SHAW

The 17 non-universal serine codons (CTG) in the Candida rugosa LIP2 gene have been converted into universal serine codons (TCT) by overlap extension PCR-based multiple site-directed mutagenesis. An active recombinant LIP2 lipase was overexpressed in Pichia pastoris and secreted into the culture medium. The recombinant LIP2 showed distinguishing catalytic activities when compared with recombinant LIP4 and commercial C. rugosa lipase. The purified enzyme showed optimum activity at pH7 and a broad temperature optimum in the range 30–50°C. The enzyme retained 80% of residual activity after being heated at 70°C for 10min. Recombinant LIP2 demonstrated high esterase activity towards long-chain (C12–C16) p-nitrophenyl esters. Tributyrin was the preferred substrate among all triacylglycerols tested for lipolysis. Among cholesteryl esters, LIP2 showed highest lipolytic activity towards cholesteryl laurate. The esterification of myristic acid with alcohols of various chain lengths showed that the long-chain n-octadecanol (C18) was the preferred substrate. In contrast, the esterification of n-propanol with fatty acids of various chain lengths showed that the short-chain butyric acid was the best substrate. From comparative modelling analysis, it appears that several amino acid substitutions resulting in greater hydrophobicity in the substrate-binding site might play an important role in the substrate specificity of LIP2.



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