<span style="font-size:15.0pt;mso-bidi-font-size: 12.0pt;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:Mangal;mso-ansi-language:EN-GB;mso-fareast-language:EN-US; mso-bidi-language:HI" lang="EN-GB">A comparative study of immobilized lipase produced from <i style="mso-bidi-font-style:normal">Penicillium chrysogenum</i><span style="mso-bidi-font-style:italic"> SNP5 on two different anionic carriers for its pH and thermostability</span></span>

Abstract

The present work aimed to increase the thermostability and pH stability of lipase produced from <i>Penicillium chrysogenum </i><span style="mso-bidi-font-style:italic">SNP5<i> </i>using different anionic carriers. The immobilized lipase from the fungus on 1.25% sodium alginate beads and 12% polyacrylamide beads retained 37.28 and 59.75% immobilization efficiency, respectively, on 3 mm bead size. Immobilized lipase on calcium alginate and polyacrylamide beads retained 56.16 and 91.11% of its initial activity after 3^rd use, whereas significant loss in lipase activity was observed after 5^th and 7^th reuse, respectively. Properties like optimum pH, K_m, V_max and thermostability of immobilized lipase were changed with respect to free lipase. Optimum pH shifted from 7 to 7.5 in calcium alginate and from 7 to 9 in polyacrylamide beads, whereas t_1/2 increased from 71 min to 205 min in calcium alginate and from 71 min to 380 min in polyacrylamide beads at 45°C. K_m and V_maxvalues at free state lipase were observed as 0.30 mM and 31.948 μM min^-1 mL^-1, whereas after immobilization on calcium alginate and polyacrylamide beads values changed to 0.188 mM and 27.24 μM min^-1 mL^-1, and 0.24 mM and 30.96 μmol min^-1 mL^-1, respectively. Thus, on immobilization, lipase has shown enhanced thermostability, specificity and working range of pH, which would be more beneficial for its industrial application.

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