(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Viridiplantae: NE > Streptophyta: NE > Streptophytina: NE > Embryophyta: NE > Tracheophyta: NE > Euphyllophyta: NE > Spermatophyta: NE > Magnoliophyta: NE > Mesangiospermae: NE > Liliopsida: NE > Petrosaviidae: NE > commelinids: NE > Arecales: NE > Arecaceae: NE > Arecoideae: NE > Cocoseae: NE > Elaeidinae: NE > Elaeis: NE > Elaeis guineensis: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acid identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Elaeis guineensis var. tenera: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MPPIGTATSAPARHVSPSRSSLPPRHGSPLNPHSPPRTLKPTPVSAASSS SIATKIHLSNLDRVLVKHPSSQTPQHTHDVGRDDDPPKPDHLGGATAAGG GGGVGLLHALNLPSLFPFLRKPAAEEMSPRSLTHLQRLLSDSPRPSPKSS IASKWRLYHGAEDWSGLLDPLDENLRRELLRYGDFVQAAYHAFHSRPAAS SPARHHHLLLPDRSYRPTKSLFATSSLSIPPWTHSSASNWRTQSSSWIGY VAVSDSDREIRRMGRREIVVVLRGTATCLEWAENLRASLVPMDSPDDSSG EVRQHVPKVARGFWSLYKTAGEQVSSLSASVVEEVRRLMELYKGEELSIT VTGHSLGAALAILVADELSTCAPNVPPIAVVSFGGPRVGNRAFADRVEKE HGVKVLRIVNAHDVITKVPAGMPLPHVREGYEHVGSELRINSRDSPYLRP DAGPACSHDLEAYLHLVDGFTGTGSPFRSNAKRSLVRLLDQQRRSVKEVY VNRARALGVDPTAAVPLSSPHGCLASPS
Reference
Title: Heterologous Expression and Characterization of Plant Lipase LIP2 from Elaeis guineensis Jacq. Oil Palm Mesocarp in Escherichia coli Mohd Din MH, Nair A, Masomian M, Ali MSM, Rahman RNZRA Ref: Catalysts, 11:244, 2021 : PubMed
In order to determine the potential of biochemical and structural features of Elaeis guineensis Jacq. oil palm mesocarp lipases, the LIP2 gene was isolated, expressed, purified and characterized through the Escherichia coli microbial recombinant system. Gene analysis of LIP2 revealed that it is composed of 1584 base pairs which are encoded in 528 amino acid residues with a molecular weight of around 57 kDa. LIP2 has distinctive lipolytic properties in terms of alpha/beta fold and the catalytic triad for lipase. The LIP2 lipase was successfully expressed and purified from E. coli Rosetta (DE3) via affinity chromatography. The optimal temperature and pH for the lipase activity was 30 degC and a pH of 9, respectively. Stability was profoundly increased with the addition of metal ions (Ca2+, Mg2+, Mn+, and Ni+), along with organic solvents (ethanol and octanol). pNP myristate was the most suitable among all pNP esters. In biophysical characterization analysis, LIP2 has a thermal denaturing point at 66 degC, which mostly consists of random patterns (39.8%) followed by alpha-helix (30.3%), turns (23.8%) and beta-sheet (6.2%). From the successful purification and characterization, the potential of oil palm mesocarp lipase was able to be further explored.
