Characterization and spray drying of lipase produced by the endophytic fungus Cercospora kikuchii

Abstract

-A lipase from the endophytic fungus Cercospora kikuchii was purified, biochemically characterized and the effects of spray drying on stabilization of the purified enzyme were studied. The lipase was purified 9.31-fold with recovery of 26.6% and specific activity of 223.6 U/mg. The optimum pH and temperature were 4.6 and 35 °C, respectively, while the Vmax was 10.28 µmol/min.mg -1 protein and Km 0.0324 mM. All the metal ions tested enhanced the enzyme activity. The lipase retained almost 100% activity in the presence of strong oxidants and was also resistant to Triton X, Tween 80 and 20 and SDS, as well as to proteases. The purified lipase was spray dried and kept until 85.2% of enzymatic activity. At least 70% of the enzymatic activity was maintained for spray dried purified lipase during the storage period. The lipase produced by Cercospora kikuchii has properties useful for industrial application and showed adequate stabilization and retention of its enzymatic activity after spray drying.

Drying of enzyme immobilized on eco-friendly supports

“…The last one is attractive for all types of enzymes, in particular lipases due to its use in organic media, bringing some industrial and economical advantages such as recovery and re-use, greater stability and continuous operation (Adlercreutz, 2013). So far, various carriers and methodologies have been used for enzyme immobilization in order to improve the properties of free enzyme (Castro et al, 2001;Freitas et al, 2010;Pereira et al, 2003;Costa-Silva et al, 2014a). Enzymes *Corresponding author.…”

New alkaline lipase from Rhizomucor variabilis: Biochemical properties and stability in the presence of microbial EPS

“…A number of studies have investigated the effects of carbohydrates on enzyme stability after the spray-drying process [45][46][47][48]. The samples of lipase from fungus Cercospora kikuchii were stored at temperatures 5, 25, and 40 • C for up to 6 months [45]. Costa-Silva et al [45] showed that the enzyme residual activity decreased with increasing temperature.…”

“…The samples of lipase from fungus Cercospora kikuchii were stored at temperatures 5, 25, and 40 • C for up to 6 months [45]. Costa-Silva et al [45] showed that the enzyme residual activity decreased with increasing temperature. After stored at temperatures 5 • C for 6 months, the purified lipase in the presence of maltose, maltodextrin, and β-cyclodextrin remains over 70% residual activity.…”

Immobilization of Candida rugosa lipase on eco-friendly supports by spouted-bed technology: Use in the synthesis of isoamyl caprylate

“…[3] Drying technologies can be utilized to obtain dehydrated and stable thermosensitive products like microbial enzymes. [4] On the other hand, enzyme immobilization are other mechanisms used to improve enzymes properties (like stability, activity, inhibition by reaction products and selectivity toward non-natural substrates), and allows recovery and reuse of the biocatalyst. [2] In this work, we associated the benefits of drying and immobilizing processes and performed them in a single step employing a spouted bed system.…”