EVALUATION OF ACTIVITY AND MASS SPECTROMETRIC CHARACTERIZATION OF TWO PARTIALLY PURIFIED THERMO-TOLE

Thermo-tolerant lipases with stability across a wide pH range and temperature, which are useful for industrial applications, were screened from fungal infections of groundnut seeds. Because DNA sequencing of the ITS 1, 5.8S, and ITS 2 sections revealed that the isolate was 99 percent identical to Aspergillus niger, it was identified as A. niger GN1 in this investigation. The pellet obtained from culture extract that had been precipitated with 65 percent ammonium sulphate was suspended in Tris-buffer and tested for lipase activity. Lipase was isolated in two fractions (1 and 2) at pH 4 and pH 9, respectively. LC-MS/MS spectroscopic analysis was used to analyse both the lipase 1 and 2 fractions. In the temperature range of 60 – 80°C and over a pH of 4 – 8 for lipase 1 and 2-6 for lipase 2 fractions, relative and residual activity of the enzyme fractions were high. Lipase 1 (32 kDa) and Lipase 2 (30 kDa) fractions having 4 and 2 distinct peptides, respectively, were validated by LC-MS/MS.

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