Dear Sir. Concerning your issue about the method for lipase identification and quantification using an RP-HPLC. The purified lipase preparation was analyzed for homogeneity by RP–HPLC under the following conditions: column Bondapack (preparative scale; 7.8x300mm); flow rate 1 mL/min; initial solution (sol A): 0.1% TFA in water, elution: linear gradient with solution B (60% acetonitrile in sol. A); total volume: 50 mL. Protein was detected at 280 nm. The lipase purification steps involved, 60% ammonium sulphate saturation, gel filtration chromatography using Sephadex G200 and ion exchange chromatography with DEAE cellulose. A purification fold of 186 was achieved following only three step purification process with specific activity of 3525.6 U/mg to apparent homogeneity as evident by a single band of 62.2kDa on sodium dodecyl sulphate polyacrylamide gel electrophoresis and reverse phase HPLC chromatogram. The purified enzyme exhibited optimum activity at temperature 60°C, pH 6.0, Km of 1.83 mM l and the Vmax of 10.0 mM l min . 1 1 1 EDTA-K almost completely inhibited the lipase activity. The enzyme had property to tolerate a wide range of organic solvents which make it attractive towards industrial applications. I think the following below links may help you in your analysis:

http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-70542006000300016

https://pdfs.semanticscholar.org/8583/33920f09208c4ae4d8c79febf194a04ea17c.pdf

http://www.iiste.org/Journals/index.php/JBAH/article/viewFile/20625/21559

http://www.sciencedirect.com/science/article/pii/S1044030507004424

Thanks

 https://academic.oup.com/chromsci/article/50/4/294/385580/High-Performance-Liquid-Chromatography