Inhibitors of sterol synthesis. 15-Oxygenated steryl ester hydrolase activity of rat liver at neutral and acid pH

1989 ◽  
Vol 1001 (2) ◽  
pp. 127-133 ◽  
Author(s):  
Thomas W. Stephens ◽  
George J. Schroepfer
Keyword(s):  
Rat Liver ◽  
Steryl Ester ◽  
Hydrolase Activity ◽  
Sterol Synthesis ◽  
Acid Ph ◽  
Ester Hydrolase

scholarly journals High-level soluble expression and enzymatic characterization of Burkholderia sp. lipase with steryl ester hydrolysis activity in E. coli

2019 ◽  
Author(s):  
Zhengyu Shu ◽  
Feng Li ◽  
Wenjing Jia ◽  
Xiangduo Mu ◽  
Hong Lin ◽  
...  
Keyword(s):  
Steryl Ester ◽  
Specific Activity ◽  
Soluble Expression ◽  
Hydrolase Activity ◽  
Biodiesel Production ◽  
Enzymatic Characterization ◽  
E Coli ◽  
Ester Hydrolase ◽  
Triacylglycerol Hydrolase ◽  
High Level

Abstract Background Burkholderia cepacia lipase is an important industrial biocatalyst for biodiesel production and chiral pharmaceutical synthesis. Heterologous soluble expression of lipase lipA gene from B. cepacia in Escherichia coli highly depends on co-expression of its cognate foldase gene, lipB. However, the interaction between recombinant lipase LipA and chaperonin LipB is rather complicated and confusing. In this research, various systems of lipA/lipB co-expression combinations are investigated to obtain high-level soluble expression of lipA, respectively. Results The best co-expression combination system for lipA and lipB is E. coli Origami 2 (DE3)/pETDuet-lipB(MCS1)/lipA(MCS2). The soluble expression level of lipA is 100.4 U/OD600 towards 4-nitrophenyl laurate hydrolysis. The recombinant LipA can be rapidly isolated from cell-free supernatant of recombinant E. coli lysate using HisTrap HP affinity chromatography column, and the lipA/LipB complex is obtained. Enzymatic characterization analysis shows that the purified LipA is a mesothermal and alkaline enzyme. LipA displays preference for medium-chain-length acyl groups (C10-C12) and sn-1,3 regioselectivity. Besides triacylglycerol hydrolase activity (EC. 3.1.1.3), LipA also displays steryl ester hydrolase activity (EC. 3.1.1.13). The specific activity of LipA towards 4-nitrophenyl decanoate and cholesterol linoleate are 638.9 U/mg and 1111.5 mU/mg, respectively. Conclusions Host strain E. coli Origami 2 (DE3), lipB locus at MCS1 on the dual expression cassette plasmid pETDuet, and low-temperature induction contribute to the soluble expression of lipA. Recombinant LipA displays both triacylglycerol hydrolase activity and steryl ester hydrolase activity.

scholarly journals Carnitine Ester Hydrolase of Rat Liver

1969 ◽  
Vol 244 (16) ◽  
pp. 4448-4453
Author(s):  
S Mahadevan ◽  
F Sauer
Keyword(s):  
Rat Liver ◽  
Ester Hydrolase

scholarly journals Retinyl palmitate hydrolase activity in normal rat liver.

1981 ◽  
Vol 256 (9) ◽  
pp. 4498-4503
Author(s):  
J.H. Prystowsky ◽  
J.E. Smith ◽  
D.S. Goodman
Keyword(s):  
Rat Liver ◽  
Retinyl Palmitate ◽  
Hydrolase Activity ◽  
Normal Rat
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